KAD8_MACFA
ID KAD8_MACFA Reviewed; 479 AA.
AC Q4R3W4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Adenylate kinase 8;
DE Short=AK 8;
DE EC=2.7.4.3;
DE EC=2.7.4.6;
DE AltName: Full=ATP-AMP transphosphorylase 8;
GN Name=AK8; ORFNames=QtsA-13756;
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;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q96MA6}.
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:Q96MA6};
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:Q96MA6};
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:Q96MA6};
CC -!- SUBUNIT: Interacts with CFAP45 and CFAP52; CFAP45 and AK8 dimerization
CC may create a cavity at the interface of the dimer that can accommodate
CC AMP. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of
CC respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR EMBL; AB179151; BAE02202.1; -; mRNA.
DR RefSeq; NP_001271521.1; NM_001284592.1.
DR AlphaFoldDB; Q4R3W4; -.
DR SMR; Q4R3W4; -.
DR STRING; 9541.XP_005580614.1; -.
DR GeneID; 101867160; -.
DR CTD; 158067; -.
DR eggNOG; KOG3078; Eukaryota.
DR eggNOG; KOG3079; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; 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:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR CDD; cd01428; ADK; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57774; SSF57774; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..479
FT /note="Adenylate kinase 8"
FT /id="PRO_0000279384"
FT REGION 58..258
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 87..113
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 177..206
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 269..471
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT REGION 298..327
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 391..424
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 67..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 140..143
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 147
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 203
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 278..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 325..327
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 354..357
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 361
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 479 AA; 54710 MW; 1A1B001390D88C59 CRC64;
MDSASVPHRI PPEMPQYGEE NHIFELMQNM LEQLLIHQPE DPIPFMIQHL HKDNDNVPRI
VILGPPASGK TTIAMWLCKH LNSSLLTLEN LVLNEFSLTA TKAKRLYLQR KTIPSALLVQ
LIQERLAEED CVKRGWILDG IPETREQALR IQTLGITPRH VIVLSAPDTV LIERNLGKRI
DPQTGEIYHT TFDWPPESEI QNRLMVPEDI SELETAQKLL EYHRNIVRVI PSYPKILKVI
SADQPCVDVF YQALTYVQSN HRTNAPFTPR VLLLGPVGSG KSLQAALLAQ KYRLVNVCCG
QLLKEAMADR TTFGELIQPF FEKEMAVLDS LLMKVLSQRL DQQDCIQKGW VLHGVPRDLD
QAHLLNSLGY NPNRVFFLNV PFDSIMERLT LRRIDPVTGE RYHLMYKPPP TMEILARLLQ
NPKDAEEQVK LKMDLSYRNS ADLEQLYGSA ITVNGDQDPY TVFEYIESGI INPLPKKIP
