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ADAT2_XENTR
ID   ADAT2_XENTR             Reviewed;         170 AA.
AC   Q0P4H0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=tRNA-specific adenosine deaminase 2;
DE            EC=3.5.4.33 {ECO:0000305};
DE   AltName: Full=Deaminase domain-containing protein 1;
DE   AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT2;
GN   Name=adat2; Synonyms=deadc1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Oviduct;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably participates in deamination of adenosine-34 to
CC       inosine in many tRNAs. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC         NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC         COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC         Evidence={ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. ADAT2 subfamily. {ECO:0000305}.
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DR   EMBL; BC122084; AAI22085.1; -; mRNA.
DR   RefSeq; NP_001072562.1; NM_001079094.1.
DR   AlphaFoldDB; Q0P4H0; -.
DR   SMR; Q0P4H0; -.
DR   STRING; 8364.ENSXETP00000030728; -.
DR   PaxDb; Q0P4H0; -.
DR   DNASU; 780017; -.
DR   GeneID; 780017; -.
DR   KEGG; xtr:780017; -.
DR   CTD; 134637; -.
DR   Xenbase; XB-GENE-963029; adat2.
DR   eggNOG; KOG1018; Eukaryota.
DR   InParanoid; Q0P4H0; -.
DR   OrthoDB; 1616309at2759; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR   HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR028883; tRNA_aden_deaminase.
DR   Pfam; PF14437; MafB19-deam; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..170
FT                   /note="tRNA-specific adenosine deaminase 2"
FT                   /id="PRO_0000287657"
FT   DOMAIN          3..128
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  19121 MW;  9C3F7BCD3E2B7028 CRC64;
     MTEEIQNWMH KAFQMAQDAL NNGEVPVGCL MVYDNQVVGK GRNEVNETKN ATRHAEMVAI
     DQVLDWCEKN SKKSRDVFEN IVLYVTVEPC IMCAGALRLL KIPLVVYGCR NERFGGCGSV
     LNVAGDNIPD TGTEFKYIGG YQAEKAVELL KTFYKQENPN APRSKVRKKE
 
 
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