STE20_NEUCR
ID STE20_NEUCR Reviewed; 954 AA.
AC Q7RZD3; V5ILJ2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Serine/threonine-protein kinase ste20;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine protein kinase 4;
GN Name=stk-4; Synonyms=ste20; ORFNames=NCU03894;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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 Phosphorylates histone H2B to form H2BS10ph (By similarity).
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; CM002241; ESA42235.1; -; Genomic_DNA.
DR EMBL; CM002241; ESA42236.1; -; Genomic_DNA.
DR RefSeq; XP_011394882.1; XM_011396580.1.
DR RefSeq; XP_011394883.1; XM_011396581.1.
DR AlphaFoldDB; Q7RZD3; -.
DR SMR; Q7RZD3; -.
DR STRING; 5141.EFNCRP00000003720; -.
DR PRIDE; Q7RZD3; -.
DR EnsemblFungi; ESA42235; ESA42235; NCU03894.
DR EnsemblFungi; ESA42236; ESA42236; NCU03894.
DR GeneID; 3873759; -.
DR KEGG; ncr:NCU03894; -.
DR VEuPathDB; FungiDB:NCU03894; -.
DR HOGENOM; CLU_000288_26_1_1; -.
DR InParanoid; Q7RZD3; -.
DR OMA; PKEWQRM; -.
DR Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 kinase activity (H2B-S14 specific); IEA:EnsemblFungi.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
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 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Pheromone response; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..954
FT /note="Serine/threonine-protein kinase ste20"
FT /id="PRO_0000237632"
FT DOMAIN 334..347
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 674..925
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 793
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 680..688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 954 AA; 103792 MW; 7EAA07F4B73DDAF0 CRC64;
MDGQLSLLSP TSSSSTSHSR KRLTKKQRPP SANHRTSSSF NVESLRIDAQ SLDSKRSASS
LRQGPNCNQS PSLARTVSVP VSVPSNAPAH TKASDLSLPR SHTTRSQSAN RPYNPTQTIP
TNRFILSPAS SSQPQTQSPP YPSAVASTTV TSSRNKDTSK QYDPLDSCIG SFDQNKLSTD
ELIGAPFDGN AILSRIEATK LSAAPAPTST TTIAHSNNIS PRRVAPPPPP PPPALSRSNT
DSKAARSSKP SKSPKSTISN KTMGASSFRH SASFSSAEQL PPSEKPSKSE SSSSSNKRHS
GDGKESRVPG MLRKKSGFSG FMNSLVGSPK KPLISAPENP VHVTHVGYDS NTGQFTGLPK
EWQRLISESG ITEKDRREHP QILVDVLTFY KETTEKPQED QQLEKFHDAR ATDFRSPPVT
GTAPLVLQTG VGYAHGPMSP MISPPASPRF PQVGHEGSFE NPRAPPPVPK GPGPLPAKDI
NLIPSRPAPK PPAISTRPLV PPASLPAKDS GIGMPPPGDE APMPYLPPKD NVQHMYQEEH
RNRSRSNSRT NGAAPFSPVQ ASPLHPIATA NQTAAYQQQL LQHQQEQAMA QAQAAMSGQL
SRAASKRQQP TPPTSQHQHP RQPDINGAPR MPQTQGAAPQ ASARPRHRPR QSNAIDVVAS
LKRICSDGDP REIYRGFTKI GQGASGGVYT GHERGSNRLV AIKQMNLEQQ PKKDLIINEI
LVMKESSHPN IVNFIDSYLC AGELWVVMEY MEGGSLTDVV TFNIMTEGQI ASVCRETLRG
LQHLHSKGVI HRDIKSDNIL LSMEGNIKLT DFGFCATINE AQSKRTTMVG TPYWMAPEVV
TRKEYGRKVD IWSLGIMAIE MIEGEPPYLT ESPLRALWLI ATNGTPHIKD EQSLSPVFRD
FLYFALKVDP EKRASAHDLL RHDFMNKCVD LSTLAPLVRA AREARAQEKA RKGQ
