ID A0A673XGT2_SALTR Unreviewed; 419 AA.
AC A0A673XGT2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=DnaJ homolog subfamily A member 2-like {ECO:0000313|Ensembl:ENSSTUP00000023455.1};
GN Name=LOC115197250 {ECO:0000313|Ensembl:ENSSTUP00000023455.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000023455.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000023455.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
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DR AlphaFoldDB; A0A673XGT2; -.
DR Ensembl; ENSSTUT00000024605.1; ENSSTUP00000023455.1; ENSSTUG00000010135.1.
DR GeneTree; ENSGT00940000154688; -.
DR Proteomes; UP000472277; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030544; F:Hsp70 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; IPR044713; DNJA1/2-like.
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; PTHR43888:SF31; DNAJ HOMOLOG SUBFAMILY A MEMBER 2; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; 2.
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:UP000472277};
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 8..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 138..222
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 138..222
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 374..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 45762 MW; 961015A8BDB515FE CRC64;
MANVVDTKLY DILGVSPSAS ENDLKKVSDC AYRKLYDQFH PDKNPDAGDK FKEISFAYEV
LTNPEKKELY DRYGEQGLRE GGGGGAGMDD IFSHIFGGGL FGFMGGQGRG GGGRNGGRRR
GEDMVHPLKV SLEDLYNGKT TKLQLSKNVL CASCNGAGGK AGAVQKCVAC RGRGMRIMIR
QLAPGMVQQM QSVCTDCNGE GEVISEKDRC KKCEGRKVNK ETKLLEVHVD KGMRHGQKIS
FTGEADQAPG TEPGDILLVL QEKEHEEFRR DGHDLHMTQR IGLVEALCGF QLAVTHLDGR
QLAVKYPPGK VIDPGCIRVV KGEGMPQYRN PFEKGDLFIK FDVQFPDNNW ISPEKLTELE
DLLPARADGP VISSEAEEVD LQDCEVRGQG SAGARREAYN DSSDEEGGPH GPGVQCAHQ
//
