7ZHS | pdb_00007zhs

3D reconstruction of the cylindrical assembly of DnaJA2 delta G/F by imposing D5 symmetry

External Resource: Annotation

Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	PF00684	DnaJ central domain (DnaJ_CXXCXGXG)	DnaJ central domain	The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although ...	The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found [1].	Domain
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	PF01556	DnaJ C terminal domain (DnaJ_C)	DnaJ C terminal domain	This family consists of the C terminal region of the DnaJ protein. It is always found associated with Pfam:PF00226 and Pfam:PF00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after ...	This family consists of the C terminal region of the DnaJ protein. It is always found associated with Pfam:PF00226 and Pfam:PF00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions [2]. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	Ubiquitin-like protein SMT3,DnaJ homolog subfamily A member 2	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding unfolded protein binding protein binding ATPase activator activity molecular function activator activity molecular function regulator activity ATPase regulator activity ATP-dependent activity Hsp70 protein binding protein-folding chaperone binding heat shock protein binding cation binding metal ion binding protein tag activity molecular tag activity ubiquitin-like protein ligase binding enzyme binding identical protein binding	protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of biological process cell population proliferation regulation of cellular process protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of biological process cell population proliferation regulation of cellular process positive regulation of cell population proliferation regulation of cell population proliferation biological regulation positive regulation of biological process positive regulation of cellular process response to stimulus response to stress response to heat response to abiotic stimulus response to temperature stimulus peptidyl-lysine modification protein sumoylation macromolecule modification peptidyl-amino acid modification protein modification process post-translational protein modification protein modification by small protein conjugation protein modification by small protein conjugation or removal	cellular anatomical structure membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cellular anatomical structure membrane extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cell cortex septin ring intracellular membraneless organelle intracellular organelle cell periphery cytoskeleton membraneless organelle septin cytoskeleton condensed nuclear chromosome nucleus membrane-enclosed lumen nuclear chromosome chromosome intracellular membrane-bounded organelle intracellular organelle lumen organelle lumen condensed chromosome nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR018253	DnaJ domain, conserved site	Conserved Site
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR044713	DnaJ homolog subfamily A member 1/2-like	Family
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR002939	Chaperone DnaJ, C-terminal	Domain
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR036869	Chaperone J-domain superfamily	Homologous Superfamily
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR001305	Heat shock protein DnaJ, cysteine-rich domain	Domain
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR001623	DnaJ domain	Domain
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR008971	HSP40/DnaJ peptide-binding	Homologous Superfamily
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR012724	Chaperone DnaJ	Family
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR036410	Heat shock protein DnaJ, cysteine-rich domain superfamily	Homologous Superfamily
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR029071	Ubiquitin-like domain superfamily	Homologous Superfamily
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR000626	Ubiquitin-like domain	Domain
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	IPR022617	Rad60/SUMO-like domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, AA [auth O], B [auth C], BA [auth W], C [auth B], A, AA [auth O], B [auth C], BA [auth W], C [auth B], CA [auth a], D, DA [auth i], E, EA [auth e], F [auth G], FA [auth m], G [auth F], GA [auth L], H, HA [auth T], I, IA [auth P], J [auth Q], JA [auth X], K [auth M], KA [auth b], L [auth U], LA [auth j], M [auth Y], MA [auth f], N [auth g], NA [auth n], O [auth c], P [auth k], Q [auth J], R, S [auth N], T [auth V], U [auth Z], V [auth h], W [auth d], X [auth l], Y [auth K], Z [auth S]	Pharos: O60884	glioblastoma psoriasis osteosarcoma ovarian cancer

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.