ID H3BBT8_LATCH Unreviewed; 402 AA.
AC H3BBT8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=DnaJ heat shock protein family (Hsp40) member A4 {ECO:0008006|Google:ProtNLM};
GN Name=LOC102350613 {ECO:0000313|Ensembl:ENSLACP00000019359.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000019359.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000019359.1}
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 EMBL; AFYH01035366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01035367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01035368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005991724.1; XM_005991662.2.
DR RefSeq; XP_005991725.1; XM_005991663.2.
DR AlphaFoldDB; H3BBT8; -.
DR STRING; 7897.ENSLACP00000019359; -.
DR Ensembl; ENSLACT00000019494.1; ENSLACP00000019359.1; ENSLACG00000017028.1.
DR GeneID; 102350613; -.
DR KEGG; lcm:102350613; -.
DR eggNOG; KOG0712; Eukaryota.
DR GeneTree; ENSGT00940000153558; -.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; H3BBT8; -.
DR OMA; TRQHVQC; -.
DR OrthoDB; 2785358at2759; -.
DR TreeFam; TF105141; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000017028; Expressed in muscle tissue and 6 other cell types or tissues.
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:SF58; CR-TYPE DOMAIN-CONTAINING PROTEIN; 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:UP000008672};
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 6..68
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 124..208
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 124..208
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 368..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 45374 MW; 2A1A57995ADD95AA CRC64;
MVRETRYYDI LGVKPNASLE EIKRAYRKLA LKYHPDKNPK EGERFKQISH VYDVLSDTNK
RELYDQGGEA ALKEGGGSGG GFSSPMDIFD MFFGGGGRMY SRTEKRGKTV VHQLAVSLED
LYNGATRKLA LQKNVVCGKC NGCGAKEGAV GCCPNCHGTG MKVHVQQLRP GMIQHIQTVC
SECQGQGEWI RPRDRCRSCN GKKIVREKKI LEVHIDKGMK DGQRITFHRE GDQAPGLEPG
DIVIVLDQKD HPTFQRHDNN LIMKMEIDLV EALCGCKRSV QTLDNRLLMV TSQPGEVIKP
GDVKCVLNEG MPIYKDPFEK GKLIIQFQVS FPEPGWLPAN ELCKLEAFFP PRDEFMTMED
MEEVDLTEFD PHTESRGRYA GEVYEEDEDE DGPRRHVQCQ TS
//
