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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//