ID A0A067BFD8_SAPPC Unreviewed; 284 AA.
AC A0A067BFD8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=CR-type domain-containing protein {ECO:0000259|PROSITE:PS51188};
GN ORFNames=SPRG_17671 {ECO:0000313|EMBL:KDO16843.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO16843.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO16843.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO16843.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
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DR EMBL; KK583900; KDO16843.1; -; Genomic_DNA.
DR RefSeq; XP_012212447.1; XM_012357057.1.
DR AlphaFoldDB; A0A067BFD8; -.
DR STRING; 695850.A0A067BFD8; -.
DR EnsemblProtists; KDO16843; KDO16843; SPRG_17671.
DR GeneID; 24139202; -.
DR KEGG; spar:SPRG_17671; -.
DR VEuPathDB; FungiDB:SPRG_17671; -.
DR OMA; NGTFNVH; -.
DR OrthoDB; 212009at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0031072; F:heat shock 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; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43096:SF52; DNAJ HOMOLOG 1, MITOCHONDRIAL-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:UP000030745};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00546}.
FT DOMAIN 36..114
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 36..114
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 30536 MW; 1A1EC18C4F266F95 CRC64;
MFGHQAGGRR SGRPQPQRGA DVQVNCHVSF MEAVNGTTRD LNLNTDVTCD PCDGSGAKPG
TSKRKCKSCG GSGVEILQQG FFAVEQPCRR CRGEGFIIET PCTSCRGRGK VKKARTVEVK
IPEGVDNGMN LRLAHQGEAG SKGGPSGHLY VSISVASDPF FKRNKTDVHC EVPISVAQAI
LGGSIVVPTL TGQVEMTIPK GTQSGTTLKM RGKGIKELNS SRRGSQLVTM NVHIPDTLSA
RQKELMEEFA KEEQLRSEAG ESSCKTHTFA ETAFLKPKDD EEKA
//
