STE20_USTMA
ID STE20_USTMA Reviewed; 746 AA.
AC Q4P5N0; A0A0D1DY77; Q8NK62;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine/threonine-protein kinase SMU1;
DE EC=2.7.11.1;
GN Name=SMU1; Synonyms=STE20; ORFNames=UMAG_12272;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=14871948; DOI=10.1128/ec.3.1.180-189.2004;
RA Smith D.G., Garcia-Pedrajas M.D., Hong W., Yu Z., Gold S.E., Perlin M.H.;
RT "An ste20 homologue in Ustilago maydis plays a role in mating and
RT pathogenicity.";
RL Eukaryot. Cell 3:180-189(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000269|PubMed:14871948}.
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 -!- SEQUENCE CAUTION:
CC Sequence=KIS67485.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF299352; AAM97788.1; -; Genomic_DNA.
DR EMBL; CM003152; KIS67485.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_011391020.1; XM_011392718.1.
DR AlphaFoldDB; Q4P5N0; -.
DR SMR; Q4P5N0; -.
DR STRING; 5270.UM04583P0; -.
DR PRIDE; Q4P5N0; -.
DR EnsemblFungi; KIS67485; KIS67485; UMAG_12272.
DR GeneID; 23568019; -.
DR KEGG; uma:UMAG_12272; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_4_1; -.
DR InParanoid; Q4P5N0; -.
DR OMA; IEISTPY; -.
DR OrthoDB; 757766at2759; -.
DR PHI-base; PHI:2233; -.
DR PHI-base; PHI:382; -.
DR Proteomes; UP000000561; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
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..746
FT /note="Serine/threonine-protein kinase SMU1"
FT /id="PRO_0000237635"
FT DOMAIN 237..250
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 472..723
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 478..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 746 AA; 79535 MW; 139F9B15F3E6194E CRC64;
MSLVPQRSAP PPPSSSANRA ASSLAFQPAS TSNSASPTSS STSTFANGSS SSTTAYRPQP
TINTSVSALQ GPRSGLPAQT GLAFSVSSLS NNPPAASPIT APSSALPWSS QNPAASGSTA
TFPPRPVRSN TAGPDTLHTI SSVSASQTVA PVMVQRSHSS IAAHQASPSL NQSSPTLDAD
GPASLTTQSH FVHPSRDRER SRDGTTTPGS RNTFKSVFGG FVNSMSDVFS AQKKIEISTP
YDPVHLTHVG FNSDTGEFTG LPKEWQQLLQ ESGISRQDQE ANPQAVIDIV AFYQDATQSQ
GGSDVWKKMG AAKGNKAPAT PRTDTSSEDG IYRVAPQPVL YEKPRTAPAP PGITHPNRPS
EFGSPDLRQP PSNASTSSAD TALRPSRSTP APGAAPPPNA KTTSSSNPPP CKPSPASRAP
DAPAAVSAAS KNAKGPGSVP RRRETKKSTI KDSEVIAKLQ AICTDADPTK LYRSLQKIGQ
GASGGVFTAY QVGTNVSVAI KQMNLEQQPK KDLIINEILV MKESRHRNIV NFIDSFLFKG
DLWVVMEYME GGSLTDVVTC NIMTEGQIAA VSREVLEGLR HLHQHGVIHR DIKSDNVLLS
LQGDIKLTDF GFCAQIGESQ AKRTTMVGTP YWMAPEVVTR KEYGPKVDIW SLGIMCIEMV
EGEPPYLNEN PLRALYLIAT NGTPKINNPE NLSNTFKDFL TTSLDVDAER RPDALGMLAH
PFLKRSESLR TLTPLIKAAR EQTRKS
