(data stored in ACNUC7421 zone)

SWISSPROT: Q758E1_ASHGO

ID   Q758E1_ASHGO            Unreviewed;       386 AA.
AC   Q758E1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 109.
DE   SubName: Full=AEL115Cp {ECO:0000313|EMBL:AAS52570.2};
GN   ORFNames=AGOS_AEL115C {ECO:0000313|EMBL:AAS52570.2};
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:AAS52570.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52570.2, 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   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; AE016818; AAS52570.2; -; Genomic_DNA.
DR   RefSeq; NP_984746.2; NM_210100.2.
DR   STRING; 33169.AAS52570; -.
DR   EnsemblFungi; AAS52570; AAS52570; AGOS_AEL115C.
DR   GeneID; 4620933; -.
DR   KEGG; ago:AGOS_AEL115C; -.
DR   HOGENOM; HOG000233033; -.
DR   InParanoid; Q758E1; -.
DR   KO; K04345; -.
DR   OMA; FIVNLRW; -.
DR   Proteomes; UP000000591; Chromosome V.
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; IEA:UniProtKB-KW.
DR   GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   3: Inferred from homology;
DR   PRODOM; Q758E1.
DR   SWISS-2DPAGE; Q758E1.
KW   ATP-binding {ECO:0000256|RuleBase:RU000304, ECO:0000256|SAAS:SAAS00593399};
KW   Kinase {ECO:0000256|SAAS:SAAS00593820};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|SAAS:SAAS00592725}.
FT   DOMAIN          76..330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          331..386
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
SQ   SEQUENCE   386 AA;  44477 MW;  AB53F33B19C2493F CRC64;
     MVETADVTHF VQPRVATEEI VPQQDASSTM PGLSMESRSL CKNIMRAEWA QESGRQLRGR
     KLEGRTTKGK YTLYDFQILR TLGTGSFGRV HLVRSNHNGR FYAMKVLKKH VVVKLKQVEH
     TNDERKMLSV VSHPFIIRMW GTFQDAHQVF MIMDYIEGGE LFSLLRKSQR FPNPVAKFYA
     AEVCLALEYL HSKDIIYRDL KPENILLDKN GHIKLTDFGF AKYVPDVTYT LCGTPDYIAP
     EVVSTKPYNK SVDWWSFGIL IYEMLAGYTP FYDQNTMGTY ENILNAEVKF PPFFNAEVRD
     LLSQLITRDL SKRLGNLQNG SQDVKAHPWF SEVIWDKLLC RNIETPYEPP IHAGQGDTSQ
     YDRYPEEDAN YGALGEDQYQ ALFSDF
//

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