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Serine/threonine-protein kinase STE20 (EC 2.7.11.1)

 STE20_KLULA             Reviewed;         989 AA.
Q6CVA2;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
10-OCT-2018, entry version 97.
RecName: Full=Serine/threonine-protein kinase STE20;
EC=2.7.11.1;
Name=STE20; OrderedLocusNames=KLLA0B13607g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: MAP4K component of the MAPK pathway required for the
mating pheromone response and the regulation of cell polarity and
cell cycle. Phosphorylates histone H2B to form H2BS10ph (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CR382122; CAH02530.1; -; Genomic_DNA.
RefSeq; XP_452137.1; XM_452137.1.
ProteinModelPortal; Q6CVA2; -.
SMR; Q6CVA2; -.
STRING; 284590.XP_452137.1; -.
PRIDE; Q6CVA2; -.
EnsemblFungi; CAH02530; CAH02530; KLLA0_B13607g.
GeneID; 2897018; -.
KEGG; kla:KLLA0_B13607g; -.
eggNOG; KOG0578; Eukaryota.
eggNOG; ENOG410XP4K; LUCA.
HOGENOM; HOG000234202; -.
InParanoid; Q6CVA2; -.
KO; K04409; -.
OMA; FNIMTEG; -.
OrthoDB; EOG092C2E30; -.
Proteomes; UP000000598; Chromosome B.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044025; F:histone kinase activity (H2B-S14 specific); IEA:EnsemblFungi.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:EnsemblFungi.
GO; GO:0007121; P:bipolar cellular bud site selection; IEA:EnsemblFungi.
GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
GO; GO:1990872; P:negative regulation of sterol import by negative regulation of transcription from RNA polymerase II promoter; IEA:EnsemblFungi.
GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IEA:EnsemblFungi.
GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblFungi.
GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IEA:EnsemblFungi.
GO; GO:0035376; P:sterol import; IEA:EnsemblFungi.
GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
GO; GO:0000011; P:vacuole inheritance; IEA:EnsemblFungi.
CDD; cd01093; CRIB_PAK_like; 1.
Gene3D; 3.90.810.10; -; 1.
InterPro; IPR000095; CRIB_dom.
InterPro; IPR036936; CRIB_dom_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033923; PAK_BD.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00786; PBD; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00285; PBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50108; CRIB; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Nucleus; Pheromone response; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 989 Serine/threonine-protein kinase STE20.
/FTId=PRO_0000237631.
DOMAIN 404 417 CRIB. {ECO:0000255|PROSITE-
ProRule:PRU00057}.
DOMAIN 698 949 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 704 712 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 817 817 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 727 727 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SEQUENCE 989 AA; 108623 MW; 47CD34A2B4A6AF37 CRC64;
MTDTGYTEEL LPGTFDALSV RENGGNTESD TSSIRKSQNQ DSKQEDVHRE NLSVQTLEDH
TEVTETREQS VSKDLFDLPR APASLDVKGL QESDEDHYVK DLSDYKSMDP GKPGTVPTNV
SEIFNSNQPT LDEPIQFTRV SSSSVLSESI SEGDADLISH LEGKVEEGNN LTSKETPGTI
ESIVGDKTMS TIEGSSQNIG RISTGGRMTP DLSLMGGALE TSSDFLNSTQ TSNSPKITTP
ITEVDANDVY ESPLNEILSS TDSFNKASTA SADHSKHVSV HEVIPEEEPH PETTNEDPPI
KTPVMVNNFF ENQTPVSESR SPFRTISSPF SSLRKNVKSQ HGTPDHSQRN SNSSTSSNDV
KRKTGTKKKG VFSTFVQNIK RNSHSEKRIS SGSGNGSGNN AFKISTPYNA KHVYHVGVDS
KTGEYTGLPN EWEKLLTSSG ISMKEQQQHP QAVMDIVKFY QDVTENSGEE KVFKTFKVGG
GSGANIASTP SFRTPSTASV QKFETPQMQT DATFPNENND TPYSSNLQGP LLTNDFSETV
NNEKFIPTRP APKPQGSSTV SRRVEIPSPI NSLGHGTPKV QRSDTQSSSI FSFKKMPTLK
SEQPLPPIPK AAEKPANLLP ARAAPTPPKP AIPTTPEQSS IPAIPSGLAV EVKEESNTSN
VQTRKAQEKK REERKRKNQQ IQSKLTEICT TGDPSKLYKN LIKIGQGASG GVYTAYELGT
NASVAIKQMN LEKQPKKELI VNEILVMKGS KHNNIVNFID SYLFRGDLWV VMEYMEGGSL
TDVVTHCILT EGQIGAVSRE TLKGLQFLHS KGVIHRDIKS DNILLSMNGD IKLTDFGFCA
QINEVNLKRT TMVGTPYWMA PEVVSRKEYG PKVDIWSLGI MIIEMIEGEP PYLNETPLRA
LYLIATNGTP KLKDPGNLSH KMAMFLNWCL MVDPEDRGTA ADLLEDPFIT EIAEENTSLA
PLVKLARMKK LAESMEDDEN DEDKYDEQS


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