Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
FSCOP2B SuperfamilyRecA-like P-loop NTPases8091625 3002019 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyRestriction endonuclease-like8091621 3000104 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyHsdR C-terminal domain-like8091622 3002528 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyRecA-like P-loop NTPases8091624 3002019 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF12161e7btqA2 A: alpha arraysX: N-terminal helical domain in restriction-modification system methylation subunit-likeH: N-terminal helical domain in restriction-modification system methylation subunit (From Topology)T: N-terminal helical domain in restriction-modification system methylation subunitF: PF12161ECOD (1.6)
APF02384e7btqA1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF02384ECOD (1.6)
DPF12161e7btqD2 A: alpha arraysX: N-terminal helical domain in restriction-modification system methylation subunit-likeH: N-terminal helical domain in restriction-modification system methylation subunit (From Topology)T: N-terminal helical domain in restriction-modification system methylation subunitF: PF12161ECOD (1.6)
DPF02384e7btqD1 A: a/b three-layered sandwichesX: Rossmann-likeH: Rossmann-relatedT: S-adenosyl-L-methionine-dependent methyltransferasesF: PF02384ECOD (1.6)
EPF01420e7btqE1 A: a+b complex topologyX: DNA methylase specificity domain (From Topology)H: DNA methylase specificity domain (From Topology)T: DNA methylase specificity domainF: PF01420ECOD (1.6)
FPF12008e7btqF3 A: alpha arraysX: HSDR subunit helical domain (From Topology)H: HSDR subunit helical domain (From Topology)T: HSDR subunit helical domainF: PF12008ECOD (1.6)
FPF12008e7btqF1 A: alpha complex topologyX: EcoR124I HsdR C-terminal domain (From Topology)H: EcoR124I HsdR C-terminal domain (From Topology)T: EcoR124I HsdR C-terminal domainF: PF12008ECOD (1.6)
FPF18766e7btqF2 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF18766ECOD (1.6)
FPF22679e7btqF4 A: a/b three-layered sandwichesX: P-loop domains-likeH: P-loop domains-relatedT: P-loop containing nucleoside triphosphate hydrolasesF: PF22679ECOD (1.6)
FPF04313e7btqF5 A: a/b three-layered sandwichesX: Restriction endonuclease-likeH: Restriction endonuclease-like (From Topology)T: Restriction endonuclease-likeF: PF04313ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, D
PF12161HsdM N-terminal domain (HsdM_N)HsdM N-terminal domainThis domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with ...This domain is found at the N-terminus of the methylase subunit of Type I DNA methyltransferases. This domain family is found in bacteria and archaea, and is typically between 123 and 138 amino acids in length. The family is found in association with Pfam:PF02384. Mutations in this region of EcoKI methyltransferase Swiss:P08957 abolish the normally strong preference of this system for methylating hemimethylated substrate [1]. The structure of this domain has been shown to be all alpha-helical.
Domain
PF01420Type I restriction modification DNA specificity domain (Methylase_S)Type I restriction modification DNA specificity domainThis domain is also known as the target recognition domain (TRD). Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host ge ...This domain is also known as the target recognition domain (TRD). Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The host genome is protected from cleavage by methylation of specific nucleotides in the target sites. In type I systems, both restriction and modification activities are present in one heteromeric enzyme complex composed of one DNA specificity subunit (this family), two modification (M) subunits and two restriction (R) subunits [2].
Domain
PF18766SWI2/SNF2 ATPase (SWI2_SNF2)SWI2/SNF2 ATPase- Family
PF04313Type I restriction enzyme R protein N terminus (HSDR_N) (HSDR_N)Type I restriction enzyme R protein N terminus (HSDR_N)- Family
PF12008Type I restriction and modification enzyme - subunit R C terminal (EcoR124_C)Type I restriction and modification enzyme - subunit R C terminalThis enzyme has been characterised and shown to belong to a new family of the type I class of restriction and modification enzymes. This family is involved in bacterial defence by making double strand breaks in specific double stranded DNA sequences, ...This enzyme has been characterised and shown to belong to a new family of the type I class of restriction and modification enzymes. This family is involved in bacterial defence by making double strand breaks in specific double stranded DNA sequences, e.g. that of invading bacteriophages. EcoR124 is made up of three subunits, HsdR, HsdS and HsdM. The R subunit has ATPase and restriction endonuclease activity. This domain is the C terminal of the R subunit [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, D
Type I restriction enzyme EcoR124II M protein -
DNA (64-MER)---
DNA (64-MER)---
Type-1 restriction enzyme EcoR124II specificity protein -
Type I restriction enzyme R Protein -