5T0C

Structural basis for dynamic regulation of the human 26S proteasome


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
T [auth AH]SCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
ZA [auth BH]SCOP2B SuperfamilyClass II glutamine amidotransferases8064014 3000131 SCOP2B (2022-06-29)
AB [auth BI]SCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
U [auth AI]SCOP2B SuperfamilyClass II glutamine amidotransferases8064036 3000131 SCOP2B (2022-06-29)
BB [auth BJ]SCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
V [auth AJ]SCOP2B SuperfamilyClass II glutamine amidotransferases8064004 3000131 SCOP2B (2022-06-29)
CB [auth BK]SCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)
W [auth AK]SCOP2B SuperfamilyClass II glutamine amidotransferases8064022 3000131 SCOP2B (2022-06-29)
DB [auth BL]SCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
X [auth AL]SCOP2B SuperfamilyClass II glutamine amidotransferases8064060 3000131 SCOP2B (2022-06-29)
EB [auth BM]SCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
Y [auth AM]SCOP2B SuperfamilyClass II glutamine amidotransferases8064054 3000131 SCOP2B (2022-06-29)
FB [auth BN]SCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
Z [auth AN]SCOP2B SuperfamilyClass II glutamine amidotransferases8079175 3000131 SCOP2B (2022-06-29)
AA [auth AO]SCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
GB [auth BO]SCOP2B SuperfamilyClass II glutamine amidotransferases8064074 3000131 SCOP2B (2022-06-29)
DA [auth AR]SCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)
JB [auth BR]SCOP2B SuperfamilyClass II glutamine amidotransferases8079492 3000131 SCOP2B (2022-06-29)
D [auth AX]SCOP2B SuperfamilyWinged helix DNA-binding domain8067905 3000034 SCOP2B (2022-06-29)
JA [auth BX]SCOP2B SuperfamilyWinged helix DNA-binding domain8067905 3000034 SCOP2B (2022-06-29)
E [auth AY]SCOP2B SuperfamilyTPR-like8057045 3001345 SCOP2B (2022-06-29)
E [auth AY]SCOP2B SuperfamilyWinged helix DNA-binding domain8057047 3000034 SCOP2B (2022-06-29)
KA [auth BY]SCOP2B SuperfamilyWinged helix DNA-binding domain8057047 3000034 SCOP2B (2022-06-29)
KA [auth BY]SCOP2B SuperfamilyTPR-like8057045 3001345 SCOP2B (2022-06-29)
F [auth AZ]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053251 3002167 SCOP2B (2022-06-29)
F [auth AZ]SCOP2B SuperfamilyJAB1/MPN domain-like8053252 3001105 SCOP2B (2022-06-29)
LA [auth BZ]SCOP2B SuperfamilyJAB1/MPN domain-like8053252 3001105 SCOP2B (2022-06-29)
LA [auth BZ]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053251 3002167 SCOP2B (2022-06-29)
I [auth Ac]SCOP2B SuperfamilyJAB1/MPN domain-like8053255 3001105 SCOP2B (2022-06-29)
I [auth Ac]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053254 3002167 SCOP2B (2022-06-29)
OA [auth Bc]SCOP2B SuperfamilyEIF3 subunit F C-terminal domain-like8053254 3002167 SCOP2B (2022-06-29)
OA [auth Bc]SCOP2B SuperfamilyJAB1/MPN domain-like8053255 3001105 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth AU]PF18004e5t0cAU3 A: beta sandwichesX: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)H: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 C-terminal domainF: PF18004ECOD (1.6)
A [auth AU]PF21505e5t0cAU1 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF21505ECOD (1.6)
A [auth AU]PF01851e5t0cAU2 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
GA [auth BU]PF18004e5t0cBU1 A: beta sandwichesX: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)H: 26S proteasome subunit Rpn2 C-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 C-terminal domainF: PF18004ECOD (1.6)
GA [auth BU]PF21505e5t0cBU2 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF21505ECOD (1.6)
GA [auth BU]PF01851e5t0cBU3 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
J [auth Ad]PF10075e5t0cAd1 A: alpha arraysX: HTHH: HTHT: wingedF: PF10075ECOD (1.6)
J [auth Ad]PF10075e5t0cAd2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10075ECOD (1.6)
PA [auth Bd]PF10075e5t0cBd1 A: alpha arraysX: HTHH: HTHT: wingedF: PF10075ECOD (1.6)
PA [auth Bd]PF10075e5t0cBd2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10075ECOD (1.6)
L [auth Af]PF17781e5t0cAf2 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF17781ECOD (1.6)
L [auth Af]PF01851e5t0cAf3 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
RA [auth Bf]PF17781e5t0cBf2 A: alpha superhelicesX: Repetitive alpha hairpinsH: 26S proteasome subunit Rpn2 N-terminal domain (From Topology)T: 26S proteasome subunit Rpn2 N-terminal domainF: PF17781ECOD (1.6)
RA [auth Bf]PF01851e5t0cBf3 A: alpha superhelicesX: Repetitive alpha hairpinsH: Proteasome/cyclosome (PC) repeat (From Topology)T: Proteasome/cyclosome (PC) repeatF: PF01851ECOD (1.6)
M [auth AA]PF17862e5t0cAA1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
M [auth AA]PF00004e5t0cAA3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
SA [auth BA]PF17862e5t0cBA2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
SA [auth BA]PF00004e5t0cBA1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
N [auth AB]PF16450e5t0cAB2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
N [auth AB]PF17862e5t0cAB1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
N [auth AB]PF00004e5t0cAB3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
TA [auth BB]PF16450e5t0cBB1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
TA [auth BB]PF17862e5t0cBB3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
TA [auth BB]PF00004e5t0cBB2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
O [auth AD]PF16450e5t0cAD3 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
O [auth AD]PF17862e5t0cAD2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
O [auth AD]PF00004e5t0cAD1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
UA [auth BD]PF16450e5t0cBD2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
UA [auth BD]PF17862e5t0cBD1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
UA [auth BD]PF00004e5t0cBD3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
P [auth AE]PF16450e5t0cAE3 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
P [auth AE]PF17862e5t0cAE1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
P [auth AE]PF00004e5t0cAE2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
VA [auth BE]PF16450e5t0cBE2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
VA [auth BE]PF17862e5t0cBE3 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
VA [auth BE]PF00004e5t0cBE1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
Q [auth AF]PF16450e5t0cAF3 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
Q [auth AF]F_UNCLASSIFIEDe5t0cAF4 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: F_UNCLASSIFIEDECOD (1.6)
Q [auth AF]PF17862e5t0cAF2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
Q [auth AF]PF00004e5t0cAF1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
WA [auth BF]PF16450e5t0cBF3 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
WA [auth BF]F_UNCLASSIFIEDe5t0cBF4 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: F_UNCLASSIFIEDECOD (1.6)
WA [auth BF]PF17862e5t0cBF2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
WA [auth BF]PF00004e5t0cBF1 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
R [auth AC]PF16450e5t0cAC2 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
R [auth AC]PF17862e5t0cAC1 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
R [auth AC]PF00004e5t0cAC3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
XA [auth BC]PF16450e5t0cBC1 A: beta barrelsX: OB-foldH: Nucleic acid-binding proteins (From Topology)T: Nucleic acid-binding proteinsF: PF16450ECOD (1.6)
XA [auth BC]PF17862e5t0cBC2 A: alpha arraysX: Histone-likeH: Histone-relatedT: AAA+ ATPase lid domainF: PF17862ECOD (1.6)
XA [auth BC]PF00004e5t0cBC3 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF00004ECOD (1.6)
S [auth AG]PF00227,PF10584e5t0cAG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
YA [auth BG]PF00227,PF10584e5t0cBG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
B [auth AV]PF01399e5t0cAV1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
B [auth AV]F_UNCLASSIFIEDe5t0cAV3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
B [auth AV]PF08375e5t0cAV2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN3 C-terminal helixF: PF08375ECOD (1.6)
HA [auth BV]PF01399e5t0cBV3 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
HA [auth BV]F_UNCLASSIFIEDe5t0cBV1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: F_UNCLASSIFIEDECOD (1.6)
HA [auth BV]PF08375e5t0cBV2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN3 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN3 C-terminal helixF: PF08375ECOD (1.6)
T [auth AH]PF00227,PF10584e5t0cAH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
ZA [auth BH]PF00227,PF10584e5t0cBH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
AB [auth BI]PF00227,PF10584e5t0cBI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
U [auth AI]PF00227,PF10584e5t0cAI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
BB [auth BJ]PF00227,PF10584e5t0cBJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
V [auth AJ]PF00227,PF10584e5t0cAJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
CB [auth BK]PF00227,PF10584e5t0cBK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
W [auth AK]PF00227,PF10584e5t0cAK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
DB [auth BL]PF00227,PF10584e5t0cBL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
X [auth AL]PF00227,PF10584e5t0cAL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
EB [auth BM]PF00227,PF10584e5t0cBM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
Y [auth AM]PF00227,PF10584e5t0cAM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF10584ECOD (1.6)
FB [auth BN]PF00227e5t0cBN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
Z [auth AN]PF00227e5t0cAN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
AA [auth AO]PF00227,PF12465e5t0cAO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)
GB [auth BO]PF00227,PF12465e5t0cBO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227,PF12465ECOD (1.6)
BA [auth AP]PF00227e5t0cAP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
HB [auth BP]PF00227e5t0cBP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
CA [auth AQ]PF00227e5t0cAQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
IB [auth BQ]PF00227e5t0cBQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
C [auth AW]PF01399e5t0cAW1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
C [auth AW]PF22241e5t0cAW2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22241ECOD (1.6)
C [auth AW]PF18098e5t0cAW3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN5 C-terminal helixF: PF18098ECOD (1.6)
IA [auth BW]PF01399e5t0cBW1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
IA [auth BW]PF22241e5t0cBW3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22241ECOD (1.6)
IA [auth BW]PF18098e5t0cBW2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN5 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN5 C-terminal helixF: PF18098ECOD (1.6)
DA [auth AR]PF00227e5t0cAR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
JB [auth BR]PF00227e5t0cBR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
EA [auth AS]PF00227e5t0cAS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
KB [auth BS]PF00227e5t0cBS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
FA [auth AT]PF00227e5t0cAT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
LB [auth BT]PF00227e5t0cBT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: PF00227ECOD (1.6)
D [auth AX]PF01399e5t0cAX1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
D [auth AX]PF18055e5t0cAX3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF18055ECOD (1.6)
D [auth AX]PF18503e5t0cAX2 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN6 C-termial helix (From Topology)T: 26S proteasome regulatory subunit RPN6 C-termial helixF: PF18503ECOD (1.6)
JA [auth BX]PF01399e5t0cBX1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
JA [auth BX]PF18055e5t0cBX2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF18055ECOD (1.6)
JA [auth BX]PF18503e5t0cBX3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN6 C-termial helix (From Topology)T: 26S proteasome regulatory subunit RPN6 C-termial helixF: PF18503ECOD (1.6)
E [auth AY]PF01399e5t0cAY1 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
E [auth AY]PF10602e5t0cAY2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10602ECOD (1.6)
E [auth AY]PF21154e5t0cAY3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN7 C-terminal helixF: PF21154ECOD (1.6)
KA [auth BY]PF01399e5t0cBY2 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
KA [auth BY]PF10602e5t0cBY3 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF10602ECOD (1.6)
KA [auth BY]PF21154e5t0cBY1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN7 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN7 C-terminal helixF: PF21154ECOD (1.6)
F [auth AZ]PF01398e5t0cAZ2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
F [auth AZ]PF13012e5t0cAZ1 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: PF13012ECOD (1.6)
LA [auth BZ]PF01398e5t0cBZ1 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
LA [auth BZ]PF13012e5t0cBZ2 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: PF13012ECOD (1.6)
G [auth Aa]PF01399e5t0cAa3 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
G [auth Aa]PF22037e5t0cAa2 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22037ECOD (1.6)
G [auth Aa]F_UNCLASSIFIEDe5t0cAa1 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN9 C-terminal helixF: F_UNCLASSIFIEDECOD (1.6)
MA [auth Ba]PF01399e5t0cBa2 A: alpha arraysX: HTHH: HTHT: wingedF: PF01399ECOD (1.6)
MA [auth Ba]PF22037e5t0cBa1 A: alpha superhelicesX: Repetitive alpha hairpinsH: ARM repeat (From Topology)T: ARM repeatF: PF22037ECOD (1.6)
MA [auth Ba]F_UNCLASSIFIEDe5t0cBa3 A: extended segmentsX: 26S proteasome regulatory subunits C-terminal helicesH: 26S proteasome regulatory subunit RPN9 C-terminal helix (From Topology)T: 26S proteasome regulatory subunit RPN9 C-terminal helixF: F_UNCLASSIFIEDECOD (1.6)
H [auth Ab]PF13519e5t0cAb1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: vWA-likeF: PF13519ECOD (1.6)
NA [auth Bb]PF13519e5t0cBb1 A: a/b three-layered sandwichesX: HAD domain-likeH: HAD domain-relatedT: vWA-likeF: PF13519ECOD (1.6)
I [auth Ac]PF01398e5t0cAc2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
I [auth Ac]F_UNCLASSIFIEDe5t0cAc1 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: F_UNCLASSIFIEDECOD (1.6)
OA [auth Bc]PF01398e5t0cBc2 A: a+b three layersX: Cytidine deaminase-like (From Topology)H: Cytidine deaminase-like (From Topology)T: Cytidine deaminase-likeF: PF01398ECOD (1.6)
OA [auth Bc]F_UNCLASSIFIEDe5t0cBc1 A: extended segmentsX: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)H: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domain (From Topology)T: 26S proteasome regulatory subunit RPN8/RPN11 C-terminal domainF: F_UNCLASSIFIEDECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth AU],
GA [auth BU]
PF13646HEAT repeats (HEAT_2)HEAT repeats- Repeat
A [auth AU],
GA [auth BU]
PF1800426S proteasome regulatory subunit RPN2 C-terminal domain (RPN2_C)26S proteasome regulatory subunit RPN2 C-terminal domainThis is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating inter ...This is the C-terminal domain found in S. cerevisiae Rpn2 (26S proteasome regulatory subunit RPN2) as well as other eukaryotic species. A study revealed that the C-terminal 52 residues of the Rpn2 C-terminal domain are responsible for mediating interactions with the ubiquitin-binding subunit Rpn13. Futhermore, the extreme C-terminal 20 or 21 residues of Rpn2 (926-945 or 925-945) of S. cerevisiae, were shown to be equally effective at binding Rpn13. Multiple sequence alignments indicate that Rpn2 orthologs are highly conserved in this C-terminal region and share characteristic acidic, aromatic, and proline residues, suggesting a common function. In the structure of Rpn2 from S. cerevisiae , this region is exposed and disordered, and is thus accessible for associating with Rpn13. The Rpn2 binding surface of human Rpn13 has been mapped by nuclear magnetic resonance titration to one surface of its Pru domain [1].
Domain
A [auth AU],
GA [auth BU]
PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
J [auth Ad],
PA [auth Bd]
PF10075CSN8/PSMD8/EIF3K family (CSN8_PSD8_EIF3K)CSN8/PSMD8/EIF3K family- Family
K [auth Ae],
QA [auth Be]
PF05160DSS1/SEM1 family (DSS1_SEM1)DSS1/SEM1 family- Family
L [auth Af],
RA [auth Bf]
PF01851Proteasome/cyclosome repeat (PC_rep)Proteasome/cyclosome repeat- Repeat
L [auth Af],
RA [auth Bf]
PF1805126S proteasome non-ATPase regulatory subunit RPN1 C-terminal (RPN1_C)26S proteasome non-ATPase regulatory subunit RPN1 C-terminalThis is the C-terminal domain found in RPN1 proteins (26S proteasome non-ATPase regulatory subunit 2). The 26S proteasome holocomplex consists of a 28-subunit barrel-shaped core particle (CP) in the center capped at the top and bottom by 19-subunit ...This is the C-terminal domain found in RPN1 proteins (26S proteasome non-ATPase regulatory subunit 2). The 26S proteasome holocomplex consists of a 28-subunit barrel-shaped core particle (CP) in the center capped at the top and bottom by 19-subunit regulatory particles (RPs). The CP forms the catalytic chamber and the RP is formed from two subcomplexes known as the lid and the base [1]. The lid comprises nine Rpn subunits in yeast (Rpn3/5/6/7/8/9/11/12/15) and the base comprises three Rpn subunits (Rpn1/2/13) and six ATPases (Rpt1-6) [2].
Domain
M [auth AA],
SA [auth BA]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
M [auth AA],
SA [auth BA]
PF2123626S proteasome regulatory subunit 7, OB domain (PRS7_OB)26S proteasome regulatory subunit 7, OB domainThis is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This doma ...This is the OB domain from 26S proteasome regulatory subunit 7 (PRS7, also known as PSMC2, Rpt1 or MSS1), a component of the 19S proteasome cap [1-5]. These are one of six ATPases of the regulatory particle that form a heterohexameric ring. This domain mediates interactions with USP14 or Ubp6 [2,4].
Domain
M [auth AA],
SA [auth BA]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
N [auth AB],
TA [auth BB]
PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
N [auth AB],
TA [auth BB]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
N [auth AB],
TA [auth BB]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
O [auth AD],
UA [auth BD]
PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
O [auth AD],
UA [auth BD]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
O [auth AD],
UA [auth BD]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
P [auth AE],
VA [auth BE]
PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
P [auth AE],
VA [auth BE]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
P [auth AE],
VA [auth BE]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
Q [auth AF],
WA [auth BF]
PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
Q [auth AF],
WA [auth BF]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
Q [auth AF],
WA [auth BF]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
R [auth AC],
XA [auth BC]
PF16450Proteasomal ATPase OB C-terminal domain (Prot_ATP_ID_OB_C)Proteasomal ATPase OB C-terminal domainThis is the C-terminal interdomain (ID) or oligonucleotide binding (OB) domain of proteasomal ATPase [1-2]Domain
R [auth AC],
XA [auth BC]
PF17862AAA+ lid domain (AAA_lid_3)AAA+ lid domainThis entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.Domain
R [auth AC],
XA [auth BC]
PF00004ATPase family associated with various cellular activities (AAA) (AAA)ATPase family associated with various cellular activities (AAA)AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes [2].Domain
S [auth AG],
YA [auth BG]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
S [auth AG],
YA [auth BG]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
B [auth AV],
HA [auth BV]
PF08375Proteasome regulatory subunit C-terminal (Rpn3_C)Proteasome regulatory subunit C-terminal- Family
B [auth AV],
HA [auth BV]
PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
T [auth AH],
ZA [auth BH]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
T [auth AH],
ZA [auth BH]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
AB [auth BI],
U [auth AI]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
AB [auth BI],
U [auth AI]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
BB [auth BJ],
V [auth AJ]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
BB [auth BJ],
V [auth AJ]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
CB [auth BK],
W [auth AK]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
CB [auth BK],
W [auth AK]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
DB [auth BL],
X [auth AL]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
DB [auth BL],
X [auth AL]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
EB [auth BM],
Y [auth AM]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
EB [auth BM],
Y [auth AM]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
FB [auth BN],
Z [auth AN]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
AA [auth AO],
GB [auth BO]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
AA [auth AO],
GB [auth BO]
PF12465Proteasome beta subunits C terminal (Pr_beta_C)Proteasome beta subunits C terminal- Family
BA [auth AP],
HB [auth BP]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
CA [auth AQ],
IB [auth BQ]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
C [auth AW],
IA [auth BW]
PF1809826S proteasome regulatory subunit RPN5 C-terminal domain (RPN5_C)26S proteasome regulatory subunit RPN5 C-terminal domainThis is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degrada ...This is the C-terminal domain of the 26S proteasome regulatory subunit RPN5 proteins.This helical domain can be found adjacent to Pfam:PF01399. The 26S proteasome is the major ATP-dependent protease in eukaryotes. Three subcomplexes form this degradation machine: the lid, the base, and the core. The helices found at the C terminus of each lid subunit form a helical bundle that directs the ordered self-assembly of the lid subcomplex. This domain which comprises the tail of RPN5 along with the tail of Rpn9, are important for Rpn12 binding to the lid [1].
Domain
C [auth AW],
IA [auth BW]
PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
DA [auth AR],
JB [auth BR]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
EA [auth AS],
KB [auth BS]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
FA [auth AT],
LB [auth BT]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
D [auth AX],
JA [auth BX]
PF1805526S proteasome regulatory subunit RPN6 N-terminal domain (RPN6_N)26S proteasome regulatory subunit RPN6 N-terminal domain- Repeat
D [auth AX],
JA [auth BX]
PF1850326S proteasome subunit RPN6 C-terminal helix domain (RPN6_C_helix)26S proteasome subunit RPN6 C-terminal helix domainThis is the C-terminal helix domain found in RPN6, a component of the 26S proteasome. The C-terminal helices are essential for lid assembly [1, 2].Domain
D [auth AX],
JA [auth BX]
PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
E [auth AY],
KA [auth BY]
PF2115426S proteasome regulatory subunit RPN7/PSMD6 C-terminal helix (RPN7_PSMD6_C)26S proteasome regulatory subunit RPN7/PSMD6 C-terminal helixRPN7/PSDM6 are regulatory subunits from the 26S proteasome. This entry represents the C-terminal helix.Domain
E [auth AY],
KA [auth BY]
PF1060226S proteasome subunit RPN7 (RPN7)26S proteasome subunit RPN7- Repeat
E [auth AY],
KA [auth BY]
PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
F [auth AZ],
LA [auth BZ]
PF13012Maintenance of mitochondrial structure and function (MitMem_reg)Maintenance of mitochondrial structure and function- Family
F [auth AZ],
LA [auth BZ]
PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family
G [auth Aa],
MA [auth Ba]
PF01399PCI domain (PCI)PCI domainThis domain has also been called the PINT motif (Proteasome, Int-6, Nip-1 and TRIP-15) [1].Domain
H [auth Ab],
NA [auth Bb]
PF13519von Willebrand factor type A domain (VWA_2)von Willebrand factor type A domain- Domain
I [auth Ac],
OA [auth Bc]
PF01398JAB1/Mov34/MPN/PAD-1 ubiquitin protease (JAB)JAB1/Mov34/MPN/PAD-1 ubiquitin protease- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth AU],
GA [auth BU]
26S proteasome non-ATPase regulatory subunit 1
J [auth Ad],
PA [auth Bd]
26S proteasome non-ATPase regulatory subunit 8-
K [auth Ae],
QA [auth Be]
26S proteasome complex subunit DSS1-
L [auth Af],
RA [auth Bf]
26S proteasome non-ATPase regulatory subunit 2
M [auth AA],
SA [auth BA]
26S protease regulatory subunit 7
N [auth AB],
TA [auth BB]
26S protease regulatory subunit 4
O [auth AD],
UA [auth BD]
26S protease regulatory subunit 6B
P [auth AE],
VA [auth BE]
26S protease regulatory subunit 10B
Q [auth AF],
WA [auth BF]
26S protease regulatory subunit 6A
R [auth AC],
XA [auth BC]
26S protease regulatory subunit 8
S [auth AG],
YA [auth BG]
Proteasome subunit alpha type-6
B [auth AV],
HA [auth BV]
26S proteasome non-ATPase regulatory subunit 3
T [auth AH],
ZA [auth BH]
Proteasome subunit alpha type-2-
AB [auth BI],
U [auth AI]
Proteasome subunit alpha type-4-
BB [auth BJ],
V [auth AJ]
Proteasome subunit alpha type-7
CB [auth BK],
W [auth AK]
Proteasome subunit alpha type-5-
DB [auth BL],
X [auth AL]
Proteasome subunit alpha type-1
EB [auth BM],
Y [auth AM]
Proteasome subunit alpha type-3
FB [auth BN],
Z [auth AN]
Proteasome subunit beta type-6
AA [auth AO],
GB [auth BO]
Proteasome subunit beta type-7
BA [auth AP],
HB [auth BP]
Proteasome subunit beta type-3-
CA [auth AQ],
IB [auth BQ]
Proteasome subunit beta type-2-
C [auth AW],
IA [auth BW]
26S proteasome non-ATPase regulatory subunit 12-
DA [auth AR],
JB [auth BR]
Proteasome subunit beta type-5
EA [auth AS],
KB [auth BS]
Proteasome subunit beta type-1-
FA [auth AT],
LB [auth BT]
Proteasome subunit beta type-4
D [auth AX],
JA [auth BX]
26S proteasome non-ATPase regulatory subunit 11
E [auth AY],
KA [auth BY]
26S proteasome non-ATPase regulatory subunit 6-
F [auth AZ],
LA [auth BZ]
26S proteasome non-ATPase regulatory subunit 7
G [auth Aa],
MA [auth Ba]
26S proteasome non-ATPase regulatory subunit 13
H [auth Ab],
NA [auth Bb]
26S proteasome non-ATPase regulatory subunit 4
I [auth Ac],
OA [auth Bc]
26S proteasome non-ATPase regulatory subunit 14

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A [auth AU],
GA [auth BU]
IPR04062326S proteasome regulatory subunit RPN2, C-terminalDomain
A [auth AU],
GA [auth BU]
IPR016024Armadillo-type foldHomologous Superfamily
A [auth AU],
GA [auth BU]
IPR002015Proteasome/cyclosome repeatRepeat
A [auth AU],
GA [auth BU]
IPR011989Armadillo-like helicalHomologous Superfamily
A [auth AU],
GA [auth BU]
IPR04857026S proteasome non-ATPase regulatory subunit 1/RPN2, N-terminal domainDomain
A [auth AU],
GA [auth BU]
IPR01664226S proteasome regulatory complex, non-ATPase subcomplex, Rpn2/Psmd1 subunitFamily
J [auth Ad],
PA [auth Bd]
IPR000717Proteasome component (PCI) domainDomain
J [auth Ad],
PA [auth Bd]
IPR00674626S proteasome non-ATPase regulatory subunit Rpn12Family
J [auth Ad],
PA [auth Bd]
IPR033464CSN8/PSMD8/EIF3KDomain
K [auth Ae],
QA [auth Be]
IPR007834DSS1/SEM1Family
L [auth Af],
RA [auth Bf]
IPR04143326S proteasome non-ATPase regulatory subunit RPN1, C-terminalDomain
L [auth Af],
RA [auth Bf]
IPR016024Armadillo-type foldHomologous Superfamily
L [auth Af],
RA [auth Bf]
IPR002015Proteasome/cyclosome repeatRepeat
L [auth Af],
RA [auth Bf]
IPR01664326S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 subunitFamily
L [auth Af],
RA [auth Bf]
IPR011989Armadillo-like helicalHomologous Superfamily
L [auth Af],
RA [auth Bf]
IPR040892RPN1, N-terminalDomain
M [auth AA],
SA [auth BA]
IPR003593AAA+ ATPase domainDomain
M [auth AA],
SA [auth BA]
IPR003959ATPase, AAA-type, coreDomain
M [auth AA],
SA [auth BA]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
M [auth AA],
SA [auth BA]
IPR04872326S proteasome regulatory subunit 7-like, OB domainDomain
M [auth AA],
SA [auth BA]
IPR041569AAA ATPase, AAA+ lid domainDomain
M [auth AA],
SA [auth BA]
IPR003960ATPase, AAA-type, conserved siteConserved Site
M [auth AA],
SA [auth BA]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
N [auth AB],
TA [auth BB]
IPR041569AAA ATPase, AAA+ lid domainDomain
N [auth AB],
TA [auth BB]
IPR032501Proteasomal ATPase, second OB domainDomain
N [auth AB],
TA [auth BB]
IPR003960ATPase, AAA-type, conserved siteConserved Site
N [auth AB],
TA [auth BB]
IPR003593AAA+ ATPase domainDomain
N [auth AB],
TA [auth BB]
IPR003959ATPase, AAA-type, coreDomain
N [auth AB],
TA [auth BB]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
N [auth AB],
TA [auth BB]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
O [auth AD],
UA [auth BD]
IPR041569AAA ATPase, AAA+ lid domainDomain
O [auth AD],
UA [auth BD]
IPR032501Proteasomal ATPase, second OB domainDomain
O [auth AD],
UA [auth BD]
IPR003960ATPase, AAA-type, conserved siteConserved Site
O [auth AD],
UA [auth BD]
IPR003593AAA+ ATPase domainDomain
O [auth AD],
UA [auth BD]
IPR003959ATPase, AAA-type, coreDomain
O [auth AD],
UA [auth BD]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
O [auth AD],
UA [auth BD]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
P [auth AE],
VA [auth BE]
IPR003593AAA+ ATPase domainDomain
P [auth AE],
VA [auth BE]
IPR003959ATPase, AAA-type, coreDomain
P [auth AE],
VA [auth BE]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
P [auth AE],
VA [auth BE]
IPR041569AAA ATPase, AAA+ lid domainDomain
P [auth AE],
VA [auth BE]
IPR032501Proteasomal ATPase, second OB domainDomain
P [auth AE],
VA [auth BE]
IPR003960ATPase, AAA-type, conserved siteConserved Site
P [auth AE],
VA [auth BE]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
Q [auth AF],
WA [auth BF]
IPR003593AAA+ ATPase domainDomain
Q [auth AF],
WA [auth BF]
IPR003959ATPase, AAA-type, coreDomain
Q [auth AF],
WA [auth BF]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
Q [auth AF],
WA [auth BF]
IPR041569AAA ATPase, AAA+ lid domainDomain
Q [auth AF],
WA [auth BF]
IPR032501Proteasomal ATPase, second OB domainDomain
Q [auth AF],
WA [auth BF]
IPR003960ATPase, AAA-type, conserved siteConserved Site
Q [auth AF],
WA [auth BF]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
R [auth AC],
XA [auth BC]
IPR003593AAA+ ATPase domainDomain
R [auth AC],
XA [auth BC]
IPR003959ATPase, AAA-type, coreDomain
R [auth AC],
XA [auth BC]
IPR027417P-loop containing nucleoside triphosphate hydrolaseHomologous Superfamily
R [auth AC],
XA [auth BC]
IPR041569AAA ATPase, AAA+ lid domainDomain
R [auth AC],
XA [auth BC]
IPR032501Proteasomal ATPase, second OB domainDomain
R [auth AC],
XA [auth BC]
IPR003960ATPase, AAA-type, conserved siteConserved Site
R [auth AC],
XA [auth BC]
IPR012340Nucleic acid-binding, OB-foldHomologous Superfamily
S [auth AG],
YA [auth BG]
IPR034642Proteasome subunit alpha6Family
S [auth AG],
YA [auth BG]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
S [auth AG],
YA [auth BG]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
S [auth AG],
YA [auth BG]
IPR023332Proteasome alpha-type subunitFamily
S [auth AG],
YA [auth BG]
IPR001353Proteasome, subunit alpha/betaFamily
B [auth AV],
HA [auth BV]
IPR01358626S proteasome regulatory subunit, C-terminalDomain
B [auth AV],
HA [auth BV]
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
B [auth AV],
HA [auth BV]
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
B [auth AV],
HA [auth BV]
IPR000717Proteasome component (PCI) domainDomain
T [auth AH],
ZA [auth BH]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
T [auth AH],
ZA [auth BH]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
T [auth AH],
ZA [auth BH]
IPR023332Proteasome alpha-type subunitFamily
T [auth AH],
ZA [auth BH]
IPR001353Proteasome, subunit alpha/betaFamily
AB [auth BI],
U [auth AI]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AB [auth BI],
U [auth AI]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AB [auth BI],
U [auth AI]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
AB [auth BI],
U [auth AI]
IPR023332Proteasome alpha-type subunitFamily
AB [auth BI],
U [auth AI]
IPR001353Proteasome, subunit alpha/betaFamily
BB [auth BJ],
V [auth AJ]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BB [auth BJ],
V [auth AJ]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
BB [auth BJ],
V [auth AJ]
IPR023332Proteasome alpha-type subunitFamily
BB [auth BJ],
V [auth AJ]
IPR001353Proteasome, subunit alpha/betaFamily
CB [auth BK],
W [auth AK]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
CB [auth BK],
W [auth AK]
IPR033812Proteasome subunit alpha5Family
CB [auth BK],
W [auth AK]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
CB [auth BK],
W [auth AK]
IPR023332Proteasome alpha-type subunitFamily
CB [auth BK],
W [auth AK]
IPR001353Proteasome, subunit alpha/betaFamily
DB [auth BL],
X [auth AL]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
DB [auth BL],
X [auth AL]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
DB [auth BL],
X [auth AL]
IPR035144Proteasome subunit alpha 1Family
DB [auth BL],
X [auth AL]
IPR023332Proteasome alpha-type subunitFamily
DB [auth BL],
X [auth AL]
IPR001353Proteasome, subunit alpha/betaFamily
EB [auth BM],
Y [auth AM]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
EB [auth BM],
Y [auth AM]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
EB [auth BM],
Y [auth AM]
IPR023332Proteasome alpha-type subunitFamily
EB [auth BM],
Y [auth AM]
IPR001353Proteasome, subunit alpha/betaFamily
FB [auth BN],
Z [auth AN]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
FB [auth BN],
Z [auth AN]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
FB [auth BN],
Z [auth AN]
IPR023333Proteasome B-type subunitFamily
FB [auth BN],
Z [auth AN]
IPR001353Proteasome, subunit alpha/betaFamily
FB [auth BN],
Z [auth AN]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
AA [auth AO],
GB [auth BO]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
AA [auth AO],
GB [auth BO]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth AO],
GB [auth BO]
IPR024689Proteasome beta subunit, C-terminalDomain
AA [auth AO],
GB [auth BO]
IPR023333Proteasome B-type subunitFamily
AA [auth AO],
GB [auth BO]
IPR001353Proteasome, subunit alpha/betaFamily
AA [auth AO],
GB [auth BO]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
BA [auth AP],
HB [auth BP]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
BA [auth AP],
HB [auth BP]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth AP],
HB [auth BP]
IPR023333Proteasome B-type subunitFamily
BA [auth AP],
HB [auth BP]
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth AP],
HB [auth BP]
IPR033811Proteasome beta 3 subunitFamily
CA [auth AQ],
IB [auth BQ]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
CA [auth AQ],
IB [auth BQ]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
CA [auth AQ],
IB [auth BQ]
IPR023333Proteasome B-type subunitFamily
CA [auth AQ],
IB [auth BQ]
IPR001353Proteasome, subunit alpha/betaFamily
CA [auth AQ],
IB [auth BQ]
IPR035206Proteasome subunit beta 2Family
C [auth AW],
IA [auth BW]
IPR036388Winged helix-like DNA-binding domain superfamilyHomologous Superfamily
C [auth AW],
IA [auth BW]
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
C [auth AW],
IA [auth BW]
IPR000717Proteasome component (PCI) domainDomain
C [auth AW],
IA [auth BW]
IPR04089626S proteasome regulatory subunit RPN5, C-terminal domainDomain
C [auth AW],
IA [auth BW]
IPR04013426S Proteasome non-ATPase regulatory subunit 12/COP9 signalosome complex subunit 4Family
DA [auth AR],
JB [auth BR]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
DA [auth AR],
JB [auth BR]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
DA [auth AR],
JB [auth BR]
IPR023333Proteasome B-type subunitFamily
DA [auth AR],
JB [auth BR]
IPR001353Proteasome, subunit alpha/betaFamily
DA [auth AR],
JB [auth BR]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
EA [auth AS],
KB [auth BS]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
EA [auth AS],
KB [auth BS]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
EA [auth AS],
KB [auth BS]
IPR023333Proteasome B-type subunitFamily
EA [auth AS],
KB [auth BS]
IPR001353Proteasome, subunit alpha/betaFamily
FA [auth AT],
LB [auth BT]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
FA [auth AT],
LB [auth BT]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
FA [auth AT],
LB [auth BT]
IPR023333Proteasome B-type subunitFamily
FA [auth AT],
LB [auth BT]
IPR016295Proteasome subunit beta 4Family
FA [auth AT],
LB [auth BT]
IPR001353Proteasome, subunit alpha/betaFamily
D [auth AX],
JA [auth BX]
IPR0407806S proteasome subunit Rpn6, C-terminal helix domainDomain
D [auth AX],
JA [auth BX]
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
D [auth AX],
JA [auth BX]
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
D [auth AX],
JA [auth BX]
IPR04077326S proteasome regulatory subunit Rpn6, N-terminalDomain
D [auth AX],
JA [auth BX]
IPR000717Proteasome component (PCI) domainDomain
E [auth AY],
KA [auth BY]
IPR011990Tetratricopeptide-like helical domain superfamilyHomologous Superfamily
E [auth AY],
KA [auth BY]
IPR01958526S proteasome regulatory subunit Rpn7/COP9 signalosome complex subunit 1Family
E [auth AY],
KA [auth BY]
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
E [auth AY],
KA [auth BY]
IPR04954926S proteasome regulatory subunit RPN7/PSMD6, C-terminal helixDomain
E [auth AY],
KA [auth BY]
IPR000717Proteasome component (PCI) domainDomain
E [auth AY],
KA [auth BY]
IPR04513526S proteasome regulatory subunit Rpn7, N-terminalDomain
F [auth AZ],
LA [auth BZ]
IPR03385826S Proteasome non-ATPase regulatory subunit 7/8Family
F [auth AZ],
LA [auth BZ]
IPR024969EIF3F/CSN6-like, C-terminalDomain
F [auth AZ],
LA [auth BZ]
IPR037518MPN domainDomain
F [auth AZ],
LA [auth BZ]
IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain
G [auth Aa],
MA [auth Ba]
IPR036390Winged helix DNA-binding domain superfamilyHomologous Superfamily
G [auth Aa],
MA [auth Ba]
IPR03529826S Proteasome non-ATPase regulatory subunit 13Family
G [auth Aa],
MA [auth Ba]
IPR000717Proteasome component (PCI) domainDomain
H [auth Ab],
NA [auth Bb]
IPR036465von Willebrand factor A-like domain superfamilyHomologous Superfamily
H [auth Ab],
NA [auth Bb]
IPR002035von Willebrand factor, type ADomain
H [auth Ab],
NA [auth Bb]
IPR003903Ubiquitin interacting motifConserved Site
H [auth Ab],
NA [auth Bb]
IPR049590PSMD4, RAZUL domainDomain
I [auth Ac],
OA [auth Bc]
IPR037518MPN domainDomain
I [auth Ac],
OA [auth Bc]
IPR000555JAB1/MPN/MOV34 metalloenzyme domainDomain

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A [auth AU],
GA [auth BU]
PharosQ99460
J [auth Ad],
PA [auth Bd]
PharosP48556
K [auth Ae],
QA [auth Be]
PharosP60896
L [auth Af],
RA [auth Bf]
PharosQ13200
M [auth AA],
SA [auth BA]
PharosP35998
O [auth AD],
UA [auth BD]
PharosP43686
Q [auth AF],
WA [auth BF]
PharosP17980
R [auth AC],
XA [auth BC]
PharosP62195
S [auth AG],
YA [auth BG]
PharosP60900
B [auth AV],
HA [auth BV]
PharosO43242
T [auth AH],
ZA [auth BH]
PharosP25787
AB [auth BI],
U [auth AI]
PharosP25789
BB [auth BJ],
V [auth AJ]
PharosO14818
CB [auth BK],
W [auth AK]
PharosP28066
DB [auth BL],
X [auth AL]
PharosP25786
EB [auth BM],
Y [auth AM]
PharosP25788
FB [auth BN],
Z [auth AN]
PharosP28072
AA [auth AO],
GB [auth BO]
PharosQ99436
BA [auth AP],
HB [auth BP]
PharosP49720
CA [auth AQ],
IB [auth BQ]
PharosP49721
C [auth AW],
IA [auth BW]
PharosO00232
DA [auth AR],
JB [auth BR]
PharosP28074
EA [auth AS],
KB [auth BS]
PharosP20618
FA [auth AT],
LB [auth BT]
PharosP28070
D [auth AX],
JA [auth BX]
PharosO00231
E [auth AY],
KA [auth BY]
PharosQ15008
F [auth AZ],
LA [auth BZ]
PharosP51665
G [auth Aa],
MA [auth Ba]
PharosQ9UNM6
H [auth Ab],
NA [auth Bb]
PharosP55036
I [auth Ac],
OA [auth Bc]
PharosO00487