ADAT2_DANRE
ID ADAT2_DANRE Reviewed; 214 AA.
AC Q5RIV4; A4IGI0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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; ORFNames=si:ch211-157l15.2;
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 GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RIV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RIV4-2; Sequence=VSP_029612;
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI35110.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX088644; CAI11650.1; -; Genomic_DNA.
DR EMBL; BC135109; AAI35110.1; ALT_INIT; mRNA.
DR RefSeq; XP_005160675.1; XM_005160618.3. [Q5RIV4-1]
DR AlphaFoldDB; Q5RIV4; -.
DR SMR; Q5RIV4; -.
DR STRING; 7955.ENSDARP00000061472; -.
DR PaxDb; Q5RIV4; -.
DR Ensembl; ENSDART00000115221; ENSDARP00000103292; ENSDARG00000041944. [Q5RIV4-2]
DR Ensembl; ENSDART00000152885; ENSDARP00000127393; ENSDARG00000041944. [Q5RIV4-1]
DR GeneID; 100034610; -.
DR CTD; 134637; -.
DR ZFIN; ZDB-GENE-041014-360; adat2.
DR eggNOG; KOG1018; Eukaryota.
DR GeneTree; ENSGT00390000000280; -.
DR HOGENOM; CLU_025810_8_1_1; -.
DR InParanoid; Q5RIV4; -.
DR OMA; PCQMCAG; -.
DR OrthoDB; 1616309at2759; -.
DR TreeFam; TF313782; -.
DR PRO; PR:Q5RIV4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000041944; Expressed in early embryo and 21 other tissues.
DR ExpressionAtlas; Q5RIV4; baseline.
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; PF00383; dCMP_cyt_deam_1; 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 Alternative splicing; Hydrolase; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..214
FT /note="tRNA-specific adenosine deaminase 2"
FT /id="PRO_0000287655"
FT DOMAIN 19..144
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 72
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 177..214
FT /note="APKPKVRKDSINPQDGAAVIQVMRGPPDEETETIAHLS -> GQCQTGGRKR
FT RFLRLLLSDCLRLGSPSAVC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_029612"
FT CONFLICT 199
FT /note="M -> I (in Ref. 2; AAI35110)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="I -> N (in Ref. 2; AAI35110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23839 MW; ADAF28418759410D CRC64;
MQEVGVDPEK NDFLQPSDSE VQTWMAKAFD MAVEALENGE VPVGCLMVYN NEIIGKGRNE
VNETKNATRH AEMVALDQVL DWCRLREKDC KEVCEQTVLY VTVEPCIMCA AALRLLRIPF
VVYGCKNERF GGCGSVLDVS SDHLPHTGTS FKCIAGYRAE EAVEMLKTFY KQENPNAPKP
KVRKDSINPQ DGAAVIQVMR GPPDEETETI AHLS
