CLA4_ASHGO
ID CLA4_ASHGO Reviewed; 793 AA.
AC Q9HFW2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Serine/threonine-protein kinase CLA4;
DE EC=2.7.11.1;
GN Name=CLA4; OrderedLocusNames=AEL205W;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=11082049; DOI=10.1242/jcs.113.24.4563;
RA Ayad-Durieux Y., Knechtle P., Goff S., Dietrich F.S., Philippsen P.;
RT "A PAK-like protein kinase is required for maturation of young hyphae and
RT septation in the filamentous ascomycete Ashbya gossypii.";
RL J. Cell Sci. 113:4563-4575(2000).
RN [2]
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 [3]
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: Required for hyphal maturation and for septation.
CC {ECO:0000269|PubMed:11082049}.
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. 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; AF286114; AAG17720.1; -; Genomic_DNA.
DR EMBL; AE016818; AAS52480.1; -; Genomic_DNA.
DR RefSeq; NP_984656.1; NM_210009.1.
DR AlphaFoldDB; Q9HFW2; -.
DR SMR; Q9HFW2; -.
DR STRING; 33169.AAS52480; -.
DR EnsemblFungi; AAS52480; AAS52480; AGOS_AEL205W.
DR GeneID; 4620838; -.
DR KEGG; ago:AGOS_AEL205W; -.
DR eggNOG; KOG0578; Eukaryota.
DR HOGENOM; CLU_000288_26_2_1; -.
DR InParanoid; Q9HFW2; -.
DR OMA; RYNPSRP; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005933; C:cellular bud; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0120157; C:PAR polarity complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:EnsemblFungi.
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:0010629; P:negative regulation of gene expression; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0019236; P:response to pheromone; IEA:EnsemblFungi.
DR GO; GO:0031106; P:septin ring organization; IEA:EnsemblFungi.
DR GO; GO:0035376; P:sterol import; IEA:EnsemblFungi.
DR GO; GO:0000011; P:vacuole inheritance; IEA:EnsemblFungi.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 2.30.29.30; -; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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..793
FT /note="Serine/threonine-protein kinase CLA4"
FT /id="PRO_0000085863"
FT DOMAIN 56..168
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 173..186
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 498..776
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 8..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 644
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 504..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 793 AA; 86420 MW; 08B528E3D68491D6 CRC64;
MSLSAAAREL SESDFQDIGP APKPPPVAYN QTKPLVNYMS QMDLGAKSGG KMRAVQRKKS
GWVSYKDDGL LSFLWQKRYM VLNDNYLSLY KGDSGREDAV VQIPLTSIVS VSRNQLKQNC
FEVVRSSDRS GAPAAGAGGD SSKKSVFIAT KTELDLHTWL DSIFSKCPLL SGVSSPTNFT
HKVHVGFDPE TGSFVGMPFN WEKLLKHSRI TGEDWNNNSA AVIQVLQFYQ EYNNGTATPT
AQAAAQAAGA PGRPPMLTLS SNSSQASMQQ IASTPPYSGG EMIPQRKAPT PPKPVVTSGS
AIPSAKGGPN VGVTTSPSVH HQNTQHGKQQ SPTQSGPPKS LPPLHRDEEG PTAPLGNSVS
SVATKESPTE RLLNNLSETS LMQKQLPAKP VAPPSSVGPV APPLRLQPQR VAPGRPAQPG
PHAPDTRPGG PNAMKQQHGP PAAASGQLGP DSKKPEGAPG HPTAVAKKKK AGRPTMSNAE
IMTRLAAVTF NTDPSPFFQM IEKAGQGASG SVYLAQRLKI PPYDENSGVS QHELNDNIGD
KVAIKQMILS KQPRKELIVN EILVMKDSQH KNIVNFLEAY LKTEDDLWVV MEYMEGGSLT
DVIENSIGSD ASESPMTEPQ IAYIVRETCQ GLKFLHDKHI IHRDIKSDNV LLDTHGRVKI
TDFGFCAKLT DKRSKRATMV GTPYWMAPEV VKQREYDEKV DVWSLGIMTI EMLEGEPPYL
NEEPLKALYL IATNGTPKLK HPELLSLEIK RFLSVCLCVD VRYRASTEEL LHHSFFETSC
EPEELANLLK WKK
