TAD2_YEAST
ID TAD2_YEAST Reviewed; 250 AA.
AC P47058; D6VWE8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=tRNA-specific adenosine deaminase subunit TAD2;
DE EC=3.5.4.33;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit TAD2;
GN Name=TAD2; OrderedLocusNames=YJL035C; ORFNames=J1246;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=BMA41;
RX PubMed=10550050; DOI=10.1126/science.286.5442.1146;
RA Gerber A.P., Keller W.;
RT "An adenosine deaminase that generates inosine at the wobble position of
RT transfer RNAs.";
RL Science 286:1146-1149(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-250.
RA Sora S., Tiboni O., Sanangelantoni A.M.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Deaminates adenosine-34 to inosine in many tRNAs.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterodimer with TAD3.
CC -!- INTERACTION:
CC P47058; Q9URQ3: TAD3; NbExp=2; IntAct=EBI-18939, EBI-2094330;
CC -!- MISCELLANEOUS: Present with 830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ242667; CAB60629.1; -; Genomic_DNA.
DR EMBL; Z49310; CAA89326.1; -; Genomic_DNA.
DR EMBL; AY693172; AAT93191.1; -; Genomic_DNA.
DR EMBL; Z48229; CAA88261.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006943; DAA08764.1; -; Genomic_DNA.
DR PIR; S56807; S56807.
DR RefSeq; NP_012499.1; NM_001181469.1.
DR PDB; 7BV5; X-ray; 2.80 A; A/B=2-250.
DR PDBsum; 7BV5; -.
DR AlphaFoldDB; P47058; -.
DR SMR; P47058; -.
DR BioGRID; 33725; 90.
DR ComplexPortal; CPX-1742; tRNA-specific adenosine-34 deaminase complex.
DR DIP; DIP-5546N; -.
DR IntAct; P47058; 1.
DR MINT; P47058; -.
DR STRING; 4932.YJL035C; -.
DR PaxDb; P47058; -.
DR PRIDE; P47058; -.
DR EnsemblFungi; YJL035C_mRNA; YJL035C; YJL035C.
DR GeneID; 853417; -.
DR KEGG; sce:YJL035C; -.
DR SGD; S000003572; TAD2.
DR VEuPathDB; FungiDB:YJL035C; -.
DR eggNOG; KOG1018; Eukaryota.
DR GeneTree; ENSGT00940000164335; -.
DR HOGENOM; CLU_025810_8_1_1; -.
DR InParanoid; P47058; -.
DR OMA; PCQMCAG; -.
DR BioCyc; YEAST:YJL035C-MON; -.
DR BRENDA; 3.5.4.33; 984.
DR PRO; PR:P47058; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47058; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0052718; C:tRNA-specific adenosine-34 deaminase complex; IPI:ComplexPortal.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IDA:SGD.
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:0006400; P:tRNA modification; IDA:SGD.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:ComplexPortal.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
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; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..250
FT /note="tRNA-specific adenosine deaminase subunit TAD2"
FT /id="PRO_0000171740"
FT DOMAIN 1..119
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 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:7BV5"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 55..75
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:7BV5"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:7BV5"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:7BV5"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:7BV5"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:7BV5"
SQ SEQUENCE 250 AA; 28252 MW; C774A1E50AA68106 CRC64;
MQHIKHMRTA VRLARYALDH DETPVACIFV HTPTGQVMAY GMNDTNKSLT GVAHAEFMGI
DQIKAMLGSR GVVDVFKDIT LYVTVEPCIM CASALKQLDI GKVVFGCGNE RFGGNGTVLS
VNHDTCTLVP KNNSAAGYES IPGILRKEAI MLLRYFYVRQ NERAPKPRSK SDRVLDKNTF
PPMEWSKYLN EEAFIETFGD DYRTCFANKV DLSSNSVDWD LIDSHQDNII QELEEQCKMF
KFNVHKKSKV
