ID A0A1W2TN46_ROSNE Unreviewed; 766 AA.
AC A0A1W2TN46;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative CMGC CLK protein kinase {ECO:0000313|EMBL:GAP89773.1};
DE EC=2.7.12.1 {ECO:0000313|EMBL:GAP89773.1};
GN ORFNames=SAMD00023353_3600700 {ECO:0000313|EMBL:GAP89773.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP89773.1};
RN [1] {ECO:0000313|EMBL:GAP89773.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP89773.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DF977481; GAP89773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TN46; -.
DR STRING; 77044.A0A1W2TN46; -.
DR OMA; SINPQHY; -.
DR OrthoDB; 5477821at2759; -.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14134; PKc_CLK; 1.
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 InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45646; SERINE/THREONINE-PROTEIN KINASE DOA-RELATED; 1.
DR PANTHER; PTHR45646:SF11; SERINE_THREONINE-PROTEIN KINASE DOA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:GAP89773.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAP89773.1}.
FT DOMAIN 393..732
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 766 AA; 86434 MW; 59FEE93025A525E5 CRC64;
MSTPTTATAT LHPHYRHHHH QPSHHVHHYP SYPGLSANSA SYRSVASSSG NTLLPTPSSA
SSTASTATIP NRHSQQHQPQ QQPQHQPPQQ QPQQQQPQPQ PQPQQQPQPQ PQSQQQQYNP
QTVATPTASA ASAASSYTTN PPYSANEASS NGAVASVAPA RHLSTRTHST PHSEAHHANM
PPATYTESQP RKRRRSKEPD WKQFYKNGLP KEIIVIDDTP DPELQVSSAT TSRTYTNDTT
GATTNKQPAR HVAKKRRKED ELFTDNVYDA RSNGSYQQPT NSGSASSDPT ASAYNTTAPT
SLSSNGQYDY EAPQTGQKRK RTRQQIAQDA KRREVEVLGE GFHEYQPPQK PIKKCGEVTV
RVVNDRTHQT NVKIDDDDGH YIVVPDADLT SQYTIRKLLG QGTFGKVVEA RDRRRNKLVA
IKIIRAVQKY RDASRIELRV LQTLKANDSE NRNRCIHLRD CFDFRGHICI VMDLLGSSVF
DFLKSNNFVP FPNSQIQSFA RQLLTSVAFL HDLNLIHTDL KPENILLCDS AYQTFTYNRR
IPSSTNATNR QATQRKVLLD TEIRLIDFGS ATFDDEYHSS VVSTRHYRAP EIILGLGWSF
PCDIWSIGCI LVEFFTGDAL FQTHDNLEHL AMMENVCDSR IDTHLVQAVN KSASRTSSNS
PAKYFKRLKL DYPTAETTRA SRRFVRHMKR LSDIIPTTSP FLRLFLDLLQ KIFIYDPAKR
ITARQALEHP WFREAAIPDD GTEALKIRLE RMRDSDYHTS RLPAAV
//
