HAL5_ASHGO
ID HAL5_ASHGO Reviewed; 683 AA.
AC Q757X8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable serine/threonine-protein kinase HAL5-like;
DE EC=2.7.11.1;
GN OrderedLocusNames=AEL118C;
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 -!- 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. CAMK Ser/Thr
CC protein kinase family. NPR/HAL subfamily. HAL5 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016818; AAS52567.1; -; Genomic_DNA.
DR RefSeq; NP_984743.1; NM_210097.1.
DR AlphaFoldDB; Q757X8; -.
DR SMR; Q757X8; -.
DR STRING; 33169.AAS52567; -.
DR EnsemblFungi; AAS52567; AAS52567; AGOS_AEL118C.
DR GeneID; 4620930; -.
DR KEGG; ago:AGOS_AEL118C; -.
DR eggNOG; KOG0590; Eukaryota.
DR HOGENOM; CLU_016904_0_0_1; -.
DR InParanoid; Q757X8; -.
DR OMA; VGSEPYV; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
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:0030003; P:cellular cation homeostasis; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblFungi.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; 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..683
FT /note="Probable serine/threonine-protein kinase HAL5-like"
FT /id="PRO_0000333581"
FT DOMAIN 364..670
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 521
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 370..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 683 AA; 75760 MW; BA2D3C0684F59671 CRC64;
MPQQVRLSRE NSVKRSRSLT KSFRGLFKFN SPGSPPSSAA TSDSSEMSGA QGGRGNGLLG
GRTKKASISP KSEAQFTQRN KSAESVVSDE GVAMVASAGA QFYGRGKHES SPNVLMTGGE
EAARAAGRAS AESIALSEGG PPSIDTKLER VTPSLIYPQN GRAKHSSQRS RSASVGRNKE
RGGPTPAPIG SIREEESKKA HKCIIQQEHF TVDENGNHQH SLKVLPLIVQ DPESHKPKLF
SFSAVFKSHK NGEDEELSDA FSILPDYSTV LEKTLVEPLS EVKIFSEAAQ PDENGGRTEA
NQPKDMPKIV NKHAAIGNEE LKLINNLSET IHVGMQGPDK HSSPPQPFTC KATKSKQVLA
EKYGKCIGMI GQGAYGTVWV TCRSLPQDNQ TETHYPTETY ERNGKLFYAI KEIKPRADEP
NEKFSTRLTS EFVIGHSLSG GAGGTKRLTS HPNILKVLDL MQAHDVFIEV FEFCPSGDLF
SLLTRSSKTG SGLHPLEADC FMKQLLNGVR YMHDHGVAHC DLKPENILFT PNGTLKLCDF
GSSSVFQTAW EKRVHFQTGA VGSEPYVAPE EFIPKREYDT RLVDCWSCGI IYCTMVLGHY
LWKIAIKEKD QIYSAFLDDM TTRGEYYVFE NMRHVNQEVN RCRKMCLYNI FQWDPKKRIT
IPKLLDTPWM RRTKCCVNYR AAI
