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
//