KAD6_CAEEL
ID KAD6_CAEEL Reviewed; 182 AA.
AC Q09527;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog {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=Adrenal gland protein AD-004 like protein;
DE Short=ADLP;
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 ORFNames=E02H1.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16781712; DOI=10.1016/j.febslet.2006.05.074;
RA Zhai R., Meng G., Zhao Y., Liu B., Zhang G., Zheng X.;
RT "A novel nuclear-localized protein with special adenylate kinase properties
RT from Caenorhabditis elegans.";
RL FEBS Lett. 580:3811-3817(2006).
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 and dAMP are
CC the preferred substrates, but CMP and TMP are also good substrates. ATP
CC and dATP are the best phosphate donors. May have a role in nuclear
CC energy homeostasis. {ECO:0000269|PubMed:16781712}.
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:16781712};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03173,
CC ECO:0000269|PubMed:16781712}.
CC -!- DISRUPTION PHENOTYPE: Suppresses worm growth.
CC {ECO:0000269|PubMed:16781712}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z47075; CAA87383.2; -; Genomic_DNA.
DR PIR; T20418; T20418.
DR RefSeq; NP_496065.1; NM_063664.7.
DR AlphaFoldDB; Q09527; -.
DR SMR; Q09527; -.
DR STRING; 6239.E02H1.6; -.
DR EPD; Q09527; -.
DR PaxDb; Q09527; -.
DR PeptideAtlas; Q09527; -.
DR EnsemblMetazoa; E02H1.6.1; E02H1.6.1; WBGene00008458.
DR GeneID; 174511; -.
DR UCSC; E02H1.6; c. elegans.
DR CTD; 174511; -.
DR WormBase; E02H1.6; CE28286; WBGene00008458; -.
DR eggNOG; KOG3347; Eukaryota.
DR GeneTree; ENSGT00390000015930; -.
DR HOGENOM; CLU_079096_3_1_1; -.
DR InParanoid; Q09527; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 1488235at2759; -.
DR PhylomeDB; Q09527; -.
DR Reactome; R-CEL-499943; Interconversion of nucleotide di- and triphosphates.
DR PRO; PR:Q09527; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008458; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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..182
FT /note="Adenylate kinase isoenzyme 6 homolog"
FT /id="PRO_0000153900"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..62
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 116..126
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 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
SQ SEQUENCE 182 AA; 21024 MW; 49FCC86D29462765 CRC64;
MATPETRRRP NILVTGSPGT GKSTLGQQVA EKLGFVFIEV SKEVRENNLQ GDFDEQYNCH
VLDEDKLLDH ISDRLDSDEG GIVVDYHGCD LFPERWFDVV VVLRCPTEKL YDRLQSRGYS
EFKIKENVEC EIFGTLLEEA RESYSEDIVH ELQSETTEQM EENLERICEL AGEFKNEHTM
EQ
