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 07-JAN-2015, entry version 74. 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. 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., RA Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., RA Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., RA Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., RA Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., RA Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., RA Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., RA Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA 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., RA Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., RA Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., RA White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., RA Machida M., Hall N., 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 CC mating pheromone response and the regulation of cell polarity and CC cell cycle. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. STE20 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CRIB domain. {ECO:0000255|PROSITE- CC ProRule:PRU00057}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. 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 ProteinModelPortal; Q4WHP3; -. DR SMR; Q4WHP3; 222-266, 516-802. DR STRING; 5085.CADAFUAP00003326; -. DR PRIDE; Q4WHP3; -. DR EnsemblFungi; CADAFUAT00003326; CADAFUAP00003326; CADAFUAG00003326. DR GeneID; 3506682; -. DR KEGG; afm:AFUA_2G04680; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000234202; -. DR InParanoid; Q4WHP3; -. DR KO; K04409; -. DR OMA; FNIMTEG; -. DR OrthoDB; EOG708W7W; -. DR Proteomes; UP000002530; Chromosome 2. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:ASPGD. DR GO; GO:0004521; F:endoribonuclease activity; IMP:ASPGD. DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISA:ASPGD. DR GO; GO:0000199; P:activation of MAPK activity involved in cell wall organization or biogenesis; IMP:ASPGD. DR GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:ASPGD. DR GO; GO:0044275; P:cellular carbohydrate catabolic process; IGI:ASPGD. DR GO; GO:0070370; P:cellular heat acclimation; IMP:ASPGD. DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:ASPGD. DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:ASPGD. DR GO; GO:0035690; P:cellular response to drug; IMP:ASPGD. DR GO; GO:0034605; P:cellular response to heat; IMP:ASPGD. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:ASPGD. DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:ASPGD. DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IGI:ASPGD. DR GO; GO:0070055; P:HAC1-type intron splice site recognition and cleavage; IMP:ASPGD. DR GO; GO:0030448; P:hyphal growth; IMP:ASPGD. DR GO; GO:0009405; P:pathogenesis; IMP:ASPGD. DR GO; GO:0043945; P:positive regulation of asexual sporulation resulting in formation of a cellular spore; IMP:ASPGD. DR GO; GO:0006468; P:protein phosphorylation; IMP:ASPGD. DR GO; GO:0010810; P:regulation of cell-substrate adhesion; IMP:ASPGD. DR GO; GO:0048021; P:regulation of melanin biosynthetic process; IMP:ASPGD. DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IMP:GOC. DR GO; GO:0009847; P:spore germination; IMP:ASPGD. DR Gene3D; 3.90.810.10; -; 1. DR InterPro; IPR000095; CRIB_dom. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00285; PBD; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Nucleus; Pheromone response; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 815 Serine/threonine-protein kinase ste20. FT /FTId=PRO_0000237626. FT DOMAIN 223 236 CRIB. {ECO:0000255|PROSITE- FT ProRule:PRU00057}. FT DOMAIN 534 785 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 540 548 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT COMPBIAS 7 111 Ser-rich. FT COMPBIAS 314 405 Pro-rich. FT COMPBIAS 421 511 Gln-rich. FT ACT_SITE 653 653 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 563 563 ATP. {ECO:0000255|PROSITE- FT 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 //