ID K2S680_MACPH Unreviewed; 355 AA.
AC K2S680;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=CR-type domain-containing protein {ECO:0000259|PROSITE:PS51188};
GN ORFNames=MPH_02220 {ECO:0000313|EMBL:EKG20497.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG20497.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG20497.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG20497.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG20497.1}.
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DR EMBL; AHHD01000085; EKG20497.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S680; -.
DR STRING; 1126212.K2S680; -.
DR VEuPathDB; FungiDB:MPH_02220; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; K2S680; -.
DR OrthoDB; 2785358at2759; -.
DR Proteomes; UP000007129; 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:SF12; DNAJ PROTEIN HOMOLOG XDJ1; 1.
DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-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:UP000007129};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00546};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00546}.
FT DOMAIN 74..158
FT /note="CR-type"
FT /evidence="ECO:0000259|PROSITE:PS51188"
FT ZN_FING 74..158
FT /note="CR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 38236 MW; FDD2C7AC82290243 CRC64;
MSAFDGSRPG PGGMGGDVDL DDLLSQMFGM GGGMGGMGGM PGMGGMGGGG PRRPRKGANE
EQEYEVSLEE LYKGKTTRFA STKNVICETC KGSGGREKAK PHDCSVCGGR GQTLRIQTVG
GMLSQVTTQC ANCSGFGKVY KDKEKCKKCK GKRVVEKRKI LELYIPRGAR EGERIVLAGE
ADQQPDQEPG DIIFELVEKE HPTFRRAGAD LQADLHVTLS EALTGFHRVV LTHLDGRGIA
LNVKQPQGKI LRPGEVLKVS GEGMPIKKSD ARGDLYLIVH IEFPEDGYIQ DEAAIKKIRD
LLPGPGPEIK SDDVEDVEFE ADADLDNFGA DSDDPRAAHW EDDDTEEGGP QCATQ
//