ID A0A2B4SKE4_STYPI Unreviewed; 480 AA.
AC A0A2B4SKE4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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|EMBL:PFX30351.1};
GN ORFNames=AWC38_SpisGene4860 {ECO:0000313|EMBL:PFX30351.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX30351.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|RuleBase:RU003330}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX30351.1}.
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DR EMBL; LSMT01000051; PFX30351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SKE4; -.
DR STRING; 50429.A0A2B4SKE4; -.
DR EnsemblMetazoa; XM_022927122.1; XP_022782857.1; LOC111323707.
DR OrthoDB; 314591at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
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: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; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
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:UP000225706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ SEQUENCE 480 AA; 54438 MW; 0293201CC6907243 CRC64;
MDATKKPLLI PPEFSNYAEK HNIFQIYESL LTKLIIEQPA DPLTYMIGLL EQESEVPQII
IHGPPAAGKR TMSVMAAEHF DCVHITLENL LAVSDSKSSK KAQEYISAKE MVPTHIWVSL
IKERLQKEDC ISKGWLLEAF PQTREQAQAL QAEGINPRHF VLLEAPDTVL IERVMGKRID
PETGDVYHST FDPPTDPAVV QRLVPDSKSS EKVMIQRLME YHRHIDGILM CFEKIHKSIN
VDQPKADVFS QVLSYLKMNH RNNAPHTPRL ILLGPTGCGK SVQAELLASK YGLVNVSCTE
LIKQSLVDDS NVGDAVRPYT DRHMLVPDDL VLQLLKYRLA QLDAVTKGWV IHGFPKTREQ
ARALTRAGYE ANRVIFMDVP TDTILERLTL RSVDPVTGER YHLIYNPPRT NEVKQRLHTS
PKDVESAVNS RIAQYQAYVE EIAEYYEESV QHINADQDIH TVFECIESII VNPIPTKNEV
//
