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
//