ADAT3_DANRE
ID ADAT3_DANRE Reviewed; 336 AA.
AC Q8JFW4; B0V342; Q8JFR8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 93.
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; ORFNames=si:busm1-72b14.5, si:dkey-204g5.2, zgc:103555;
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].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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-221 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; AL591593; CAD43470.1; -; Genomic_DNA.
DR EMBL; AL672217; CAD43442.1; -; Genomic_DNA.
DR EMBL; CT737230; CAQ15728.1; -; Genomic_DNA.
DR EMBL; BC085551; AAH85551.1; -; mRNA.
DR AlphaFoldDB; Q8JFW4; -.
DR SMR; Q8JFW4; -.
DR STRING; 7955.ENSDARP00000018770; -.
DR PaxDb; Q8JFW4; -.
DR ZFIN; ZDB-GENE-030616-531; adat3.
DR eggNOG; KOG2771; Eukaryota.
DR InParanoid; Q8JFW4; -.
DR PhylomeDB; Q8JFW4; -.
DR TreeFam; TF313277; -.
DR PRO; PR:Q8JFW4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..336
FT /note="Probable inactive tRNA-specific adenosine deaminase-
FT like protein 3"
FT /id="PRO_0000287661"
FT DOMAIN 167..322
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="K -> R (in Ref. 1; CAD43470/CAQ15728)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="C -> S (in Ref. 1; CAD43470/CAQ15728)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> K (in Ref. 1; CAQ15728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37683 MW; 46B47912355C27A3 CRC64;
MEPQAKRKKE MDDYDDTWEV LPVLSDEQSQ DPELLPAYAA PILERRETSR LVKELSLIHP
LPNLQHIKRV RPCKHKDSPH PLEVIVCLVS DVQCTDPKKV TLSHLLHTQC FNSNGLGDPF
IVQIPANPPL TRPQFEKASK HWPTSFHEDK LVTFALKGQL FTAHQKTKMR EYMCVAVKAA
KSGRELGMDA VGAVIVDPKT EQIIAVAHDC KRGSHPLHHA VMVCIDLVAC GQDGGAYNYE
KYPACRFSCS NSVCDGKETG LPYICTGYDL YVTREPCVMC AMALVHSRIS RVFYGASTAD
GAFGSRYKIH CQKDLNHRFE VFKGVMVNAC EDLCKE
