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Database: UniProt
Entry: A0A0D1XN46_EXOME
LinkDB: A0A0D1XN46_EXOME
Original site: A0A0D1XN46_EXOME 
ID   A0A0D1XN46_EXOME        Unreviewed;       638 AA.
AC   A0A0D1XN46;
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=PV10_06924 {ECO:0000313|EMBL:KIV89531.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV89531.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV89531.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV89531.1,
RC   ECO:0000313|Proteomes:UP000054302};
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 Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847524; KIV89531.1; -; Genomic_DNA.
DR   RefSeq; XP_016221105.1; XM_016371773.1.
DR   AlphaFoldDB; A0A0D1XN46; -.
DR   STRING; 212818.A0A0D1XN46; -.
DR   GeneID; 27324769; -.
DR   VEuPathDB; FungiDB:PV10_06924; -.
DR   HOGENOM; CLU_000288_120_0_1; -.
DR   OMA; YLVMEFE; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000054302; 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:UP000054302};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          296..553
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          554..625
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          16..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          235..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   638 AA;  70788 MW;  ABE45FCA78EBC0E6 CRC64;
     MSWKLTKKLK ETHLAPLTSG FGRSTSTSTI KGEEHPANSA DTPDLTTTPS NVSVSSNNGI
     AASESLASPP VQQTKPGILI VTLHEGRAFS LPQQYQSVFS SHYGSPGVSG SVRPSSSYAA
     GSIAGSYAQS NRPVSTHGGI NSAPTIHGRY NSKYLPYALL DFDKLQVFVD AVSGTPENPL
     WAGDNTSFKF DVSRVCELSV QLYLRNPAAR PGAGRSEDIF LGGARVTPRF EEARTFVPDP
     KKSKKENEKD EANFHSEKQA GQLGTEWLDV QFGTGTIKVG VNYVETRKGS LTMDDFELLK
     VVGRGSFGKV MQVLKKDTGR IYALKTIRKA HIISRSEVAH TLAERSVLAQ INNPFITPLK
     FSFQSPDKLY FVLAFVNGGE LFHHLQKEQR FDINRSRFYT AELLCALECL HGFKVIYRDL
     KPENILLDYT GHIALCDFGL CKLDMKDEDR TNTFCGTPEY LAPELLLGHG YTKTVDWWTL
     GVLLYEMLTG LPPFYDENTN EMYRKILQEP LHFPGPEIVP AAAKDLLQKL LDRNPERRLG
     AGGAAEIKAH HFFAGIDWRK LLQRKYEPSF KPNVVDARDT ANFDKEFTSE VPKDSFVEGP
     MLSQTMQQQF AGWSYNRPVA GLGDAGGSVR DPSFDQLH
//
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