Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyActin/HSP708082534 4000313 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyActin-like ATPases8082535 3000092 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyActin-like ATPases8092416 3000092 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyRac1-binding domain structural repeat-like8089928 3002403 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyRac1-binding domain structural repeat-like8089930 3002403 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyProtein kinase-like (PK-like)8089932 3000066 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyRac1-binding domain structural repeat-like8089929 3002403 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF00022e4ci6A2 A: mixed a+b and a/bX: Ribonuclease H-likeH: Ribonuclease H-like (From Topology)T: Ribonuclease H-likeF: PF00022ECOD (1.6)
BPF09632e4ci6B2 A: alpha bundlesX: Yersinia protein kinase A (YpkA) Rho-GTPase binding domain (From Topology)H: Yersinia protein kinase A (YpkA) Rho-GTPase binding domain (From Topology)T: Yersinia protein kinase A (YpkA) Rho-GTPase binding domainF: PF09632ECOD (1.6)
BPF00069e4ci6B1 A: a+b complex topologyX: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)H: Protein kinase/SAICAR synthase/ATP-graspT: Protein kinaseF: PF00069ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.30.420.40 Alpha Beta 2-Layer Sandwich Nucleotidyltransferase domain 5CATH (4.3.0)
A3.90.640.10 Alpha Beta Alpha-Beta Complex Actin Chain A, domain 4CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00022Actin (Actin)Actin- Family
PF09632Rac1-binding domain (Rac1)Rac1-binding domainThe Rac1-binding domain is the C-terminal portion of YpkA from Yersinia. It is an all-helical molecule consisting of two distinct subdomains connected by a linker. the N-terminal end, residues 434-615, consists of six helices organised into two three ...The Rac1-binding domain is the C-terminal portion of YpkA from Yersinia. It is an all-helical molecule consisting of two distinct subdomains connected by a linker. the N-terminal end, residues 434-615, consists of six helices organised into two three-helix bundles packed against each other. This region is involved with binding to GTPases. The C-terminal end, residues 705-732. is a novel and elongated fold consisting of four helices clustered into two pairs, and this fold carries the helix implicated in actin activation. Rac1-binding domain mimics host guanidine nucleotide dissociation inhibitors (GDIs) of the Rho GTPases, thereby inhibiting nucleotide exchange in Rac1 and causing cytoskeletal disruption in the host [1]. It is usually found downstream of Pfam:PF00069.
Domain
PF00069Protein kinase domain (Pkinase)Protein kinase domain- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
ACTIN - -
PROTEIN KINASE YOPO -