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KAD8_DANRE
ID   KAD8_DANRE              Reviewed;         486 AA.
AC   Q502L7;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=zgc:112030;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q96MA6}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR   EMBL; BC095649; AAH95649.1; -; mRNA.
DR   RefSeq; NP_001018480.1; NM_001020644.1.
DR   AlphaFoldDB; Q502L7; -.
DR   SMR; Q502L7; -.
DR   STRING; 7955.ENSDARP00000043095; -.
DR   PaxDb; Q502L7; -.
DR   GeneID; 553671; -.
DR   KEGG; dre:553671; -.
DR   CTD; 158067; -.
DR   ZFIN; ZDB-GENE-050522-275; ak8.
DR   eggNOG; KOG3078; Eukaryota.
DR   InParanoid; Q502L7; -.
DR   OrthoDB; 961384at2759; -.
DR   PhylomeDB; Q502L7; -.
DR   Reactome; R-DRE-499943; Interconversion of nucleotide di- and triphosphates.
DR   PRO; PR:Q502L7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..486
FT                   /note="Adenylate kinase 8"
FT                   /id="PRO_0000279387"
FT   REGION          58..258
FT                   /note="Adenylate kinase 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96MA6"
FT   REGION          87..112
FT                   /note="NMP 1"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   REGION          176..205
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         139..142
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         202
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         392
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         432
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
SQ   SEQUENCE   486 AA;  55589 MW;  16A2873426F6885F CRC64;
     MDSAERPLRI PPEMVIYAEK HDIFHLIQTL VRNLMVDKPD DPIQYLINFL ERDNVDVPRI
     ILLGPPASGK KTVAKKLCEH TQAIHITFCD ILKDDSDLTR AAQSYYDKKQ NVPKDLWIQL
     IQQRLSKPDC VQRGWVLEAI PKTQDEALCL QEAGITPDHV VMLEAPDVVL IERSSGKRID
     PVTGDVYHVT FMWPESEEVA QRLETPRTLM PVQVMSQKLQ KYHTEAHALK RTYHNCLKII
     NADQPHVDVF SQVLNFICTP RHSPSPYTPR ILLFGPPGAG RNLQAKLIAQ KYGIINICCG
     ELLKAVSADE SHMGELIKPY LESEQQVPSS IVLRVLTERL SRMDCTARGW VLHGFPRDVE
     EAELLHKSNF TPNRVFFLEI TDDIAIERLA LRAVDPVTGE WYHSVYKPPP GPEVQARLRF
     NPQHSEAQLL MRLKEYWSQT VRLQAFYPQA VYINADQDPH TVFESLESRL VGQLPKVLSN
     QQTNEN
 
 
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