PKH3_ASHGO
ID PKH3_ASHGO Reviewed; 726 AA.
AC Q753D9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein kinase PKH3;
DE EC=2.7.11.1;
GN Name=PKH3; OrderedLocusNames=AFR377C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Serine/threonine-protein kinase. {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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AE016819; AAS53748.1; -; Genomic_DNA.
DR RefSeq; NP_985924.1; NM_211279.1.
DR AlphaFoldDB; Q753D9; -.
DR SMR; Q753D9; -.
DR STRING; 33169.AAS53748; -.
DR EnsemblFungi; AAS53748; AAS53748; AGOS_AFR377C.
DR GeneID; 4622194; -.
DR KEGG; ago:AGOS_AFR377C; -.
DR eggNOG; KOG0592; Eukaryota.
DR HOGENOM; CLU_008400_0_0_1; -.
DR InParanoid; Q753D9; -.
DR OMA; CSKRHII; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0000196; P:cell wall integrity MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd05581; STKc_PDK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..726
FT /note="Serine/threonine-protein kinase PKH3"
FT /id="PRO_0000086553"
FT DOMAIN 10..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 629..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 726 AA; 81035 MW; 153038B55DB42AFE CRC64;
MSKRKSPHDF LFREELGHGS YSTVYRVVER SSQHQYAIKI CSKRHIIGEN KVKYVTIEKN
TLNLLGQANH PGIIKLYYTF HDQENLYFVM DLAPGGELLQ LLRRQRVFSE AWARHYMCQL
VDTVEYIHSM GVIHRDLKPE NVLLDKEGRL MIADFGAAYT VGQSDAGSDG DKPATSFVGT
AEYVSPELLL ENKSYYSSDV WALGCMLYQF LQGTPPFRGQ NEMETFEQIV NLDYTWRIPA
NPLAAGLVSK ILVLDPSQRY TLEQIKKHKW FSGVDWNNKE KIWRGSWTIA SESTPRPRVG
YKSRELLDTP IKNIPVVTQR NKKPTKMNTT SSIVEWRKML GLSGNDLGIK ATLGGNGLPI
APFTPTSGIT PDNRGDNAVA PAKTRDAFRP MSSRVISSPH SKPSGRPAAL PLPLQTGTPS
HNVVQQIVVN TPGRTETSSP YVSPTVPVRN AIWKQDWVQL HEIPYSAKYS GLTLAGFSQV
SDTLIADLIS HHANELRTLS RTGILSLDNT GYLSFIEQGR ARPLSRIIDP DLSIYEYQLG
HSTEDDFLIL EKYKQSIWIV WPNKPTSASR RIPIKETWAQ TLSKYKKQVS DEEELSAKLN
RTCVSSWGSR TPSPTYPAEG KTRVAVQPQD IPLPSPAKSS SNSGVSEPIS KIPPRQLVSA
SEQSHKAKSE AHTKKANSYS YIAPNDMVLS SSRYEVLRTA SNNDSKSNGA AVSGASAAFR
TLRVNK
