Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
CSCOP2B SuperfamilyMethyl-coenzyme M reductase subunits 8073481 3001305 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyMethyl-coenzyme M reductase subunits 8073481 3001305 SCOP2B (2022-06-29)
ISCOP2 FamilyMethyl-coenzyme M reductase gamma chain 8073480 4001330 SCOP2 (2022-06-29)
ISCOP2 SuperfamilyMethyl-coenzyme M reductase subunits 8073481 3001305 SCOP2 (2022-06-29)
LSCOP2B SuperfamilyMethyl-coenzyme M reductase subunits 8073481 3001305 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AMCR_alphae5a8rA2 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_alphaECOD (1.6)
AMCR_alpha_Ne5a8rA1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_alpha_NECOD (1.6)
DMCR_alphae5a8rD1 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_alphaECOD (1.6)
DMCR_alpha_Ne5a8rD2 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_alpha_NECOD (1.6)
GMCR_alphae5a8rG2 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_alphaECOD (1.6)
GMCR_alpha_Ne5a8rG1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_alpha_NECOD (1.6)
JMCR_alphae5a8rJ2 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_alphaECOD (1.6)
JMCR_alpha_Ne5a8rJ1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_alpha_NECOD (1.6)
BMCR_betae5a8rB1 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_betaECOD (1.6)
BMCR_beta_Ne5a8rB2 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_beta_NECOD (1.6)
EMCR_betae5a8rE2 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_betaECOD (1.6)
EMCR_beta_Ne5a8rE1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_beta_NECOD (1.6)
KMCR_betae5a8rK1 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_betaECOD (1.6)
KMCR_beta_Ne5a8rK2 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_beta_NECOD (1.6)
HMCR_betae5a8rH2 A: alpha bundlesX: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)H: Methyl-coenzyme M reductase alpha and beta chain-C (From Topology)T: Methyl-coenzyme M reductase alpha and beta chain-CF: MCR_betaECOD (1.6)
HMCR_beta_Ne5a8rH1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_beta_NECOD (1.6)
CMCR_gammae5a8rC1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_gammaECOD (1.6)
FMCR_gammae5a8rF1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_gammaECOD (1.6)
IMCR_gammae5a8rI1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_gammaECOD (1.6)
LMCR_gammae5a8rL1 A: a+b two layersX: Alpha-beta plaitsH: Methyl-coenzyme M reductase subunits (From Topology)T: Methyl-coenzyme M reductase subunitsF: MCR_gammaECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.90.390.10 Alpha Beta Alpha-Beta Complex Methyl-coenzyme M Reductase Chain A, domain 1CATH (4.3.0)
A3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
A1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
D3.90.390.10 Alpha Beta Alpha-Beta Complex Methyl-coenzyme M Reductase Chain A, domain 1CATH (4.3.0)
D3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
D1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
G3.90.390.10 Alpha Beta Alpha-Beta Complex Methyl-coenzyme M Reductase Chain A, domain 1CATH (4.3.0)
G3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
G1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
J3.90.390.10 Alpha Beta Alpha-Beta Complex Methyl-coenzyme M Reductase Chain A, domain 1CATH (4.3.0)
J3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
J1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
B1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
B3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
E1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
E3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
K1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
K3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
H1.20.840.10 Mainly Alpha Up-down Bundle Methyl-coenzyme M Reductase Chain B, domain 2CATH (4.3.0)
H3.30.70.470 Alpha Beta 2-Layer Sandwich Alpha-Beta Plaits CATH (4.3.0)
C3.90.320.20 Alpha Beta Alpha-Beta Complex Lambda Exonuclease Chain ACATH (4.3.0)
F3.90.320.20 Alpha Beta Alpha-Beta Complex Lambda Exonuclease Chain ACATH (4.3.0)
I3.90.320.20 Alpha Beta Alpha-Beta Complex Lambda Exonuclease Chain ACATH (4.3.0)
L3.90.320.20 Alpha Beta Alpha-Beta Complex Lambda Exonuclease Chain ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, D, G, J
PF02745Methyl-coenzyme M reductase alpha subunit, N-terminal domain (MCR_alpha_N)Methyl-coenzyme M reductase alpha subunit, N-terminal domainMethyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (Pfam:PF02241), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active ...Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (Pfam:PF02241), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active sites [1]. The N-terminal domain has a ferredoxin-like fold.
Domain
A, D, G, J
PF02249Methyl-coenzyme M reductase alpha subunit, C-terminal domain (MCR_alpha)Methyl-coenzyme M reductase alpha subunit, C-terminal domainMethyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (Pfam:PF02241), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active ...Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (Pfam:PF02241), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active sites [1]. The C-terminal domain is comprised of an all-alpha multi-helical bundle.
Domain
B, E, H, K
PF02241Methyl-coenzyme M reductase beta subunit, C-terminal domain (MCR_beta)Methyl-coenzyme M reductase beta subunit, C-terminal domainMethyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (this family), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active ...Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (this family), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active sites [1]. The C-terminal domain of MCR beta has an all-alpha fold with buried central helix.
Domain
B, E, H, K
PF02783Methyl-coenzyme M reductase beta subunit, N-terminal domain (MCR_beta_N)Methyl-coenzyme M reductase beta subunit, N-terminal domainMethyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (this family), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active ...Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (this family), and 2 gamma (Pfam:PF02240) subunits with two identical nickel porphinoid active sites [1]. The N-terminal domain has an alpha/beta ferredoxin-like fold.
Domain
C, F, I, L
PF02240Methyl-coenzyme M reductase gamma subunit (MCR_gamma)Methyl-coenzyme M reductase gamma subunitMethyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (Pfam:PF02241), and 2 gamma (this family) subunits with two identical nickel porphinoid activ ...Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (Pfam:PF02249), 2 beta (Pfam:PF02241), and 2 gamma (this family) subunits with two identical nickel porphinoid active sites [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, D, G, J
METHYL-COENZYME M REDUCTASE II SUBUNIT ALPHA -
B, E, H, K
METHYL-COENZYME M REDUCTASE II SUBUNIT GAMMA -
C, F, I, L
METHYL-COENZYME M REDUCTASE II, SUBUNIT BETA -

InterPro: Protein Family Classification InterPro Database Homepage

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
A, D, G, J
AGM Parent Component: ARG

RESIDAA0272

PSI-MOD :  5-methyl-L-arginine MOD:00277
A, D, G, J
DYA Parent Component: ASP

RESIDAA0272

A, D, G, J
GL3 Parent Component: GLY

RESIDAA0272 , AA0265

PSI-MOD :  5-methyl-L-arginine MOD:00277 , 1-thioglycine (internal) MOD:00270 , 1-thioglycine (C-terminal) MOD:01623
A, D, G, J
MGN Parent Component: GLN

RESIDAA0272 , AA0265 , AA0273

PSI-MOD :  5-methyl-L-arginine MOD:00277 , 1-thioglycine (internal) MOD:00270 , 1-thioglycine (C-terminal) MOD:01623 , 2-methyl-L-glutamine MOD:00278
A, D, G, J
MHS Parent Component: HIS

RESIDAA0272 , AA0265 , AA0273 , AA0073

PSI-MOD :  5-methyl-L-arginine MOD:00277 , 1-thioglycine (internal) MOD:00270 , 1-thioglycine (C-terminal) MOD:01623 , 2-methyl-L-glutamine MOD:00278 , 3'-methyl-L-histidine MOD:00082
A, D, G, J
SMC Parent Component: CYS

RESIDAA0272 , AA0265 , AA0273 , AA0073 , AA0234

PSI-MOD :  5-methyl-L-arginine MOD:00277 , 1-thioglycine (internal) MOD:00270 , 1-thioglycine (C-terminal) MOD:01623 , 2-methyl-L-glutamine MOD:00278 , 3'-methyl-L-histidine MOD:00082 , S-methyl-L-cysteine MOD:00239