ID V2WVA4_MONRO Unreviewed; 512 AA.
AC V2WVA4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dj-1 family protein {ECO:0000313|EMBL:ESK84486.1};
GN ORFNames=Moror_6166 {ECO:0000313|EMBL:ESK84486.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK84486.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK84486.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK84486.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK84486.1}.
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DR EMBL; AWSO01001292; ESK84486.1; -; Genomic_DNA.
DR RefSeq; XP_007856199.1; XM_007858008.1.
DR AlphaFoldDB; V2WVA4; -.
DR STRING; 1381753.V2WVA4; -.
DR KEGG; mrr:Moror_6166; -.
DR HOGENOM; CLU_532189_0_0_1; -.
DR OrthoDB; 46148at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd03139; GATase1_PfpI_2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002818; DJ-1/PfpI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43130; ARAC-FAMILY TRANSCRIPTIONAL REGULATOR; 1.
DR PANTHER; PTHR43130:SF3; THIJ_PFPI FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_5G14240); 1.
DR Pfam; PF01965; DJ-1_PfpI; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 1..227
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 56358 MW; FD986D8BA4357298 CRC64;
MEVAVLHHLS GHENIVPFIG TLDGSLRPCI VLEWMNGGNI VQYLAEHPEE SKESLIQQVV
SGLLYLKERS VVHGDIKPDN ILVTEHGLVR ISDFGSAFFS FMGSTTSRIR ASSLAPPPVG
GTDRYLAPEL LREDSQIPSY QSDVFSFGMT VFQIFTGAIP FPEIKHAAYA SVLIVQGIRP
QRSEDIPDHI WALISTCWSQ GPNDRPTVQQ IHKNLRAVRL ASYIPFFLLL RGRMLVFTSA
RAYCLMEPLN DFVPRIQTQG CAYMGSCSVV FAIFPAVDIK TTIAMANPEG SIHPVNFGVL
LFPTFQALDV FGPLDALNIL SMSFPLNLSI IAKSLDPVST KHRDQTLNPL NSNFGESVVP
THDFDNAPPL DVLLIPGGYG VRADDTESLI DFIRRTYPSL KYVITVCTGS WLAARAGILD
GKRATSNKAS WAGTKVAGPN VKWVSHARWV VDGNIWTSSG VSAGIDVTLA FIEQFYGAKA
ADKVASTMEY ERHTDSTRDP FADKYNLPKE NE
//
