ID A0A3Q3F2T1_9LABR Unreviewed; 454 AA.
AC A0A3Q3F2T1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DnaJ heat shock protein family (Hsp40) member A3b {ECO:0000313|Ensembl:ENSLBEP00000014106.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000014106.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000014106.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q3F2T1; -.
DR STRING; 56723.ENSLBEP00000014106; -.
DR Ensembl; ENSLBET00000014915.1; ENSLBEP00000014106.1; ENSLBEG00000010949.1.
DR GeneTree; ENSGT00940000155280; -.
DR InParanoid; A0A3Q3F2T1; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00546}; Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00546}.
FT DOMAIN 92..157
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 231..309
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 231..309
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
SQ SEQUENCE 454 AA; 49890 MW; 3464463646FCB2EC CRC64;
MASSAARFSS RWLSTSVSSA YRNSGFPSFP ASFAGVCSAT LLQTQRGGTA FGFSSWTHGK
LVTLRGLTGS RCPCCITSHS FHTSSYLSNK DDFYGVLGVS RTATQKDIKK AYYQLAKKYH
PDTSPDDPDA KEKFAKLAEA YEVLSDEVKR KQYDTYGAAG FDPSRAGQSQ QQYYRAGGTN
VDPEELFRKI FGDFLEEWAS ETFTTCYKCN QMYIFLPQYV MELTFAEAAK GSNKDLNINI
DDNCPRCGGK GSEPGTKVSH CQYCNGTGME SVNTGPFMMR TTCRRCGGKG SIITTPCALC
RGSGQMKKRQ TVNVPVPAGV ENGQTVRMSV GNKEILITFR VHRSPVFRRN GVDIHSDVLI
SIAQAILGGT ATSQGLHETI SIVIPPSCQP DQVIRLHGKG IRRMNSYSYG DHYVHIKIKV
PKKLTRKQRS LLLSYAEEEM EVQGTVNGVT PSPG
//
