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Database: UniProt
Entry: W6L9R1_9TRYP
LinkDB: W6L9R1_9TRYP
Original site: W6L9R1_9TRYP 
ID   W6L9R1_9TRYP            Unreviewed;       331 AA.
AC   W6L9R1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=CR-type domain-containing protein {ECO:0000259|PROSITE:PS51188};
GN   ORFNames=GSHART1_T00000494001 {ECO:0000313|EMBL:CCW66286.1};
OS   Phytomonas sp. Hart1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW66286.1, ECO:0000313|Proteomes:UP000053358};
RN   [1] {ECO:0000313|EMBL:CCW66286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW66286.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW66286.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hart1 {ECO:0000313|EMBL:CCW66286.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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DR   EMBL; HF955199; CCW66286.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6L9R1; -.
DR   EnsemblProtists; CCW66286; CCW66286; GSHART1_T00000494001.
DR   OrthoDB; 2785358at2759; -.
DR   Proteomes; UP000053358; Unassembled WGS sequence.
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   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 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   InterPro; IPR002939; DnaJ_C.
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   PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR43888:SF37; SHOCK PROTEIN DNAJ, PUTATIVE-RELATED; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053358};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00546}.
FT   DOMAIN          50..135
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         50..135
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          309..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  37075 MW;  D13221F4721B5BCE CRC64;
     MFSSNIDNML NAFFGGGIPE MGIHESGRRF MEKLNQHQTV SVSLDDLYNG CEVELNSTRR
     VICVNCSGRG TRKKNKSMLR CTRCGGTGTS IEVQQMGMMI QQMQTTCNAC NGTGTRIDPS
     ACCQSCYGEK VVEIEVPIQV EIEPGMRHEE SIFYPKMGNE YPGYASAGDL TVEVSQRSHP
     LFVRSENDLH MKHVISLAEA LCGLRFKIVQ LDGRELLVTR KRGEITYPGE QKCLRGEGMP
     IRSTGKFGDL HIEFIVNYPE YVDDNQIRLL SAALPEPRQH PMHEVPNDES KNEEVCYASR
     EDIETLKKEI SLDEMSDEDD EQGGTVGCQA Q
//
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