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Database: UniProt
Entry: W2SED3_9EURO
LinkDB: W2SED3_9EURO
Original site: W2SED3_9EURO 
ID   W2SED3_9EURO            Unreviewed;       637 AA.
AC   W2SED3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Serine/threonine-protein kinase gad8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1541_01286 {ECO:0000313|EMBL:ETN47096.1};
OS   Cyphellophora europaea CBS 101466.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX   NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN47096.1, ECO:0000313|Proteomes:UP000030752};
RN   [1] {ECO:0000313|EMBL:ETN47096.1, ECO:0000313|Proteomes:UP000030752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN47096.1,
RC   ECO:0000313|Proteomes:UP000030752};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phialophora europaea CBS 101466.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KB822711; ETN47096.1; -; Genomic_DNA.
DR   RefSeq; XP_008711808.1; XM_008713586.1.
DR   AlphaFoldDB; W2SED3; -.
DR   STRING; 1220924.W2SED3; -.
DR   GeneID; 19968625; -.
DR   VEuPathDB; FungiDB:HMPREF1541_01286; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   HOGENOM; CLU_000288_120_0_1; -.
DR   InParanoid; W2SED3; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000030752; 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:UP000030752};
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          14..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..254
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   637 AA;  70784 MW;  F38ABE475204A61A CRC64;
     MSWKLTKKLK ETHLAPLTSG FGRSTSTSTV KAEDETTPQQ ESPSLSTMQS NTSVTSANGI
     AASEAMSNPP VQTTKPGILI VTLHEGKGFS LPQQYQQAFN NYYGGGHAGS VRPNSSYSAN
     SVAGSFSQSN RPVSTHAGIN AAPTIHGRYN SKHLPYALLD FDKLQVFVDA VSGSPENPLW
     AGDNTSFKFD VSRVCELSVQ LYLRNPAARP GVGRSEDIFL GGARIQPRFE EAKPFVPDPK
     KSKKDNDKAE AQHQQQEKQA GQLGAEWVDV QFGTGSIKIG VNYVENRQGS LKIDDFELLK
     VVGRGSFGKV MQVLKKDTGR IYALKTIRKA HIISRSEVAH TLAERSVLAQ INNPFITPLK
     FSFQSPDKLY FVLAFVNGGE LFHHLQKEQR FDINRARFYT AELLCALECL HGFKVIYRDL
     KPENILLDYS GHIALCDFGL CKLDMKDEDR TNTFCGTPEY LAPELLLGHG YTKTVDWWTL
     GVLLYEMLTG LPPFYDENTN EMYRKILQEP LHFPGPEIVP AAAKDLLTKL LDRDPQRRLG
     ASGASEIKAH HFFANIDWRK LLQRKYEPSF KPSVADARDT ANFDKEFTSE VPKDSYVEGP
     VLSQTMQQQF AGWSYNRPVA GLGDAGGSVK DPSFDNI
//
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