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TAD3_YEAST
ID   TAD3_YEAST              Reviewed;         322 AA.
AC   Q9URQ3; D6VYW0; O13552;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=tRNA-specific adenosine deaminase subunit TAD3;
DE   AltName: Full=tRNA-specific adenosine-34 deaminase subunit TAD3;
GN   Name=TAD3; OrderedLocusNames=YLR316C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   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   -!- SUBUNIT: Heterodimer with TAD2.
CC   -!- INTERACTION:
CC       Q9URQ3; P47058: TAD2; NbExp=2; IntAct=EBI-2094330, EBI-18939;
CC   -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. ADAT3 subfamily. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other cytidine and deoxycytidylate deaminase,
CC       lacks to conserved Glu active site in position 218 which is replaced by
CC       a Val residue, suggesting that it acts as a regulatory subunit.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB64529.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ242668; CAB60630.1; -; Genomic_DNA.
DR   EMBL; U20618; AAB64529.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006945; DAA09626.1; -; Genomic_DNA.
DR   RefSeq; NP_013420.2; NM_001182205.1.
DR   PDB; 7BV5; X-ray; 2.80 A; C/D=1-322.
DR   PDBsum; 7BV5; -.
DR   AlphaFoldDB; Q9URQ3; -.
DR   SMR; Q9URQ3; -.
DR   BioGRID; 31581; 573.
DR   ComplexPortal; CPX-1742; tRNA-specific adenosine-34 deaminase complex.
DR   DIP; DIP-5917N; -.
DR   IntAct; Q9URQ3; 1.
DR   STRING; 4932.YLR316C; -.
DR   MaxQB; Q9URQ3; -.
DR   PaxDb; Q9URQ3; -.
DR   PRIDE; Q9URQ3; -.
DR   EnsemblFungi; YLR316C_mRNA; YLR316C; YLR316C.
DR   GeneID; 851027; -.
DR   KEGG; sce:YLR316C; -.
DR   SGD; S000004308; TAD3.
DR   VEuPathDB; FungiDB:YLR316C; -.
DR   eggNOG; KOG2771; Eukaryota.
DR   GeneTree; ENSGT00390000010706; -.
DR   HOGENOM; CLU_013817_2_0_1; -.
DR   InParanoid; Q9URQ3; -.
DR   OMA; GDGYCMH; -.
DR   BioCyc; YEAST:YLR316C-MON; -.
DR   BRENDA; 3.5.4.33; 984.
DR   PRO; PR:Q9URQ3; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q9URQ3; 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:0006400; P:tRNA modification; IDA:SGD.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:ComplexPortal.
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   1: Evidence at protein level;
KW   3D-structure; Reference proteome; tRNA processing.
FT   CHAIN           1..322
FT                   /note="tRNA-specific adenosine deaminase subunit TAD3"
FT                   /id="PRO_0000171741"
FT   DOMAIN          162..283
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   TURN            13..16
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           46..63
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          78..83
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           96..101
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           129..138
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           160..179
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          200..203
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           217..231
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           255..263
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          267..273
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   TURN            276..278
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          302..306
FT                   /evidence="ECO:0007829|PDB:7BV5"
FT   STRAND          308..311
FT                   /evidence="ECO:0007829|PDB:7BV5"
SQ   SEQUENCE   322 AA;  37107 MW;  08D0878F10B36403 CRC64;
     MVKKVNNPLK IDYQNGIIEN RLLQIRNFKD VNTPKLINVW SIRIDPRDSK KVIELIRNDF
     QKNDPVSLRH LKRIRKDIET STLEVVLCSK EYICDEGEIN NKLKSIWVGT KKYELSDDIE
     VPEFAPSTKE LNNAWSVKYW PLIWNGNPND QILNDYKIDM QEVRNELSRA STLSVKMATA
     GKQFPMVSVF VDPSRKKDKV VAEDGRNCEN SLPIDHSVMV GIRAVGERLR EGVDEDANSY
     LCLDYDVYLT HEPCSMCSMA LIHSRVRRVV FLTEMQRTGS LKLTSGDGYC MNDNKQLNST
     YEAFQWIGEE YPVGQVDRDV CC
 
 
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