ID A0A0K9PDV0_ZOSMR Unreviewed; 349 AA.
AC A0A0K9PDV0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative Chaperone protein dnaJ {ECO:0000313|EMBL:KMZ67129.1};
GN ORFNames=ZOSMA_278G00150 {ECO:0000313|EMBL:KMZ67129.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ67129.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ67129.1}.
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DR EMBL; LFYR01000930; KMZ67129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PDV0; -.
DR STRING; 29655.A0A0K9PDV0; -.
DR OMA; LYITYNV; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10747; DnaJ_C; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
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; IPR036869; J_dom_sf.
DR PANTHER; PTHR44298; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR PANTHER; PTHR44298:SF1; DNAJ HOMOLOG SUBFAMILY B MEMBER 11; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..349
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005527620"
FT DOMAIN 31..96
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 349 AA; 39489 MW; FE68A110AA0C6466 CRC64;
MLSARRMSAT SLLFFTFFAV SLFLHAFAGK NYYDVLQISK SATEEQIKRA YRKLALKYHP
DKNPGNEEAN KKFAEISNAY EVLSDQEKRG IYDRYGEEGL KQSGGRGQGG GMNMQDIFSS
FFGGGGSHEE EEETIAKGDD VIIDLDASLE DLYMGGSLKV WREKNVLKSA PGKRKCNCKN
EVYHRQIAPG MYQQMTQEVC EECPNVKYVR EGYFIDVDIE KGMQDGHEVV FYEDGEPMID
GESGDLKFII KTAPHDTFRR EKNDLHTTVT ISLLQALIGF EKSIKHLDER LVSIGTKGIT
KPKEVRRIKG EGMPLHMSLR KGDLYVKYEV LFPSTLTEDQ KTKIKAALS
//
