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Database: UniProt
Entry: K2S680_MACPH
LinkDB: K2S680_MACPH
Original site: K2S680_MACPH 
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
//
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