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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1qhr.1 All beta proteins Trypsin-like serine proteases Trypsin-like serine proteases Eukaryotic proteases Thrombin (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)
Bd1qhr.1 All beta proteins Trypsin-like serine proteases Trypsin-like serine proteases Eukaryotic proteases Thrombin (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyTrypsin-like serine proteases 8042154 3000114 SCOP2B (2022-06-29)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B2.40.10.10 Mainly Beta Beta Barrel Thrombin, subunit H Trypsin-like serine proteasesCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF09396Thrombin light chain (Thrombin_light)Thrombin light chainThrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleave ...Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.
Domain
PF00089Trypsin (Trypsin)Trypsin- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
ALPHA THROMBIN
ALPHA THROMBIN
C [auth I]HIRUGEN

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR018992Thrombin light chainDomain
IPR037111Thrombin light chain domain superfamilyHomologous Superfamily
IPR003966Prothrombin/thrombinFamily
IPR018114Serine proteases, trypsin family, histidine active siteActive Site
IPR009003Peptidase S1, PA clanHomologous Superfamily
IPR033116Serine proteases, trypsin family, serine active siteActive Site
IPR001254Serine proteases, trypsin domainDomain
IPR035972Gamma-carboxyglutamic acid-rich (GLA) domain superfamilyHomologous Superfamily
IPR000001KringleDomain
IPR000294Gamma-carboxyglutamic acid-rich (GLA) domainDomain
IPR051659Serine Protease S1 Domain-Containing ProteinFamily
IPR018056Kringle, conserved siteConserved Site
IPR013806Kringle-like foldHomologous Superfamily
IPR038178Kringle superfamilyHomologous Superfamily
IPR001314Peptidase S1A, chymotrypsin familyFamily
IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
IPR018992Thrombin light chainDomain
IPR037111Thrombin light chain domain superfamilyHomologous Superfamily
IPR003966Prothrombin/thrombinFamily
IPR018114Serine proteases, trypsin family, histidine active siteActive Site
IPR009003Peptidase S1, PA clanHomologous Superfamily
IPR033116Serine proteases, trypsin family, serine active siteActive Site
IPR001254Serine proteases, trypsin domainDomain
IPR035972Gamma-carboxyglutamic acid-rich (GLA) domain superfamilyHomologous Superfamily
IPR000001KringleDomain
IPR000294Gamma-carboxyglutamic acid-rich (GLA) domainDomain
IPR051659Serine Protease S1 Domain-Containing ProteinFamily
IPR018056Kringle, conserved siteConserved Site
IPR013806Kringle-like foldHomologous Superfamily
IPR038178Kringle superfamilyHomologous Superfamily
IPR001314Peptidase S1A, chymotrypsin familyFamily
IPR043504Peptidase S1, PA clan, chymotrypsin-like foldHomologous Superfamily
C [auth I]IPR011061Hirudin/antistatinHomologous Superfamily
C [auth I]IPR000429Proteinase inhibitor I14, hirudinFamily
C [auth I]IPR024793Thrombin inhibitor hirudinHomologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosP00734
PharosP00734

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
C [auth I]TYS Parent Component: TYR

RESIDAA0172

PSI-MOD :  O4'-sulfo-L-tyrosine MOD:00181