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Database: UniProt
Entry: A0A0D2AHR1_9PEZI
LinkDB: A0A0D2AHR1_9PEZI
Original site: A0A0D2AHR1_9PEZI 
ID   A0A0D2AHR1_9PEZI        Unreviewed;       654 AA.
AC   A0A0D2AHR1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Serine/threonine-protein kinase gad8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV09_03264 {ECO:0000313|EMBL:KIW06095.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW06095.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW06095.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW06095.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847536; KIW06094.1; -; Genomic_DNA.
DR   EMBL; KN847536; KIW06095.1; -; Genomic_DNA.
DR   RefSeq; XP_016215963.1; XM_016356440.1.
DR   RefSeq; XP_016215964.1; XM_016356441.1.
DR   STRING; 253628.A0A0D2AHR1; -.
DR   GeneID; 27311237; -.
DR   VEuPathDB; FungiDB:PV09_03264; -.
DR   HOGENOM; CLU_000288_120_0_1; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000053259; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd11651; YPK1_N_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          312..569
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          570..641
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          16..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   654 AA;  72480 MW;  8E60711018C7F9BD CRC64;
     MSWKLTKKLK ETHLAPLANT FSRSSSTATI TPEAPQQTPR PSSTDGSPLS QVSTLTAAKD
     PNNVAYSEAN AAAPAAPLKP GILIVTLHEG RGFQLPAHLE EKWQPSHHAG SLSQGGGFSV
     AGSMRPNSSR DPNLAGSYVR GGRPQSSAGA INAAPTIHGR YNSRHLPYAL IDFDKQQVFI
     NAVSGTPENP LWAGESTQYK FDVSRPTDIS ISLYIRNPNA PPNSARTDDA FIGTLKVNPR
     FEEVALGPAQ AQDDAKLSKK DKEKAALARS EQEKEGGQVG TQWIDVQFGA GQMKVGVHFV
     ENRQRSLKIE DFELLKVVGK GSFGKVMQVQ KKDTHRIYAL KTIRKAHIIS RSEVAHTLAE
     RSVLAQINNP FIVPLKFSFQ SPEKLYLVLA FVNGGELFHH LQREQRFDVN RARFYTAELL
     CALECLHGFN VIYRDLKPEN ILLDYTGHIA LCDFGLCKLD MKDEDRTNTF CGTPEYLAPE
     LLTGGGYTKT VDWWTLGVLL YEMLTGLPPF YDENTNEMYR KILTEPLHFP GPEIVPPAAR
     DLLTRLLDRN AEKRLGAKGA SEIKTHHFFH SIDWRKLLDR KYEPTFKPSV VDARDTANFD
     REFTSEPPTD SYVDGPMLSS TMQQQFAGWS YNRPVAGLGD AGGSVKDPSF ENVA
//
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