NDK7_BOVIN
ID NDK7_BOVIN Reviewed; 377 AA.
AC Q5E9Y9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Nucleoside diphosphate kinase 7;
DE Short=NDK 7;
DE Short=NDP kinase 7;
DE EC=2.7.4.6;
GN Name=NME7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:7RRO}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=34715025; DOI=10.1016/j.cell.2021.10.007;
RA Gui M., Farley H., Anujan P., Anderson J.R., Maxwell D.W., Whitchurch J.B.,
RA Botsch J.J., Qiu T., Meleppattu S., Singh S.K., Zhang Q., Thompson J.,
RA Lucas J.S., Bingle C.D., Norris D.P., Roy S., Brown A.;
RT "De novo identification of mammalian ciliary motility proteins using cryo-
RT EM.";
RL Cell 184:5791-5806.e19(2021).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate. Microtubule inner protein (MIP) part of the dynein-
CC decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC required for motile cilia beating (PubMed:34715025).
CC {ECO:0000269|PubMed:34715025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:34715025}.
CC -!- TISSUE SPECIFICITY: Expressed in trachea multiciliated cells.
CC {ECO:0000269|PubMed:34715025}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; BT020780; AAX08797.1; -; mRNA.
DR EMBL; BC109996; AAI09997.1; -; mRNA.
DR RefSeq; NP_001015656.1; NM_001015656.1.
DR PDB; 7RRO; EM; 3.40 A; 5/6=1-377.
DR PDBsum; 7RRO; -.
DR AlphaFoldDB; Q5E9Y9; -.
DR SMR; Q5E9Y9; -.
DR STRING; 9913.ENSBTAP00000044149; -.
DR PaxDb; Q5E9Y9; -.
DR PRIDE; Q5E9Y9; -.
DR Ensembl; ENSBTAT00000046902; ENSBTAP00000044149; ENSBTAG00000002689.
DR GeneID; 534611; -.
DR KEGG; bta:534611; -.
DR CTD; 29922; -.
DR VEuPathDB; HostDB:ENSBTAG00000002689; -.
DR VGNC; VGNC:32129; NME7.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000158946; -.
DR HOGENOM; CLU_060216_3_1_1; -.
DR InParanoid; Q5E9Y9; -.
DR OMA; VCMCLEI; -.
DR OrthoDB; 1230088at2759; -.
DR TreeFam; TF106374; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000002689; Expressed in occipital lobe and 105 other tissues.
DR ExpressionAtlas; Q5E9Y9; baseline and differential.
DR GO; GO:0005879; C:axonemal microtubule; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR CDD; cd04415; NDPk7A; 1.
DR CDD; cd04412; NDPk7B; 1.
DR Gene3D; 3.30.70.141; -; 2.
DR InterPro; IPR006602; DM10_dom.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR011410; NDPK7.
DR InterPro; IPR035525; NDPk7A.
DR InterPro; IPR037993; NDPk7B.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR Pfam; PF00334; NDK; 2.
DR PIRSF; PIRSF036503; NDK7; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00676; DM10; 1.
DR SMART; SM00562; NDK; 2.
DR SUPFAM; SSF54919; SSF54919; 2.
DR PROSITE; PS51336; DM10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="Nucleoside diphosphate kinase 7"
FT /id="PRO_0000245168"
FT DOMAIN 3..91
FT /note="DM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT ACT_SITE 206
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 42599 MW; 95E8E0AD5D5047EA CRC64;
MNHSERFVFI AEWFDPNASL FRRYELLFYP GDGSVEMHDV KNHRTFLKRT KYEDLHLEDL
FIGNKVNIFS RQLVLLDYGD QYTARQLGSK KEKTLALIKP DAVSKAGEII EIINKAGFTL
TKLKMMTLSR KEATDFHIDH QSRPFLNELI QFITSGPIIA MEILRDDAVC EWKRLLGPAN
SGLARTDAPE SIRALFGTDG IKNAAHGPDS FACAAREMEL FFPSSGVCGP ANTAKFTNCT
TCCIVKPHAV SEGLLGKILM TIRDAGFEIS AMQMFNMDRI NVEEFYEVYK GVVSEYNEMV
TEMYSGPCVA MEIQQTNPTM TFREFCGPAD PEIARHLRPG TLRAIFGKTK IQNAVHCTDL
PEDGLLEVQY FFKILDN
