1RTW

X-ray Structure of PF1337, a TenA Homologue from Pyrococcus furiosus. Northeast Structural Genomics Research Consortium (Nesg) Target PFR34

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1rtwb_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	TENA/THI-4	Putative transcriptional activator PF1337	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
D	d1rtwd_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	TENA/THI-4	Putative transcriptional activator PF1337	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
A	d1rtwa_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	TENA/THI-4	Putative transcriptional activator PF1337	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)
C	d1rtwc_	All alpha proteins	Heme oxygenase-like	Heme oxygenase-like	TENA/THI-4	Putative transcriptional activator PF1337	(Pyrococcus furiosus DSM 3638 ) [TaxId: 186497 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Heme oxygenase-like	8040911	3001676	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Heme oxygenase-like	8040911	3001676	SCOP2B (2022-06-29)
A	SCOP2 Family	TenA/THI4-like	8028532	4000765	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Heme oxygenase-like	8040911	3001676	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Heme oxygenase-like	8040911	3001676	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	TENA_THI-4	e1rtwB1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: TENA_THI-4	ECOD (1.6)
D	TENA_THI-4	e1rtwD1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: TENA_THI-4	ECOD (1.6)
A	TENA_THI-4	e1rtwA1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: TENA_THI-4	ECOD (1.6)
C	TENA_THI-4	e1rtwC1	A: alpha bundles	X: Ferritin/Heme oxygenase/4-helical cytokines	H: Ferritin/Heme oxygenase	T: Heme oxygenase/Ribonucleotide reductase	F: TENA_THI-4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
D	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
A	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)
C	1.20.910.10	Mainly Alpha	Up-down Bundle	Heme Oxygenase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03070	TENA/THI-4/PQQC family (TENA_THI-4)	TENA/THI-4/PQQC family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	transcriptional activator, putative	-	organic hydroxy compound metabolic process metabolic process cellular process small molecule metabolic process sulfur compound metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR004305	Thiaminase-2/PQQC	Domain
A, B, C, D	IPR050967	Thiamine Salvage Pathway TenA	Family
A, B, C, D	IPR016084	Haem oxygenase-like, multi-helical	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.