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Database: UniProt
Entry: A0A1W2TFI6_ROSNE
LinkDB: A0A1W2TFI6_ROSNE
Original site: A0A1W2TFI6_ROSNE 
ID   A0A1W2TFI6_ROSNE        Unreviewed;      1096 AA.
AC   A0A1W2TFI6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SAMD00023353_2100620 {ECO:0000313|EMBL:GAP86811.2};
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:GAP86811.2};
RN   [1] {ECO:0000313|EMBL:GAP86811.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP86811.2};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; DF977466; GAP86811.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TFI6; -.
DR   STRING; 77044.A0A1W2TFI6; -.
DR   OMA; PRRAMHY; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000054516; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06614; STKc_PAK; 1.
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; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:GAP86811.2};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:GAP86811.2}.
FT   DOMAIN          476..489
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          816..1067
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..42
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..154
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..401
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         845
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1096 AA;  119770 MW;  032ACC2FE5794E00 CRC64;
     MDRDMDNSNP NPNQQHLPHH HFHQQPPPLA PPLLPPLPLP SQEQQPLQEQ EQEQQQQQSS
     QRRKLTKKPP SQHHHHQHTH SYSVTGDGRF DAQSLQSKRS SSSLKRAPSA PLQNTTGGGR
     SSNASNSPPR YPPPPPPPSS QTLPHQPPPP TAPSLSSNSQ NSSNNSSNYY NTVSTHSSPA
     LHPGESFPSV PFAPSYQIAA PASALASNTH TSPPTSPHTT FPAASASAGG ATAASGAGVG
     VGSGFGIGIG IGIGVGIDFG TAAPSMSTHH NPNPNNTHNF NYHYQQQQQQ QQQQQQQQQQ
     QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QPQQQQRLSG SQQIPLRPLR SQASEDFVGA
     PFDGDTILSQ FDKAAARAPV PYQAAPQAVR PPPPPPTTSD PRMMSPLLRR SASFSVTNAT
     MSEKSLATRI NEVPVITSKR YSDESKESKG SSSLRKKTGF SSLVSNLVGS PKKPVISAPE
     NPVHVTHVGY DSSTGQFTGL PKEWQRLINE SGIPENAQRE NPQMIADLVT LYKEITERPH
     EDQVLEKFHD VRAPEFRTPS GGTVTSAGIY SPNLAGMSPI TSPPASPRFP IVNNEGTFEN
     PRAPPPVPVP GKSPVPHTAR DHPNLQPSRP APKPPISMQT RMQPQPQLQY PAKDSGIGLS
     QPGEDLPALA YAPSPKDNGV PMLPEELRSR SNSRANGSSP YNPHAPQGPT SQPSPAMQAA
     YQQQLMQQQQ EQAMSQAQAA MKGQLGRSQS TRQAPAQSMG TRTQHPRPPD ANGGGGPGGP
     QGQVQPRSRR TRQSNTMDIA AALKRICSEG DPREIYRGFS KIGQGASGGV YTGNERGSNR
     LVAIKQMNLE QQPKKDLIIN EILVMKDSIH PNIVNFIDSY LCGGELWVIM EYMEGGSLTD
     VVTFNIMTEG QIASVCRETL KGLQHLHSKG VIHRDIKSDN ILLSLEGSIK LTDFGFCAQI
     NEAHNKRTTM VGTPYWMAPE VVTRKEYGRK VDIWSLGIMA IEMIEGEPPY LTESPLRALW
     LIATNGTPQI KEEHNLSTVF RDFLYFALKV DPEKRASAHD LLRHDFMKLC VDLGSLSPLV
     RAAREARQQE KAQKGN
//
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