ADAT3_RAT
ID ADAT3_RAT Reviewed; 349 AA.
AC Q561R2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable inactive tRNA-specific adenosine deaminase-like protein 3;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT3;
GN Name=Adat3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Val-225 is present instead of the conserved Glu which is an
CC active site in the cytidine and deoxycytidylate deaminase family of
CC enzymes. It is suggested that this protein may act as a regulatory
CC subunit. {ECO:0000305}.
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DR EMBL; BC093394; AAH93394.1; -; mRNA.
DR RefSeq; NP_001096831.1; NM_001103361.1.
DR RefSeq; XP_017450047.1; XM_017594558.1.
DR AlphaFoldDB; Q561R2; -.
DR SMR; Q561R2; -.
DR PhosphoSitePlus; Q561R2; -.
DR PRIDE; Q561R2; -.
DR Ensembl; ENSRNOT00000095368; ENSRNOP00000089590; ENSRNOG00000063591.
DR GeneID; 100125374; -.
DR KEGG; rno:100125374; -.
DR UCSC; RGD:1642417; rat.
DR CTD; 113179; -.
DR RGD; 1642417; Adat3.
DR GeneTree; ENSGT00390000010706; -.
DR InParanoid; Q561R2; -.
DR OrthoDB; 1301800at2759; -.
DR PhylomeDB; Q561R2; -.
DR PRO; PR:Q561R2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..349
FT /note="Probable inactive tRNA-specific adenosine deaminase-
FT like protein 3"
FT /id="PRO_0000287660"
FT DOMAIN 171..334
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY9"
SQ SEQUENCE 349 AA; 37704 MW; 7BEE1AB539DCA463 CRC64;
MEPTSGFAEQ PGPEKVESEE QEPAQWQALP VLSEQQSGAV ELVLAYAAPV LDKRQTSRLL
REVSAVYPLP AQPHLKRVRP SRSAGGAHSS DLLLCLAGPS AGPRSLAELL PRPAVDPRGL
GTPFLVPVPA RPPLTRSQFE EARAHWPTSF HEDKQVTSAL AGQLFSAQAR AAMQTHMERA
VRAAQRAAAQ GLRAVGAVVV DPASDHVLAT GHDCCSEASP LLHAVMVCID LVAQGQGRGS
CDLRRHPACS FTQATATQSA RAGSVRKLDE DSLPYVCTGY DLYVTREPCV MCAMALVHAR
IQRVFYGAPS PDGALGTRFR VHARPDLNHR FQVFRGILED QCRQLDPDP
