KAD7_MACFA
ID KAD7_MACFA Reviewed; 533 AA.
AC Q95JP6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Adenylate kinase 7;
DE Short=AK 7;
DE EC=2.7.4.3 {ECO:0000250|UniProtKB:Q96M32};
DE EC=2.7.4.6 {ECO:0000250|UniProtKB:Q96M32};
DE AltName: Full=ATP-AMP transphosphorylase 7;
DE Flags: Fragment;
GN Name=AK7; ORFNames=QtsA-14746;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the
CC reversible transfer of the terminal phosphate group between nucleoside
CC triphosphates and monophosphates. Has highest activity toward AMP, and
CC weaker activity toward dAMP, CMP and dCMP. Also displays broad
CC nucleoside diphosphate kinase activity. Involved in maintaining ciliary
CC structure and function. {ECO:0000250|UniProtKB:Q96M32}.
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:0000250|UniProtKB:Q96M32};
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 Evidence={ECO:0000250|UniProtKB:Q96M32};
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 Evidence={ECO:0000250|UniProtKB:Q96M32};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96M32}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q96M32}. Note=Detected along the full length of
CC sperm flagellum, where it colocalizes with alpha-tubulin.
CC {ECO:0000250|UniProtKB:Q96M32}.
CC -!- SIMILARITY: In the central section; belongs to the adenylate kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the dpy-30 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB63080.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB070135; BAB63080.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q95JP6; -.
DR SMR; Q95JP6; -.
DR STRING; 9541.XP_005562225.1; -.
DR eggNOG; KOG3078; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004127; F:cytidylate kinase activity; ISS:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR026867; AK7.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PANTHER; PTHR23359:SF105; PTHR23359:SF105; 1.
DR Pfam; PF05186; Dpy-30; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Flagellum; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN <1..533
FT /note="Adenylate kinase 7"
FT /id="PRO_0000158953"
FT REGION 177..426
FT /note="Adenylate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q96M32"
FT REGION 207..265
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 347..357
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 489..533
FT /note="DPY-30"
FT /evidence="ECO:0000250|UniProtKB:Q96M32"
FT COILED 419..487
FT /evidence="ECO:0000255"
FT BINDING 187..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 242..265
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 292..295
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 299
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 365
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT NON_TER 1
SQ SEQUENCE 533 AA; 61314 MW; A1453BE088FC8E95 CRC64;
INAEKMVLKF GRKTRKFATY VVAAGLQYGA EGGMLHTFFK MAWLGEIPAL PVFGDGTNVI
PTIHVLDLAG VIQNVIDHTP KPHYLVAVDE SVHTLEDIVK CISKNTGPGK IQKIPRENAY
LTKDLTQDCL DHLLVNLRME ALFVKENFNI RWVAQTGFVE NINSILKEYK QSRGLMPVKI
CILGPPAVGK SSIAEELAKY YKLHHIQLKD VISEAIAKLE TIVAPKDIGE GKEEVEEEEE
EENVEDAQEL LDGIKESMEQ NAGQLDDQYI IRFMKEKLKS MPCRNQGYIL DGFPKTYDQA
KDLFNQEDEE EEDEVRGRMF PFDKLIIPEF VCALDASDEF LKERVINLPE RIVAGTHYSQ
DRFLRALSNY RDINIEDETV FNYFDEIEIH PIHIDVGKLE DAQNRLAIKQ LIKEIGEPRN
YGLTDEEKAE EERKAAEERL AREAAEEAER EHQEAVEMAE KIARWEEWNK RLEEVKREER
ELLEAQSIPL RNYLMTYVMP TLIQGLNECC NVRPEDPVDF LAEYLFKNNP EAQ
