KAD6_YEAST
ID KAD6_YEAST Reviewed; 197 AA.
AC Q12055; D6VRI5; E9P8W4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog FAP7 {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=POS9-activating factor 7;
GN Name=FAP7; OrderedLocusNames=YDL166C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-19 AND SER-21.
RX PubMed=10692169; DOI=10.1046/j.1365-2958.2000.01768.x;
RA Juhnke H., Charizanis C., Latifi F., Krems B., Entian K.-D.;
RT "The essential protein fap7 is involved in the oxidative stress response of
RT Saccharomyces cerevisiae.";
RL Mol. Microbiol. 35:936-948(2000).
RN [5]
RP FUNCTION.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, INTERACTION WITH RPS14B, AND MUTAGENESIS OF LYS-20; ASP-82 AND
RP HIS-84.
RX PubMed=16287850; DOI=10.1128/mcb.25.23.10352-10364.2005;
RA Granneman S., Nandineni M.R., Baserga S.J.;
RT "The putative NTPase Fap7 mediates cytoplasmic 20S pre-rRNA processing
RT through a direct interaction with Rps14.";
RL Mol. Cell. Biol. 25:10352-10364(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183; SER-188 AND SER-196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 (By similarity). Involved in 18S rRNA maturation. Required for
CC cleavage of the 20S pre-rRNA at site D in the cytoplasm. Involved in
CC oxidative stress response. Required for POS9-dependent target gene
CC transcription upon oxidative stress. {ECO:0000255|HAMAP-Rule:MF_03173,
CC ECO:0000269|PubMed:10692169, ECO:0000269|PubMed:12837249,
CC ECO:0000269|PubMed:16287850}.
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:0000255|HAMAP-Rule:MF_03173};
CC -!- SUBUNIT: Interacts with RPS14B. Not a structural component of 43S pre-
CC ribosomes, but transiently interacts with them with them by binding to
CC RPS14. {ECO:0000269|PubMed:16287850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 8350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
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DR EMBL; Z67750; CAA91580.1; -; Genomic_DNA.
DR EMBL; Z74214; CAA98740.1; -; Genomic_DNA.
DR EMBL; AY558568; AAS56894.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11695.1; -; Genomic_DNA.
DR PIR; S61047; S61047.
DR RefSeq; NP_010115.1; NM_001180226.1.
DR AlphaFoldDB; Q12055; -.
DR SMR; Q12055; -.
DR BioGRID; 31899; 58.
DR DIP; DIP-4793N; -.
DR IntAct; Q12055; 23.
DR STRING; 4932.YDL166C; -.
DR iPTMnet; Q12055; -.
DR MaxQB; Q12055; -.
DR PaxDb; Q12055; -.
DR PRIDE; Q12055; -.
DR EnsemblFungi; YDL166C_mRNA; YDL166C; YDL166C.
DR GeneID; 851388; -.
DR KEGG; sce:YDL166C; -.
DR SGD; S000002325; FAP7.
DR VEuPathDB; FungiDB:YDL166C; -.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00390000015930; -.
DR HOGENOM; CLU_079096_3_0_1; -.
DR InParanoid; Q12055; -.
DR OMA; QCEIFGT; -.
DR BioCyc; YEAST:G3O-29558-MON; -.
DR Reactome; R-SCE-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q12055; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12055; protein.
DR GO; GO:0005737; C:cytoplasm; IMP:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; rRNA processing;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..197
FT /note="Adenylate kinase isoenzyme 6 homolog FAP7"
FT /id="PRO_0000153902"
FT REGION 38..61
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 113..123
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 28..35
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 17..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 44
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT MOD_RES 183
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 19
FT /note="G->S: Sensitive to hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:10692169"
FT MUTAGEN 20
FT /note="K->R: Decreases the processing of 20S rRNA."
FT /evidence="ECO:0000269|PubMed:16287850"
FT MUTAGEN 21
FT /note="S->G: Sensitive to hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:10692169"
FT MUTAGEN 82
FT /note="D->A: Decreases the processing of 20S rRNA; when
FT associated with A-84."
FT /evidence="ECO:0000269|PubMed:16287850"
FT MUTAGEN 84
FT /note="H->A: Decreases the processing of 20S rRNA; when
FT associated with A-82."
FT /evidence="ECO:0000269|PubMed:16287850"
FT CONFLICT 80
FT /note="I -> V (in Ref. 3; AAS56894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 22723 MW; 836A25B0D7E2633C CRC64;
MEARRYGPNI IVTGTPGCGK SSTCEFLKNK LKDYKYYNIS DFAKDNDCFE GYDEGRKSHI
VDEDKLLDML EPLLRQGNSI VDWHVNDVFP ERLIDLVVVL RCDNSNLYSR LHARGYHDSK
IEENLDAEIM GVVKQDAVES YEPHIVVELQ SDTKEDMVSN VSRIVAWEKM WLEQHPDGVT
NEYQGPRSDD EDDEDSE
