STE20_YARLI
ID STE20_YARLI Reviewed; 1125 AA.
AC Q6C3D7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine/threonine-protein kinase STE20;
DE EC=2.7.11.1;
GN Name=STE20; OrderedLocusNames=YALI0F00572g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382132; CAG77627.1; -; Genomic_DNA.
DR RefSeq; XP_504825.1; XM_504825.1.
DR AlphaFoldDB; Q6C3D7; -.
DR SMR; Q6C3D7; -.
DR STRING; 4952.CAG77627; -.
DR EnsemblFungi; CAG77627; CAG77627; YALI0_F00572g.
DR GeneID; 2908251; -.
DR KEGG; yli:YALI0F00572g; -.
DR VEuPathDB; FungiDB:YALI0_F00572g; -.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; Q6C3D7; -.
DR OMA; SELWSER; -.
DR Proteomes; UP000001300; Chromosome F.
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..1125
FT /note="Serine/threonine-protein kinase STE20"
FT /id="PRO_0000237636"
FT DOMAIN 388..401
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 844..1095
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 50..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 963
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 850..858
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 873
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1125 AA; 119340 MW; 9C60CDBE3E9F2C0E CRC64;
MCFNLPLPHL PPYLPFITSS FFFFSFFPFS LTNTDAPIEF ETTIIDPAEQ TSHHVSESRP
THLSFSSSSE SPRDQSREQS SRDVSASPVF PKRQQSLLRL DEHMAGGAGE SRDEPHGEPS
DDAHKSRASS TSSSSSFGQS WNQSSASQRA SVSSMGGVDV AQKRPGPSSG GLTGASAASG
MPPAPTSQAP AIPPITPQMQ TGAFEQYTPQ TAPPIPTQSQ LGQDGRKRAA TLDRQQQYVP
SYGYSSPANG ERGGPTGGTP GGTPMSPGGV AHVTSPGGGP SAASVHRSFS TTTPHAPTKN
SRRIVSTSAA PMRKQIDDAN AALGRAVDPS RDSQPMQSRD KRSKSISSRG GMKGVFSNLV
SSMGTLSRKN TTVRRSESDT SAPSTPKISG PYDAKHVTHV GFNFDTGEFT GLPKPWQKLL
SESGISKVEA EQHPQAVMDI MAFYTDQKDD GVWQKFGGAN QAGSGATATT PYNAQNGFSP
IASPGATTPT LGALNLGTPL SVDLDTEGDT STSTGGGGGV GGGDYFAKPR SAPFPPAAGG
GSASSSTATL GTGATASGGA TTATPAIPSR DRTRESSLSS GTSNQGPPVT PLALSQSRQN
LREEAPATPE EKPLAHFVAS RKAPRPPSAS PKKTGGAGAS GDSGAGAAPP SAAPKSPPPR
PPPAPPLGVP SVHAPNSEYR QKMITQLEAF NAKRQQERAE RHAQKQKLAA AHAQAVQRQQ
RQQQQQQQQQ QQQQSAQQGA MPSVMPQMQH GSMQQAQQSV SGGSSGLTPQ QKQLIQQKQL
LELQKATGGQ VGGPVTSSTQ QVLSNPAAAA AASQRKREQR LRKDQQVVAR LNQICTPGDP
TKLYRNLVKI GQGASGGVFT AYEVGSNLSV AIKQMNLEHQ PKKELIINEI LVMKDSKHKN
IVNFIDSYLH GGDLWVVMEY MEGGSLTDVV TYNMMTESQI GAVCRETLLG LQHLHSKGVI
HRDIKSDNVL LSMRGEIKLT DFGFCAQINE SNLKRTTMVG TPYWMAPEVV SRKEYGSKVD
IWSLGIMSIE MIEGEPPYLN ESPLRALYLI ATNGTPQLKE PDALSTIFKA FLAWALQVSA
DQRASASELL KHEFLLTADD VSTLAPLVKA ARMAKIQEKN EKAQR
