KAD6_DROME
ID KAD6_DROME Reviewed; 175 AA.
AC Q7JYV7;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=DAK6;
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};
GN Name=Ak6; ORFNames=CG8816;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18294127; DOI=10.1134/s0006297908010057;
RA Meng G., Zhai R., Liu B., Zheng X.;
RT "Identification of a novel nuclear-localized adenylate kinase from
RT Drosophila melanogaster.";
RL Biochemistry (Mosc.) 73:38-43(2008).
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. AMP is the best
CC phosphate acceptor, and CMP is also a good substrate. All nucleoside
CC triphosphates ATP, TTP, CTP, GTP, and UTP are accepted as phosphate
CC donors. ATP is the best phosphate donor. May have a role in nuclear
CC energy homeostasis. {ECO:0000269|PubMed:18294127}.
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 ECO:0000269|PubMed:18294127};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_03173,
CC ECO:0000269|PubMed:18294127}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03173}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
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DR EMBL; AE013599; AAF58491.1; -; Genomic_DNA.
DR EMBL; AY071739; AAL49361.1; -; mRNA.
DR RefSeq; NP_610797.1; NM_136953.4.
DR AlphaFoldDB; Q7JYV7; -.
DR SMR; Q7JYV7; -.
DR BioGRID; 62153; 8.
DR IntAct; Q7JYV7; 6.
DR STRING; 7227.FBpp0087004; -.
DR PaxDb; Q7JYV7; -.
DR DNASU; 36379; -.
DR EnsemblMetazoa; FBtr0087891; FBpp0087004; FBgn0033754.
DR GeneID; 36379; -.
DR KEGG; dme:Dmel_CG8816; -.
DR UCSC; CG8816-RA; d. melanogaster.
DR CTD; 102157402; -.
DR FlyBase; FBgn0033754; Ak6.
DR VEuPathDB; VectorBase:FBgn0033754; -.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00390000015930; -.
DR HOGENOM; CLU_079096_3_1_1; -.
DR InParanoid; Q7JYV7; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 1488235at2759; -.
DR PhylomeDB; Q7JYV7; -.
DR Reactome; R-DME-499943; Interconversion of nucleotide di- and triphosphates.
DR BioGRID-ORCS; 36379; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 36379; -.
DR PRO; PR:Q7JYV7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033754; Expressed in eye disc (Drosophila) and 28 other tissues.
DR Genevisible; Q7JYV7; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
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; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..175
FT /note="Adenylate kinase isoenzyme 6 homolog"
FT /id="PRO_0000422287"
FT REGION 39..62
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 114..124
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 45
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
SQ SEQUENCE 175 AA; 20463 MW; 79397116DD15E176 CRC64;
MSEPEPDVKP NILITGTPGA GKSYLCERIA SELKFEWLDC SKIAKEKNFV EEYDEEYDCP
ILDEEKLMDH LEPLMAKGGN VVEYHGCDFF PERWFQAVFV VTCPNTTLYD RLKERNYNEK
KLASNIQCEI FGTILEEARD SYKSDIVFEL KGETKADAHI SIKTVKNWYR MWKRK
