(data stored in SCRATCH zone)

SWISSPROT: Q758J2_ASHGO

ID   Q758J2_ASHGO            Unreviewed;       608 AA.
AC   Q758J2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 127.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0000256|SAAS:SAAS00804148};
DE            EC=2.7.11.1 {ECO:0000256|SAAS:SAAS00804148};
GN   ORFNames=AGOS_AEL230W {ECO:0000313|EMBL:AAS52455.1};
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:AAS52455.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52455.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|SAAS:SAAS01117232};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01117231};
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DR   EMBL; AE016818; AAS52455.1; -; Genomic_DNA.
DR   RefSeq; NP_984631.1; NM_209984.2.
DR   STRING; 33169.AAS52455; -.
DR   EnsemblFungi; AAS52455; AAS52455; AGOS_AEL230W.
DR   GeneID; 4620813; -.
DR   KEGG; ago:AGOS_AEL230W; -.
DR   HOGENOM; HOG000233016; -.
DR   InParanoid; Q758J2; -.
DR   KO; K12761; -.
DR   OMA; IMEDEWF; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:EnsemblFungi.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEA:EnsemblFungi.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblFungi.
DR   GO; GO:0071940; P:fungal-type cell wall assembly; IEA:EnsemblFungi.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:EnsemblFungi.
DR   GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IEA:EnsemblFungi.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:EnsemblFungi.
DR   GO; GO:2000222; P:positive regulation of pseudohyphal growth; IEA:EnsemblFungi.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR   GO; GO:0090606; P:single-species surface biofilm formation; IEA:EnsemblFungi.
DR   InterPro; IPR032270; AMPK_C.
DR   InterPro; IPR028375; KA1/Ssp2_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   InterPro; IPR013896; SNF1_UBA.
DR   Pfam; PF16579; AdenylateSensor; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08587; UBA_2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF103243; SSF103243; 1.
DR   SUPFAM; SSF56112; SSF56112; 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;
DR   PRODOM; Q758J2.
DR   SWISS-2DPAGE; Q758J2.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00804144};
KW   Kinase {ECO:0000256|SAAS:SAAS00804143};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00804159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00804166};
KW   Transferase {ECO:0000256|SAAS:SAAS00804145}.
FT   DOMAIN          39..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..401
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..425
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   608 AA;  68918 MW;  8F4A76748026B60A CRC64;
     MSNANHHHQQ QKMYTGGRNM PHGMHRPGSI PIGQRIGKYQ VIKTLGEGSF GKVKLAHHVS
     TGQKVALKII NKKVLAKSDM QGRIEREISY LRLLRHPHII KLYDVIKSKD EIIMVIEYAG
     NELFDYIVQR DKMSENEARR FFQQIISAVE YCHRHKIVHR DLKPENLLLD EHLNVKIADF
     GLSNIMTDGN FLKTSCGSPN YAAPEVISGK LYAGPEVDVW SSGVILYVML CRRLPFDDES
     IPVLFKNISN GVYSIPKFLS QGAANLIKRM LIVNPLNRIT IHEIMEDEWF KVDLPDYLVP
     VDMKADATSK PGTDDERIDE ALVAVLANTM SYDKDEIYEA LEDPNQTDPT VLEIRDAYLL
     LKENKSLIDG LRSNKQKLDQ LDTFLSQSPP TFESHSQLGP GSGFQAALGG SQHGDQNPHQ
     VKRLASRQRT YQLSFSEQQD EDSTIAILPS SLPQIHRANM VAQGSPAAVK ISPLSNKKSK
     TRWHFGIRSR SYPLDVMGEI YLALKNLGAE WAKPSEEDLW TIRVRWKYDV GTQQNERIPD
     LMRMVIQLFQ IETNNYLVDF KFDGWESSSG NPISSSSTDD EMSTFSAYPF LHLTTRLIME
     LAVNSQSS
//

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