Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyAcyl-CoA N-acyltransferases (Nat)8036033 3000403 SCOP2B (2022-06-29)
BSCOP2 FamilyKinetochore protein Mis16-like8047411 4005630 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyWD40 repeat-like8053351 3001694 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF21184e4pswA3 A: alpha arraysX: HTHH: HTHT: HAT1, C-terminal domainF: PF21184ECOD (1.6)
APF00583,PF10394e4pswA2 A: a+b three layersX: Nat/IvyH: Acyl-CoA N-acyltransferases (Nat) (From Topology)T: Acyl-CoA N-acyltransferases (Nat)F: PF00583,PF10394ECOD (1.6)
APF10394e4pswA1 A: few secondary structure elementsX: beta-beta-alpha zinc fingersH: beta-beta-alpha zinc fingers (From Topology)T: beta-beta-alpha zinc fingersF: PF10394ECOD (1.6)
BPF00400,PF12265e4pswB1 A: beta duplicates or obligate multimersX: beta-propeller-likeH: beta-propellerT: 7-bladedF: PF00400,PF12265ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.90.360.10 Alpha Beta Alpha-Beta Complex Histone Acetyltransferase domain 1CATH (4.3.0)
A3.40.630.30 Alpha Beta 3-Layer(aba) Sandwich Aminopeptidase Gcn5-related N-acetyltransferase (GNAT)CATH (4.3.0)
A1.10.10.390 Mainly Alpha Orthogonal Bundle Arc Repressor Mutant, subunit A CATH (4.3.0)
B2.130.10.10 Mainly Beta 7 Propeller Methylamine Dehydrogenase Chain HCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF21184Fungal HAT1, C-terminal (HAT1_C_fung)Fungal HAT1, C-terminalHistone acetyltransferase type B catalytic subunit (HAT1) is the catalytic subunit of the histone acetylase B (HAT-B) complex (composed on HAT1 and HAT2 at least) [1-2]. It DNA double-strand break repair. Yeast HAT1 specifically acetylates H4 at Lys5 ...Histone acetyltransferase type B catalytic subunit (HAT1) is the catalytic subunit of the histone acetylase B (HAT-B) complex (composed on HAT1 and HAT2 at least) [1-2]. It DNA double-strand break repair. Yeast HAT1 specifically acetylates H4 at Lys5 and Lys12 residues. The C-terminal domain of HAT1 is highly variable and not required for HAT activity [1]. It consists of a bundle of helices and a short beta-strand. This entry includes HAT1 from Fungi.
Domain
PF10394Histone acetyl transferase HAT1 N-terminus (Hat1_N)Histone acetyl transferase HAT1 N-terminusThis domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (Pfam:PF00583) domain. It seems to be motifs C and D of the structure. Histon ...This domain is the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of the GNAT Acetyltransf_1 (Pfam:PF00583) domain. It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyse the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated [1].
Domain
PF00583Acetyltransferase (GNAT) family (Acetyltransf_1)Acetyltransferase (GNAT) family- Family
PF12265Histone-binding protein RBBP4 or subunit C of CAF1 complex (CAF1C_H4-bd)Histone-binding protein RBBP4 or subunit C of CAF1 complex- Repeat
PF00400WD domain, G-beta repeat (WD40)WD domain, G-beta repeat- Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Histone acetyltransferase type B catalytic subunit
Histone acetyltransferase type B subunit 2
Histone H4 type VIII -

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
TPO Parent Component: THR

RESIDAA0038

PSI-MOD :  O-phospho-L-threonine MOD:00047