ID A0A0W0FD90_9AGAR Unreviewed; 1526 AA.
AC A0A0W0FD90;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=WG66_13280 {ECO:0000313|EMBL:KTB34146.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB34146.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB34146.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB34146.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB34146.1}.
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DR EMBL; LATX01002119; KTB34146.1; -; Genomic_DNA.
DR eggNOG; KOG0578; Eukaryota.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF35; SERINE_THREONINE-PROTEIN KINASE PAK; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 178..191
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 1220..1496
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1017
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 164627 MW; 8D7905AE71C8E5AE CRC64;
MAFSDNSPGA NASSSKSSRF SSLKVFGKFS KEKDSLKPPP PPPKDPFYLN NRSLVSLHNT
NESMPATPVT PHSIGTAYAT SNTVLGSSQS QYVPSEHSKR PPLNATSSTY SLASSSASLV
SSPSDAGAPS LPPLPKQPSQ KKSGFFKFRR VTKSPSLRSA SVDDEMSSLQ SNREDENIST
PYNFQHNIHV DDGLAGMPPS WTVSLAKAGF TEEEIAAIYA RKQAGTLTPG NDFGSPYYSS
YGSDRPKSPA AISIASSAAA SSLQRPGTST SSHGSAGGVS PILTHPVPRS TSLPRQYSDN
SLRQTIVAGR NFSPSQSPNL GQQQQHVMRT ERSRNNSASS VALSVSIPIS ESSRLRPNAV
AVQGNSDDEA SGAEHRQNQS SSNPSRQPSR NPSIKSRTDS PRMQPYVPTG LVNIASQGPQ
QGSPGSRPST PPRRTYFVAN SQTPPQMQSP PPSYSAVNGI HQQSMQMGSN GYPVEKSETE
KDTPKQRVAA AGRQHHTQGS TDSTRSRSSS HSQSSPSLVT RSQPESPSKR PPFKHQYSIS
SASQQSRGSS NGSDHSPKRS MSTSTTTSRS SKRRSKRNFN NNELNLSLNL DLGLDSWTES
LFSSMPSGSP TKPMFSSKEN EDSSSERSKP TSTLPSSSSL SSSPPTRSGL GGGNSFLSSS
TSRDTIKPPP KTEEPYRSVL DRPRPKPPAP VLGVPPRVHV IAEDSSPLSA ASPSTTSFTT
SPVASASPFA STFVTNADPP SPHQPLWTFA GSGESHGMLG VEQDDRQTFP VSPNMMSEYA
PSIASPSPRA GLFDEIAGMV GIQLEDEYDD ENEGKLSPES ARGRGQGQGR TMAQRNQSPA
LSETHSPTIP ISPGFGHLNG DGRVFGNGKI NATSRTGNMG NRISAYRIQD RDKMRSALEA
DAEGYENGWR EEKGQLGEEE DDNMLTTGGK SKSNRNSSRS STSTVTTLTV RNTPAGVKTT
APGKVDTVDA VDAKSDGPAE RPSTVRVSNS SAAQRTESPR PPPPLPLPQP PPVLSPTKSE
FPLTRSKSPA ASLKHPASPQ SSTFGSEEGS AGLSSDVSSR LSGSSVSQLS PTTETDNEDE
DELVYYLESP GPGQTDFNRG VQDYRHLLTS TTDTFGGVYK EDKHIESQVS QDDDDDDDDY
DPDDDVLSSG HTISHGNVIP PPRPTIVISN APVQSGPITA AMQSAITPIT PAQRYPGWLS
EVVKPLEEFI DEPIDPREYY SDLQEIAEGE SGSVFVAKIT ETGNIHKLKL PPLLKAQDAD
NQMRGVTNLV AIKCVAIMPS GSTKLDDLRR ELVLLRGVSH PNILSMDALY VDLVEDSLWV
RMELMERSLA DVIELIDGGL MLQERMIARF TSDIVEALTF LRSHNIAHRD VRSDNLLLNQ
HGFLKLTDFS NAIKLPRERP MAFDPVGVFY WQAPEIRIGP YNALKIDVWS MGATVWEMAQ
ARPPFADSEG VSPADRWPAL DKPQLYSPAF HDFLRLCSEP YHSRPDPDQL TKNPFVKNSC
GRPVIIQLLQ QCTAIEQAIQ QREDNS
//
