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Database: UniProt
Entry: M5BP75_THACB
LinkDB: M5BP75_THACB
Original site: M5BP75_THACB 
ID   M5BP75_THACB            Unreviewed;       225 AA.
AC   M5BP75;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase {ECO:0000313|EMBL:CCO28861.1};
DE            EC=2.7.12.1 {ECO:0000313|EMBL:CCO28861.1};
GN   ORFNames=BN14_02859 {ECO:0000313|EMBL:CCO28861.1};
OS   Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS   rot fungus) (Rhizoctonia solani).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX   NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO28861.1, ECO:0000313|Proteomes:UP000012065};
RN   [1] {ECO:0000313|EMBL:CCO28861.1, ECO:0000313|Proteomes:UP000012065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX   PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA   Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA   Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA   Schlueter A.S.;
RT   "Establishment and interpretation of the genome sequence of the
RT   phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL   J. Biotechnol. 0:0-0(2013).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MNB/DYRK subfamily.
CC       {ECO:0000256|ARBA:ARBA00008867}.
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:CCO28861.1}.
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DR   EMBL; CAOJ01003861; CCO28861.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5BP75; -.
DR   HOGENOM; CLU_1230639_0_0_1; -.
DR   Proteomes; UP000012065; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR   PANTHER; PTHR24058:SF22; DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCO28861.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCO28861.1}.
FT   DOMAIN          1..114
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          53..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   225 AA;  24594 MW;  EB39C2295D30B743 CRC64;
     MWSLGCILAE LYTGFPIFPG ENEQEQLACI MEVLGVPDKD LVNRSSRKRL FFESNGQPRP
     VVNSKGRRRR PGSKTLAQVL RCDDELFIDF IAKCLIWDPE RRIKPQPALR HPFITAGRRP
     KITSPAPVVS SRHLFTPSSS TSGVTGSRSK PHATPQKSQI GAPTPLSSRI ARGPTTSANT
     SVPQTPTSAS HTANQGTTPS HRYRVPATSS YSSRTLPTSS NGYAQ
//
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