ID A0A3Q1NHP5_BOVIN Unreviewed; 468 AA.
AC A0A3Q1NHP5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Adenylate kinase 8 {ECO:0000256|ARBA:ARBA00029501};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
DE EC=2.7.4.6 {ECO:0000256|ARBA:ARBA00012966};
DE AltName: Full=ATP-AMP transphosphorylase 8 {ECO:0000256|ARBA:ARBA00042874};
GN Name=AK8 {ECO:0000313|Ensembl:ENSBTAP00000071485.1,
GN ECO:0000313|VGNC:VGNC:25777};
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 {ECO:0000313|Ensembl:ENSBTAP00000071485.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000071485.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071485.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000071485.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000071485.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037483}.
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:0000256|ARBA:ARBA00000582};
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:0000256|ARBA:ARBA00038690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|RuleBase:RU003330}.
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DR AlphaFoldDB; A0A3Q1NHP5; -.
DR Ensembl; ENSBTAT00000073782.1; ENSBTAP00000071485.1; ENSBTAG00000004092.5.
DR VEuPathDB; HostDB:ENSBTAG00000004092; -.
DR VGNC; VGNC:25777; AK8.
DR GeneTree; ENSGT00940000161613; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000004092; Expressed in semen and 105 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1NHP5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 2.
DR CDD; cd22979; DD_AK8; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF81; ADENYLATE KINASE 8; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 53329 MW; F9C0B277258B904E CRC64;
MTRGPSDSGP QGAAALRGSM DATTAPHRIP PQMPQYGEAN HIFELMQNML EQLLIHQPKD
PIPFMIDHLQ RDNDYVPKIV ILGPPASGKT TIAMWLAKHL STNLLSVESL IAKEYSPLAA
DARMHYQKFK MVPDMLLIRL MQERLKEEDC VRRGWILDGI PETREQALTI QTLGISPRHV
IVLSAPDTVL IERNLGKRID PQTGEIYHTT FDWPPESEIQ NRLMVPAGIF EGETARKLLE
YHRNIVRILP SYPKILKVIS ADQPCVDVFY QALTYVQTSH RSNAPFTPRV LLCGPVGSGK
SLQAALLAQK YGLINVPDNI IMKVLKQRLD QQDCVERGWV LHGFPRDLDQ AHLMDNLGYK
PNRVFFLNVP FDSVIERLSL RRTDPITGER YHLMYKPPPT IEVQARLLQN PKDSEEQIKL
KMDLFYRNSA ELEQFYGDAI TLNGDQDPYT VFEYIESGII NRLPKKVP
//
