(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 102.
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}.
DR   EMBL; AE016818; AAS52567.1; -; Genomic_DNA.
DR   RefSeq; NP_984743.1; NM_210097.1.
DR   STRING; 33169.AAS52567; -.
DR   EnsemblFungi; AAS52567; AAS52567; AGOS_AEL118C.
DR   GeneID; 4620930; -.
DR   KEGG; ago:AGOS_AEL118C; -.
DR   HOGENOM; HOG000112846; -.
DR   InParanoid; Q757X8; -.
DR   KO; K08286; -.
DR   OMA; ECDIENA; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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;
DR   PRODOM; Q757X8.
DR   SWISS-2DPAGE; Q757X8.
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   NP_BIND         370..378
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        521
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         411
FT                   /note="ATP"
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
//

If you have problems or comments...

PBIL Back to PBIL home page