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Database: UniProt
Entry: Q2ULU3
LinkDB: Q2ULU3
Original site: Q2ULU3 
ID   STE20_ASPOR             Reviewed;         848 AA.
AC   Q2ULU3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   08-NOV-2023, entry version 104.
DE   RecName: Full=Serine/threonine-protein kinase ste20;
DE            EC=2.7.11.1;
GN   Name=ste20; ORFNames=AO090003000267;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: MAP4K component of the MAPK pathway required for the mating
CC       pheromone response and the regulation of cell polarity and cell cycle.
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR   EMBL; AP007155; BAE57472.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2ULU3; -.
DR   SMR; Q2ULU3; -.
DR   STRING; 510516.Q2ULU3; -.
DR   EnsemblFungi; BAE57472; BAE57472; AO090003000267.
DR   VEuPathDB; FungiDB:AO090003000267; -.
DR   HOGENOM; CLU_000288_26_1_1; -.
DR   OMA; NPMHVTH; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0044025; F:histone H2BS14 kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0007121; P:bipolar cellular bud site selection; IEA:EnsemblFungi.
DR   GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:EnsemblFungi.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IEA:EnsemblFungi.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblFungi.
DR   GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
DR   GO; GO:0035376; P:sterol import; IEA:EnsemblFungi.
DR   GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
DR   GO; GO:0000011; P:vacuole inheritance; IEA:EnsemblFungi.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015:SF35; SERINE/THREONINE-PROTEIN KINASE PAK; 1.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 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;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Pheromone response; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..848
FT                   /note="Serine/threonine-protein kinase ste20"
FT                   /id="PRO_0000237627"
FT   DOMAIN          228..241
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   DOMAIN          567..818
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..397
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        686
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         573..581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   848 AA;  92889 MW;  CBB9929FD622A95B CRC64;
     MNHDSFSSLK FRRPSSKLHK DPPSIGSRML KSQQSNTSLK RHPSAPVYPR SSASRSREHS
     RTRSNAYGSS TSSLDQNSGG PSPVLANNES GYFSGNHNTT KSRPPHSGRF SLNDQSSDEL
     IGSPFDSRGM LSALQENTAE SDRQPIQKPP TLRSQTTPDT RGLRQSASFT ALHNRMDALV
     NRTDSDRSTN TKRYSDEGNG TKPVGRSKKA SFSSFVNSML GSPRGIKISA PENPVHVTHV
     GYDNQTGQFT GLPKEWQRLL QESGISKKEQ EEHPQTMVDI MRFYEKNAQG DDEVWHKFDH
     AYAHHHPVTT SSSQPSSGGS TPYGTVGQRA SSPTSPRFPQ NHEGSFENPR APPPIPRGAP
     AATQAMSPPV GGLVPNRAPP RPPAAANMTP ARPAPQPPTT ASYATTRPVQ DPWPQFGTIP
     ENAQPFGTPP IPESEPLPSG PQLSRSNSKA NGATAPWVSP AVTPSPTQYQ QQQEQAMATA
     QQAIASKQLD RSQSLRQQQA QQPKQKQATH PTPQQVSPVE DPSAALQQSA RAVPAARPRQ
     RARQSNAMDI RSRLVAICTP GDPTKMYYNL NKIGQGASGG VFTAYHNGTG SCVAIKQMNL
     DLQPKKDLII NEIIVMKDSK HKNIVNFLDS YLHGLDLWVV MEYMEGGSLT DVVTFNIMSE
     GQIAAVCRET LNGLQHLHSK GVIHRDIKSD NILLSLDGNI KLTDFGFCAQ INDSHNKRNT
     MVGTPYWMAP EVVTRKEYGR KVDIWSLGIM AIEMIEGEPP YLTESPLRAL YLIATNGTPT
     IKDEQSLTPV FRDFLHLALK VDPEKRASAH DLLKHPFMSF CAPLSHLAPL VKAARLSRAQ
     EKAQKGGH
//
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