(data stored in ACNUC7421 zone)

SWISSPROT: CLA4_ASHGO

ID   CLA4_ASHGO              Reviewed;         793 AA.
AC   Q9HFW2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Serine/threonine-protein kinase CLA4;
DE            EC=2.7.11.1;
GN   Name=CLA4; OrderedLocusNames=AEL205W;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11082049;
RA   Ayad-Durieux Y., Knechtle P., Goff S., Dietrich F.S., Philippsen P.;
RT   "A PAK-like protein kinase is required for maturation of young hyphae and
RT   septation in the filamentous ascomycete Ashbya gossypii.";
RL   J. Cell Sci. 113:4563-4575(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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   -!- FUNCTION: Required for hyphal maturation and for septation.
CC       {ECO:0000269|PubMed:11082049}.
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   -!- 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;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
DR   EMBL; AF286114; AAG17720.1; -; Genomic_DNA.
DR   EMBL; AE016818; AAS52480.1; -; Genomic_DNA.
DR   RefSeq; NP_984656.1; NM_210009.1.
DR   SMR; Q9HFW2; -.
DR   STRING; 33169.AAS52480; -.
DR   PRIDE; Q9HFW2; -.
DR   EnsemblFungi; AAS52480; AAS52480; AGOS_AEL205W.
DR   GeneID; 4620838; -.
DR   KEGG; ago:AGOS_AEL205W; -.
DR   HOGENOM; HOG000234202; -.
DR   InParanoid; Q9HFW2; -.
DR   KO; K19833; -.
DR   OMA; TKMVGVV; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
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:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:1990872; P:negative regulation of sterol import by negative regulation of transcription from RNA polymerase II promoter; IEA:EnsemblFungi.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0035376; P:sterol import; IEA:EnsemblFungi.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.90.810.10; -; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9HFW2.
DR   SWISS-2DPAGE; Q9HFW2.
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..793
FT                   /note="Serine/threonine-protein kinase CLA4"
FT                   /id="PRO_0000085863"
FT   DOMAIN          56..168
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          173..186
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          498..776
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         504..512
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   COMPBIAS        387..462
FT                   /note="Pro-rich"
FT   ACT_SITE        644
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         545
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   793 AA;  86420 MW;  08B528E3D68491D6 CRC64;
     MSLSAAAREL SESDFQDIGP APKPPPVAYN QTKPLVNYMS QMDLGAKSGG KMRAVQRKKS
     GWVSYKDDGL LSFLWQKRYM VLNDNYLSLY KGDSGREDAV VQIPLTSIVS VSRNQLKQNC
     FEVVRSSDRS GAPAAGAGGD SSKKSVFIAT KTELDLHTWL DSIFSKCPLL SGVSSPTNFT
     HKVHVGFDPE TGSFVGMPFN WEKLLKHSRI TGEDWNNNSA AVIQVLQFYQ EYNNGTATPT
     AQAAAQAAGA PGRPPMLTLS SNSSQASMQQ IASTPPYSGG EMIPQRKAPT PPKPVVTSGS
     AIPSAKGGPN VGVTTSPSVH HQNTQHGKQQ SPTQSGPPKS LPPLHRDEEG PTAPLGNSVS
     SVATKESPTE RLLNNLSETS LMQKQLPAKP VAPPSSVGPV APPLRLQPQR VAPGRPAQPG
     PHAPDTRPGG PNAMKQQHGP PAAASGQLGP DSKKPEGAPG HPTAVAKKKK AGRPTMSNAE
     IMTRLAAVTF NTDPSPFFQM IEKAGQGASG SVYLAQRLKI PPYDENSGVS QHELNDNIGD
     KVAIKQMILS KQPRKELIVN EILVMKDSQH KNIVNFLEAY LKTEDDLWVV MEYMEGGSLT
     DVIENSIGSD ASESPMTEPQ IAYIVRETCQ GLKFLHDKHI IHRDIKSDNV LLDTHGRVKI
     TDFGFCAKLT DKRSKRATMV GTPYWMAPEV VKQREYDEKV DVWSLGIMTI EMLEGEPPYL
     NEEPLKALYL IATNGTPKLK HPELLSLEIK RFLSVCLCVD VRYRASTEEL LHHSFFETSC
     EPEELANLLK WKK
//

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