TAD3_SCHPO
ID TAD3_SCHPO Reviewed; 315 AA.
AC Q9P7N4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=tRNA-specific adenosine deaminase subunit tad3;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit tad3;
GN Name=tad3 {ECO:0000250|UniProtKB:Q9URQ3}; ORFNames=SPAP27G11.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB76025.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Deaminates adenosine-34 to inosine in many tRNAs.
CC {ECO:0000250|UniProtKB:Q9URQ3}.
CC -!- SUBUNIT: Heterodimer with tad2. {ECO:0000250|UniProtKB:Q9URQ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000255}.
CC -!- CAUTION: In contrast to other cytidine and deoxycytidylate deaminase,
CC lacks the conserved Glu active site in position 213 which is replaced
CC by a Val residue, suggesting that it acts as a regulatory subunit.
CC {ECO:0000250|UniProtKB:Q9URQ3, ECO:0000305}.
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DR EMBL; CU329670; CAB76025.1; -; Genomic_DNA.
DR RefSeq; NP_593408.1; NM_001018841.2.
DR AlphaFoldDB; Q9P7N4; -.
DR SMR; Q9P7N4; -.
DR BioGRID; 278471; 2.
DR IntAct; Q9P7N4; 1.
DR STRING; 4896.SPAP27G11.04c.1; -.
DR MaxQB; Q9P7N4; -.
DR PaxDb; Q9P7N4; -.
DR EnsemblFungi; SPAP27G11.04c.1; SPAP27G11.04c.1:pep; SPAP27G11.04c.
DR GeneID; 2541987; -.
DR KEGG; spo:SPAP27G11.04c; -.
DR PomBase; SPAP27G11.04c; tad3.
DR VEuPathDB; FungiDB:SPAP27G11.04c; -.
DR eggNOG; KOG2771; Eukaryota.
DR HOGENOM; CLU_013817_2_0_1; -.
DR InParanoid; Q9P7N4; -.
DR OMA; QHWPCKF; -.
DR PhylomeDB; Q9P7N4; -.
DR PRO; PR:Q9P7N4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0052718; C:tRNA-specific adenosine-34 deaminase complex; IDA:PomBase.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:PomBase.
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 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..315
FT /note="tRNA-specific adenosine deaminase subunit tad3"
FT /id="PRO_0000310824"
FT DOMAIN 158..299
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
SQ SEQUENCE 315 AA; 36276 MW; 5B4F8203EC8ABA0F CRC64;
MVKTNISKNS PKEATVPELD WPFKLIKSHL ETRKLETENV WIACFEPKYA SKVTQYVKQI
RSKQKESLLH CNRLRRIQDE NGSLELQIII CPEKSMTANE IGKDFEDLGI VSKMIFLYAV
PAFPPLTDEQ FHEWNSVWPV SYRKHVQRQD VFTVHELKRI ESILEDLINA AGASHKHGEI
GCAAAIYDPT TDTVLAVSVD ERSKLKNPIN HCVMNAINLV AKRELSRRQN RTDGSKDRYL
CKDLTVVMTH EPCVMCSMGL LHSRIRRLIY CKKQPLTGGI ESLYGIHWRA ELNHRYLAYS
GWNKPVPSIK ENIHV
