(data stored in ACNUC7421 zone)

SWISSPROT: Q75BQ3_ASHGO

ID   Q75BQ3_ASHGO            Unreviewed;      1568 AA.
AC   Q75BQ3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 112.
DE   SubName: Full=ACR218Wp {ECO:0000313|EMBL:AAS51444.2};
GN   ORFNames=AGOS_ACR218W {ECO:0000313|EMBL:AAS51444.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51444.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51444.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016816; AAS51444.2; -; Genomic_DNA.
DR   RefSeq; NP_983620.2; NM_208973.2.
DR   STRING; 33169.AAS51444; -.
DR   EnsemblFungi; AAS51444; AAS51444; AGOS_ACR218W.
DR   GeneID; 4619752; -.
DR   KEGG; ago:AGOS_ACR218W; -.
DR   HOGENOM; HOG000248031; -.
DR   InParanoid; Q75BQ3; -.
DR   KO; K12767; -.
DR   OMA; GPFFRPL; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0001324; P:age-dependent response to oxidative stress involved in chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblFungi.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR   GO; GO:1903452; P:positive regulation of G1 to G0 transition; IEA:EnsemblFungi.
DR   GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IEA:EnsemblFungi.
DR   GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IEA:EnsemblFungi.
DR   GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IEA:EnsemblFungi.
DR   GO; GO:0051039; P:positive regulation of transcription involved in meiotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblFungi.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; Q75BQ3.
DR   SWISS-2DPAGE; Q75BQ3.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00593399};
KW   Kinase {ECO:0000256|SAAS:SAAS00593820};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|SAAS:SAAS00592725}.
FT   DOMAIN          682..1106
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1107..1252
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          1438..1551
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          848..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1262..1398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1411..1431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..920
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..985
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1188
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1272..1340
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1397
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1568 AA;  172529 MW;  05A397679A9FB41C CRC64;
     MSEADVWQQA ATAGRGAEQA HREARDADSA STSSVDSVNY LQYLEKATAK NPSVLLELDP
     DGNVKYVSQV WETVVGTRCA EVVGRPVSEV ILGGDQDKLV FQKAVAMMCQ DDRSCRVRFL
     TALGPERAAA DGEAVVELEA QGTLIHDGEI SSLPAHSMWI VKPFYEVDEL DDLPPDFVKR
     LGFGAKLFSH YLQQIEDLEV LDEQELPTPK CELCRVCETL VPAWWLETHS EMCVCEHRIE
     SAVQLIHDEL VELKRLIEDL TGALGQPGAA AEYKGLALPQ PDPSDLGPAK QAPVMLHPSL
     SCPNLSDDEH NPFRRASRSG KDARSLFHHV RFPFKQLSLL SDLCEDAINI NTSELLDADV
     REQDSPYGLL NMQSVTYRFS PNTKNNIDHV TAWDAQLGVD DPAINLLTQD TVELVKRKVE
     MVLRLDNTMR HSLKIKHEVD CQVVNLIKDK IESNKINLQA DETMQDLGQA AQPLFGTSCS
     PSSSRIATPL PQRPQSRILT DSYMASSSVT DLKAVMNVGM PPLDYTSRSN SGSHPLSRSI
     TPRQAITDHS SSAYQLPLTV SNSNTSGGTP VDTKPPTIGT PRASSTSQCN LPKLSTIINL
     TPRRGSPLSS VGMNTPFSTI QRKSTVKSIG EKSPMSSPFM VGSDLLSPEG HLPSATAPKP
     PLSPLLLATN QAKAPTPSIK DYDIIKPISK GAYGSVYLAY KRITGEYFAI KVLRKSDMIA
     KNQVTNVKSE RVIMMVQSEK PYVAKLYATF QNKENLFLVM EYLSGGDLAT LIKMMGNLPD
     KWAKQYITEV IIGVDDMHMS GIIHHDLKPD NLLIDSNGHV KLTDFGLSRI GLIQRHKKHH
     SRHCSIQAVT SKSRHNSLTP DEALEQNGAV TCTPSNLLEG LMVSRRGERS DSISSSHSQL
     DAQTLHRTGS QVSFSIMDIS RSGTPPPPLP APIASLQNQL SQQPGQQQHS HMNQPQQLSL
     APSSSGSMPK RSASVFSSDN SDTSRDFALF HPDEDGSRRF FGTPDYLSPE TILGTGESGA
     SDWWSVGCIL FEFLLGYPPF HASTVEDVFK NILSGQIDWP SFPNKETELE YLSPEAKDLI
     LKLLESNPEE RLGANGAQEI KEHPYFKGIN WSKVYDEEAS FVPTVDNPED TDYFDLRGAD
     LDELLRDNYG EDDLQSTSGM HTPNSSMRTD KKQPSNHSSG NSTPVPKMSI ASVFDPLSQD
     NTSSNSNSPI LKHIPLAIPP HLRERRPSKL NDIQTEFGSF SYRNLSALDK ANKDTINRLK
     SEHYSDHHHV RASPGSLSSS SSEASSKLKA ANPGSSASSP ICNNAGKGTF SRAGSPQMAR
     THSPSRRNSI EQSAAPGAGT ITQRRHTWDH HITLDNDYPP PGPPITKFKS PLSPTQNMGT
     SRSRMQSRTS SQRTSISEIS MEDDERHIAL SKVNTLRSRR RSGRKSSSGT SEVGYNMDVL
     LCEPIPIHRY RLTRDLESLG CSVVAVGTGD EIVRRATSGV RFDLIITTLK LPKIGAVDIT
     RLLRQTTSIN CTTPIVAVTV NYHDAGTHIF DDVLERPIGT EQLRKLVSKY ALFKSQQHED
     TILSDSEM
//

If you have problems or comments...

PBIL Back to PBIL home page