ID   A0A3Q3APZ5_KRYMA        Unreviewed;       412 AA.
AC   A0A3Q3APZ5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=DnaJ homolog subfamily A member 2 {ECO:0000313|Ensembl:ENSKMAP00000018948.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000018948.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000018948.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}.
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DR   RefSeq; XP_017261611.1; XM_017406122.1.
DR   AlphaFoldDB; A0A3Q3APZ5; -.
DR   STRING; 37003.ENSKMAP00000018948; -.
DR   Ensembl; ENSKMAT00000019209.1; ENSKMAP00000018948.1; ENSKMAG00000014076.1.
DR   GeneID; 108230153; -.
DR   KEGG; kmr:108230153; -.
DR   CTD; 324164; -.
DR   GeneTree; ENSGT00940000154688; -.
DR   OMA; KKCEGHK; -.
DR   OrthoDB; 2785358at2759; -.
DR   Proteomes; UP000264800; 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:UP000264800};
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..70
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          131..215
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         131..215
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          359..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  45331 MW;  E7A38BD0B3218F63 CRC64;
     MANVADTRLY DILGVSPSAS ENELKKAYRK LAKEYHPDKN PDAGDKFKEI SFAYEVLTNP
     EKKELYDRYG EQGLREGGGG GPGMDDIFSH IFGGGLFGFM GGQGRGRNGG KRRGDDMVHP
     LKVSLEDLYN GKTTKLQLSK NVLCSACNGQ GGKAGAVQKC VACRGRGMRI MIRQLAPGMV
     QQMQSVCTDC NGEGEVINEK DRCKKCEGQK VCKETKLLEV HVDKGMRHGQ KITFSGEADQ
     APGVEPGDIV LVLQEKDHEE FRRDGNDLHM VQRIGLVEAL CGFQITITHL DGRQLLVKYP
     PGKVIEPGCI RVVKGEGMPQ YRNPFEKGDL YIKFDVQFPE NNWISPEKLN DLENLLPARS
     DSPEIAPDAE EVELTDYDKS QGSGSGARRE AYNDSSDDEG GHHGPGVQCA HQ
//