Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ESCOP2B SuperfamilySDR-like 8088242 3000038 SCOP2B (2022-06-29)
FSCOP2B SuperfamilySDR-like 8088242 3000038 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyS-adenosylmethionine synthetase 8035289 3000766 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyS-adenosylmethionine synthetase 8035292 3000766 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyS-adenosylmethionine synthetase 8035293 3000766 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035289 3000766 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035293 3000766 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035292 3000766 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035292 3000766 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035293 3000766 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035289 3000766 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035292 3000766 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035293 3000766 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyS-adenosylmethionine synthetase 8035289 3000766 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ERmlD_sub_binde4ndnE1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: RmlD_sub_bindECOD (1.6)
FRmlD_sub_binde4ndnF1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: NAD(P)-binding Rossmann-fold domainsF: RmlD_sub_bindECOD (1.6)
AS-AdoMet_synt_Ce4ndnA1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_CECOD (1.6)
AS-AdoMet_synt_Me4ndnA2 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_MECOD (1.6)
AS-AdoMet_synt_Ne4ndnA3 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_NECOD (1.6)
BS-AdoMet_synt_Ce4ndnB1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_CECOD (1.6)
BS-AdoMet_synt_Me4ndnB2 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_MECOD (1.6)
BS-AdoMet_synt_Ne4ndnB3 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_NECOD (1.6)
CS-AdoMet_synt_Ce4ndnC1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_CECOD (1.6)
CS-AdoMet_synt_Me4ndnC2 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_MECOD (1.6)
CS-AdoMet_synt_Ne4ndnC3 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_NECOD (1.6)
DS-AdoMet_synt_Ce4ndnD1 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_CECOD (1.6)
DS-AdoMet_synt_Me4ndnD2 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_MECOD (1.6)
DS-AdoMet_synt_Ne4ndnD3 A: a+b two layersX: Alpha-lytic protease prodomain-likeH: S-adenosylmethionine synthetase (From Topology)T: S-adenosylmethionine synthetaseF: S-AdoMet_synt_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
E, F
PF04321RmlD substrate binding domain (RmlD_sub_bind)RmlD substrate binding domainL-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsi ...L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide [1,2].
Domain
A, B, C, D
PF00438S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N)S-adenosylmethionine synthetase, N-terminal domainThe three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.Domain
A, B, C, D
PF02773S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C)S-adenosylmethionine synthetase, C-terminal domainThe three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.Domain
A, B, C, D
PF02772S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M)S-adenosylmethionine synthetase, central domainThe three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
E, F
Methionine adenosyltransferase 2 subunit beta
A, B, C, D
S-adenosylmethionine synthase isoform type-2