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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Bd2rnrb_ All beta proteins PH domain-like barrel PH domain-like TFIIH domain TFIIH basal transcription factor complex p62 subunit (BTF2-p62), N-terminal domain human (Homo sapiens ) [TaxId: 9606 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTFIIEalpha C-terminal acidic domain-like8102723 3002740 SCOP2B (2022-06-29)
BSCOP2 FamilyTFIIH domain8024579 4001843 SCOP2 (2022-06-29)
BSCOP2 SuperfamilyPH domain-like8036958 3000134 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ATFIIE-A_Ce2rnrA1 A: alpha arraysX: C-terminus of TFIIE alpha (From Topology)H: C-terminus of TFIIE alpha (From Topology)T: C-terminus of TFIIE alphaF: TFIIE-A_CECOD (1.6)
BPH_TFIIHe2rnrB1 A: beta barrelsX: PH domain-likeH: PH domain-like (From Topology)T: PH domain-likeF: PH_TFIIHECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B2.30.29.30 Mainly Beta Roll PH-domain like Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF11521C-terminal general transcription factor TFIIE alpha (TFIIE-A_C)C-terminal general transcription factor TFIIE alpha- Family
PF08567TFIIH p62 subunit, N-terminal domain (PH_TFIIH)TFIIH p62 subunit, N-terminal domainThe N-terminal domain of the TFIIH basal transcription factor complex p62 subunit (BTF2-p62) forms an interaction with the 3' endonuclease XPG, which is essential for activity. The 3' endonuclease XPG is a major component of the nucleotide excision ...The N-terminal domain of the TFIIH basal transcription factor complex p62 subunit (BTF2-p62) forms an interaction with the 3' endonuclease XPG, which is essential for activity. The 3' endonuclease XPG is a major component of the nucleotide excision repair machinery. The structure of the N-terminal domain reveals that it adopts a pleckstrin homology (PH) fold [1,2]. This PH-type domain has been shown to bind to a mono-phosphorylated inositide [2].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Transcription initiation factor IIE subunit alpha
TFIIH basal transcription factor complex p62 subunit