(data stored in ACNUC7421 zone)

SWISSPROT: ISR1_ASHGO

ID   ISR1_ASHGO              Reviewed;         342 AA.
AC   Q758T2;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   11-DEC-2019, entry version 90.
DE   RecName: Full=Serine/threonine-protein kinase ISR1;
DE            EC=2.7.11.1;
GN   Name=ISR1; OrderedLocusNames=AEL330C;
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: Probable serine/threonine protein kinase which may function
CC       redundantly with MPK1-independent branch of the PCK1 pathway.
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; AE016818; AAS52354.2; -; Genomic_DNA.
DR   RefSeq; NP_984530.2; NM_209883.2.
DR   STRING; 33169.AAS52354; -.
DR   EnsemblFungi; AAS52354; AAS52354; AGOS_AEL330C.
DR   GeneID; 4620700; -.
DR   KEGG; ago:AGOS_AEL330C; -.
DR   InParanoid; Q758T2; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; Q758T2.
DR   SWISS-2DPAGE; Q758T2.
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..342
FT                   /note="Serine/threonine-protein kinase ISR1"
FT                   /id="PRO_0000086037"
FT   DOMAIN          59..342
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         65..73
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         84
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   342 AA;  37967 MW;  F18CA377B8C62451 CRC64;
     MSAWASQEAA KEEEAVGDFA RMLERRDAGL LARVLSRAQT GPEAYVRGLW RAEVGLERWR
     LTRVLGCGSV ACVFELGDGA LALKVPTSRR KAPVLLHEVL IYSHLAQQAG GRLAERHVVP
     FHGVAAVTRR EYRRLRGGEV VPALVLERMD TTLEAVHRRA AVSKGQWWRY ARDLVAALQF
     LRESCVVHGD IKTANVLVRG QDAFLADFTS AAVCDAAPEP LTTTLEYCAP GLIGGGQPTH
     STDVYAAGLC LLALITRFEP FRELSMMKSH SSAPTHSLHE TQWLMNAISK GDPIKYNVLS
     QDLYDRWAEE LHFLRRFFVP AAQDALSRWL AESNARVAEH AF
//

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