STE20_TALMA
ID STE20_TALMA Reviewed; 642 AA.
AC Q2VWQ3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Serine/threonine-protein kinase pakA;
DE EC=2.7.11.1;
GN Name=pakA; Synonyms=ste20;
OS Talaromyces marneffei (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=37727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Boyce K.J., Hynes M.J., Andrianopoulos A.;
RT "pakA, the ste20 homolog from the dimorphic human pathogen Penicillium
RT marneffei, is essential during yeast but not hyphal growth.";
RL Submitted (MAY-2004) 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 {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}.
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; AY621630; AAU88248.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2VWQ3; -.
DR SMR; Q2VWQ3; -.
DR VEuPathDB; FungiDB:PMAA_030430; -.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..642
FT /note="Serine/threonine-protein kinase pakA"
FT /id="PRO_0000237634"
FT DOMAIN 100..113
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 361..612
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 480
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 367..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 642 AA; 70974 MW; C816C6BAD0F6EF62 CRC64;
MSLKKQQQQS DFSAAPARRP PTLQSYHTSP DPRGKQILRQ SASFTALNNP RMDTALPQIQ
DAPSNSKRNS DEGFGTKPRR KNTFSSFVNS VLGSPRNIKI SAPENPVHVT HVGYDNQTGQ
FTGLPKDWQR MLQASGISKK EQEQHPQTMV DIMRFYERNA AGAGDEEVWH KFDNAILRQG
EYPDGMSPAS ATSPRFPQNH EGSFENPRAA PPPPKPSQSS PVPVLSSTIV PNRVAPKPPT
VGLIPSRPPP QPPVVSNRAP AARPANEPVT TPPIPENEPV FVNAPPVVPS AIQSPVQYQQ
QQERAMAAAQ QAIIDKQLDR SRSQPAAAVA RPRPRTRQST AFDVRAKLQA ICTPGDPTKK
YYNLNKIGQG ASGGVFTAYE TNTNKCVAIK QMNLDLQPKK DLIINEILVM KDSKHKNIVN
FLDSYLHGLD LWVVMEYMEG GSLTDVVTFN IMSEGQIAAV CRETLSGLQH LHSKGVIHRD
IKSDNILLSM DGEIKLTDFG FCAQINDSQN KRNTMVGTPY WMAPEVVTRK EYGRKVDIWS
LGIMAIEMIE GEPPYLTESP LRALYLIATN GTPKIKDEQN LSPVFRDFLH LALRVDPEKR
ASAHDLLKHP FMSICEPLNS LAPLVKSARI SRAQEKAQKG GA
