ID STE20_ASPFU Reviewed; 815 AA. AC Q4WHP3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 2. DT 22-FEB-2023, entry version 117. DE RecName: Full=Serine/threonine-protein kinase ste20; DE EC=2.7.11.1; GN Name=ste20; ORFNames=AFUA_2G04680; OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC OS A1100) (Aspergillus fumigatus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=330879; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L., RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., RA Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAHF01000008; EAL87562.2; -; Genomic_DNA. DR RefSeq; XP_749600.2; XM_744507.2. DR AlphaFoldDB; Q4WHP3; -. DR SMR; Q4WHP3; -. DR STRING; 746128.CADAFUBP00002120; -. DR EnsemblFungi; EAL87562; EAL87562; AFUA_2G04680. DR GeneID; 3506682; -. DR KEGG; afm:AFUA_2G04680; -. DR VEuPathDB; FungiDB:Afu2g04680; -. DR eggNOG; KOG0578; Eukaryota. DR HOGENOM; CLU_000288_26_1_1; -. DR InParanoid; Q4WHP3; -. DR OMA; PKEWQRM; -. DR OrthoDB; 460351at2759; -. DR Proteomes; UP000002530; 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:0019899; F:enzyme binding; IEA:EnsemblFungi. 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:0043065; P:positive regulation of apoptotic process; IEA:EnsemblFungi. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. 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..815 FT /note="Serine/threonine-protein kinase ste20" FT /id="PRO_0000237626" FT DOMAIN 223..236 FT /note="CRIB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057" FT DOMAIN 534..785 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 300..513 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 49..117 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 355..384 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..496 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 653 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 540..548 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 563 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" SQ SEQUENCE 815 AA; 89671 MW; 6F3C54CF80285724 CRC64; MSNDGFSSLK FRRTSSKLQK DPPSVSSRIL RSQQSNTSLK RHPSAPVHPR SSVTGSREHS RTRSNAYGSS SSSLEQHSGG PSPVLAGGDS NNSFSSKSRP GRFSFNTDPS SDELTGSPFD SRGMLSALEE NTAESEKSPP PQPPTLRSYH TSPDSRGLRQ SASFTALQNR MDTFTQKSEN DQSTNTKRHS DEANGTKVFG RSKKSSFSSF VNSMLGSPRG IKISAPENPV HVTHVGYDNQ TGQFTGLPKE WQRLLQENGI SKKEQEEHPQ TMVDIMRFYE KNARGDDEVW HKFDHAYAHH QPTANTPGSQ RNSPPTSPRF PQNHEGSFEN PRAPPPIPRG APAATQAMSP PIGGLVPSRA PPKPPAPANM IPARPAPQPP VARPPQDAYA NQFSTPPISE SEPLPSEAQR SRSNSKTNGA QPQWAQPGAI ASPAQYQQQQ EQAMAAAQQA IVQNQLERSR SQRQQQSRGP EPKQPTQMGH SQHANDHTTA LQSPQKAQPV PAARPRQRAR QSNAVDVRAR LLAICTPGDP TKLYYNLNKI GQGASGGVYT AYQHGTNNCV AIKQMNLDLQ PKKELIINEI LVMKDSKHKN IVNFLDSYLH GLDLWVVMEY MEGGSLTDVV TFNIMTEGQI AAVCRETLNG LQHLHSKGVI HRDIKSDNIL LSLDGNIKLT DFGFCAQIND SQNKRNTMVG TPYWMAPEVV TRKEYGRKVD IWSLGIMAIE MIEGEPPYLT ESPLRALYLI ATNGTPTIKD EHNLSPVFRD FLHLALKVDP EKRASAHDLL MHPFMSLCSP LTHLAPLVKA ARLSRAQEKA QKGGA //