TAD1_YEAST
ID TAD1_YEAST Reviewed; 400 AA.
AC P53065; D6VV92;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=tRNA-specific adenosine deaminase 1;
DE EC=3.5.4.34;
DE AltName: Full=tRNA-specific adenosine-37 deaminase;
GN Name=TAD1; OrderedLocusNames=YGL243W; ORFNames=HRA400;
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], CATALYTIC ACTIVITY, AND
RP CHARACTERIZATION.
RC STRAIN=BMA41;
RX PubMed=9707437; DOI=10.1093/emboj/17.16.4780;
RA Gerber A., Grosjean H., Melcher T., Keller W.;
RT "Tad1p, a yeast tRNA-specific adenosine deaminase, is related to the
RT mammalian pre-mRNA editing enzymes ADAR1 and ADAR2.";
RL EMBO J. 17:4780-4789(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8750240; DOI=10.1002/yea.320111507;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "The sequence of an 11.1 kb DNA fragment between ADH4 and ADE5 on the left
RT arm of chromosome VII, reveals the presence of eight open reading frames.";
RL Yeast 11:1519-1523(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP COFACTOR.
RX PubMed=16141067; DOI=10.1126/science.1113150;
RA Macbeth M.R., Schubert H.L., Vandemark A.P., Lingam A.T., Hill C.P.,
RA Bass B.L.;
RT "Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA
RT editing.";
RL Science 309:1534-1539(2005).
CC -!- FUNCTION: Deaminates adenosine-37 to inosine in tRNA-Ala.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in
CC tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855,
CC Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34;
CC Evidence={ECO:0000269|PubMed:9707437};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000269|PubMed:16141067};
CC Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC {ECO:0000269|PubMed:16141067};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
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DR EMBL; AJ007297; CAA07438.1; -; Genomic_DNA.
DR EMBL; Z49149; CAA89012.1; -; Genomic_DNA.
DR EMBL; Z72765; CAA96962.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07876.1; -; Genomic_DNA.
DR PIR; S53937; S53937.
DR RefSeq; NP_011271.1; NM_001181109.1.
DR AlphaFoldDB; P53065; -.
DR SMR; P53065; -.
DR BioGRID; 32997; 60.
DR STRING; 4932.YGL243W; -.
DR MaxQB; P53065; -.
DR PaxDb; P53065; -.
DR PRIDE; P53065; -.
DR EnsemblFungi; YGL243W_mRNA; YGL243W; YGL243W.
DR GeneID; 852608; -.
DR KEGG; sce:YGL243W; -.
DR SGD; S000003212; TAD1.
DR VEuPathDB; FungiDB:YGL243W; -.
DR eggNOG; KOG2777; Eukaryota.
DR HOGENOM; CLU_005382_5_0_1; -.
DR InParanoid; P53065; -.
DR OMA; KILHDCH; -.
DR BioCyc; YEAST:YGL243W-MON; -.
DR BRENDA; 3.5.4.34; 984.
DR PRO; PR:P53065; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53065; protein.
DR GO; GO:0005737; C:cytoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; EXP:Reactome.
DR GO; GO:0043829; F:tRNA-specific adenosine-37 deaminase activity; IDA:SGD.
DR GO; GO:0006400; P:tRNA modification; IDA:SGD.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:InterPro.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR042935; Tad1.
DR PANTHER; PTHR47803; PTHR47803; 1.
DR Pfam; PF02137; A_deamin; 1.
DR SMART; SM00552; ADEAMc; 1.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..400
FT /note="tRNA-specific adenosine deaminase 1"
FT /id="PRO_0000171777"
FT DOMAIN 76..400
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT ACT_SITE 103
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 108
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 226
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 45947 MW; 2AA9304C549026FF CRC64;
MVSCQGTRPC IVNLLTMPSE DKLGEEISTR VINEYSKLKS ACRPIIRPSG IREWTILAGV
AAINRDGGAN KIEILSIATG VKALPDSELQ RSEGKILHDC HAEILALRGA NTVLLNRIQN
YNPSSGDKFI QHNDEIPARF NLKENWELAL YISRLPCGDA SMSFLNDNCK NDDFIKIEDS
DEFQYVDRSV KTILRGRLNF NRRNVVRTKP GRYDSNITLS KSCSDKLLMK QRSSVLNCLN
YELFEKPVFL KYIVIPNLED ETKHHLEQSF HTRLPNLDNE IKFLNCLKPF YDDKLDEEDV
PGLMCSVKLF MDDFSTEEAI LNGVRNGFYT KSSKPLRKHC QSQVSRFAQW ELFKKIRPEY
EGISYLEFKS RQKKRSQLII AIKNILSPDG WIPTRTDDVK
