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
//