(data stored in ACNUC7421 zone)

SWISSPROT: Q75CB5_ASHGO

ID   Q75CB5_ASHGO            Unreviewed;       709 AA.
AC   Q75CB5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE            EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN   ORFNames=AGOS_ACL006W {ECO:0000313|EMBL:AAS51222.2};
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:AAS51222.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51222.2, 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   -!- 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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR   EMBL; AE016816; AAS51222.2; -; Genomic_DNA.
DR   RefSeq; NP_983398.2; NM_208751.2.
DR   STRING; 33169.AAS51222; -.
DR   EnsemblFungi; AAS51222; AAS51222; AGOS_ACL006W.
DR   GeneID; 4619523; -.
DR   KEGG; ago:AGOS_ACL006W; -.
DR   HOGENOM; HOG000248546; -.
DR   InParanoid; Q75CB5; -.
DR   KO; K06660; -.
DR   OMA; FEVDTWS; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:EnsemblFungi.
DR   GO; GO:0097431; C:mitotic spindle pole; IEA:EnsemblFungi.
DR   GO; GO:0044732; C:mitotic spindle pole body; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019237; F:centromeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:EnsemblFungi.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:EnsemblFungi.
DR   GO; GO:0051455; P:attachment of spindle microtubules to kinetochore involved in homologous chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0031670; P:cellular response to nutrient; IEA:EnsemblFungi.
DR   GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:EnsemblFungi.
DR   GO; GO:1990813; P:meiotic centromeric cohesion protection; IEA:EnsemblFungi.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:1904750; P:negative regulation of protein localization to nucleolus; IEA:EnsemblFungi.
DR   GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IEA:EnsemblFungi.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblFungi.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:EnsemblFungi.
DR   GO; GO:0010696; P:positive regulation of mitotic spindle pole body separation; IEA:EnsemblFungi.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:EnsemblFungi.
DR   GO; GO:0110083; P:positive regulation of protein localization to cell division site involved in mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:EnsemblFungi.
DR   GO; GO:0031031; P:positive regulation of septation initiation signaling; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR   GO; GO:1903353; P:regulation of nucleus organization; IEA:EnsemblFungi.
DR   GO; GO:1902542; P:regulation of protein localization to mitotic spindle pole body; IBA:GO_Central.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:EnsemblFungi.
DR   GO; GO:0090306; P:spindle assembly involved in meiosis; IEA:EnsemblFungi.
DR   GO; GO:0070194; P:synaptonemal complex disassembly; IEA:EnsemblFungi.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   Gene3D; 3.30.1120.30; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_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   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
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; Q75CB5.
DR   SWISS-2DPAGE; Q75CB5.
KW   ATP-binding {ECO:0000256|RuleBase:RU361162};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|RuleBase:RU361162};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU361162};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW   Transferase {ECO:0000256|RuleBase:RU361162}.
FT   DOMAIN          73..328
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          522..589
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          621..694
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          391..411
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..24
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..57
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   709 AA;  81200 MW;  B2A687F124A67E13 CRC64;
     MSAPLQIVNE KQLNTRSNAN VHTPVKQHHA KRADLERGHH DNNRQPPQKK KKEKLSALCK
     TPPSLIKTKG RDYHRGMFLG EGGFARCFQM KDDSGKVFAA KTVAKISIKS EKTRKKLLSE
     IQIHKSMKHP NIVQFTDCFE DDTNVYILLE ICPNGSLMDL LKQRKQLTEP EVRFFTTQIV
     GAIKYMHSRR IIHRDLKLGN IFFDKHFNLK IGDFGLAAVL ANDRERKYTI CGTPNYIAPE
     VLTGKHTGHS FEVDIWSIGV MIYALLIGKP PFQAKEVNTI YERIKVCDFS FPKDKPISSE
     AKVLIKDILS LDPLERPSLA EIMEYVWFRN VFPARINGDI LNFVPEFHDL DLQESLINFK
     NCMAKCGLMN PSAAAAAVAA KEYDQRLPSY SKNSNNNNNQ INQNNEQLSE AKKSVLPQSL
     SPGGTRYKYK EIVDVETQRK LNDLAREARI RRAQQSMLKQ SLVASSTNFI KSEISLRILA
     SECHMTLNGL LEAEAQKRMG GLPRSRLPEI QHPIVVTKWV DYSNKHGFAY QLSTDDIGVL
     FNNGTTVLNL ADAEEFWYIS YDDREGWVAN HYSLAEKPKE LNRHLEVVDF FSNYMNSNLS
     RISTFVRESY HKDDVFLRRF TRYKQFVMFE LSDGTFQFNF KDHHKFAISQ SGKLTTYISP
     DRQSFTFPTV EILKAEKIPG HPELGFMEKF AMIKEGLKQK SAIVSVAQQ
//

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