(data stored in SCRATCH zone)

SWISSPROT: Q75CR9_ASHGO

ID   Q75CR9_ASHGO            Unreviewed;       219 AA.
AC   Q75CR9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK6 {ECO:0000256|HAMAP-Rule:MF_03173};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03173};
DE   AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
GN   ORFNames=AGOS_ACL150W {ECO:0000313|EMBL:AAS51078.1};
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 {ECO:0000313|EMBL:AAS51078.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51078.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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., Pohlmann 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] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
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: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC       catalyzes the reversible transfer of the terminal phosphate group
CC       between nucleoside triphosphates and monophosphates. Has also ATPase
CC       activity. May be involved in rRNA maturation and transcription
CC       regulation. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03173};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03173}.
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DR   EMBL; AE016816; AAS51078.1; -; Genomic_DNA.
DR   RefSeq; NP_983254.1; NM_208607.1.
DR   STRING; 33169.AAS51078; -.
DR   EnsemblFungi; AAS51078; AAS51078; AGOS_ACL150W.
DR   GeneID; 4619374; -.
DR   KEGG; ago:AGOS_ACL150W; -.
DR   HOGENOM; HOG000224472; -.
DR   InParanoid; Q75CR9; -.
DR   KO; K18532; -.
DR   OMA; VFVVTCP; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12595:SF0; PTHR12595:SF0; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CR9.
DR   SWISS-2DPAGE; Q75CR9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03173};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   NP_BIND         17..22
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   REGION          38..61
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   REGION          113..123
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   REGION          176..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..200
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..219
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         84
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         110
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         114
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ   SEQUENCE   219 AA;  24502 MW;  55908712874A5A55 CRC64;
     MQQTRCRPNI LVSGTPGCGK STTCELLQRH LPDYQYFNIS DFAREHNCYD GYDEARKSHI
     VDEDRLLDEL EPLLRRGGAI VDWHVNDIFP ERLIDLVVVL RCDNAILHDR LQKRGYHSSK
     IEENIDAEIM GVVLQDALDS YVREIVVELQ SDDTEQMQQN VDRIAAWEAN WVSEHPDGVS
     NALQQHAGSD ASSSEADSDG VSDAGDSDGD GDGDSTQDN
//

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