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TCD1_YEAST
ID   TCD1_YEAST              Reviewed;         429 AA.
AC   P38756; D3DKU6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=tRNA threonylcarbamoyladenosine dehydratase 1;
DE            EC=6.1.-.-;
DE   AltName: Full=t(6)A37 dehydratase 1;
GN   Name=TCD1; OrderedLocusNames=YHR003C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
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   [3]
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).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [5]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA   Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA   Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT   "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT   accumulation of a subclass of preproteins.";
RL   Mol. Biol. Cell 17:1436-1450(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23242255; DOI=10.1038/nchembio.1137;
RA   Miyauchi K., Kimura S., Suzuki T.;
RT   "A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed
RT   tRNA hypermodification.";
RL   Nat. Chem. Biol. 9:105-111(2013).
CC   -!- FUNCTION: Catalyzes the ATP-dependent dehydration of
CC       threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic
CC       t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine.
CC       {ECO:0000269|PubMed:23242255}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Displays only the t(6)A but not the ct(6)A
CC       modification in tRNAs. Unable to sustain respiratory growth under non-
CC       fermenting conditions. {ECO:0000269|PubMed:23242255}.
CC   -!- MISCELLANEOUS: Present with 8430 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: ct(6)A is involved in promoting decoding efficiency. It
CC       is an unstable modification that can be easily hydrolyzed and converted
CC       to t(6)A during nucleoside preparation by conventional methods
CC       (PubMed:23242255). {ECO:0000305|PubMed:23242255}.
CC   -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR   EMBL; U10555; AAB68430.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06690.1; -; Genomic_DNA.
DR   PIR; S46801; S46801.
DR   RefSeq; NP_011866.1; NM_001179133.1.
DR   AlphaFoldDB; P38756; -.
DR   SMR; P38756; -.
DR   BioGRID; 36428; 96.
DR   DIP; DIP-4417N; -.
DR   IntAct; P38756; 6.
DR   MINT; P38756; -.
DR   STRING; 4932.YHR003C; -.
DR   iPTMnet; P38756; -.
DR   MaxQB; P38756; -.
DR   PaxDb; P38756; -.
DR   PRIDE; P38756; -.
DR   EnsemblFungi; YHR003C_mRNA; YHR003C; YHR003C.
DR   GeneID; 856392; -.
DR   KEGG; sce:YHR003C; -.
DR   SGD; S000001045; TCD1.
DR   VEuPathDB; FungiDB:YHR003C; -.
DR   eggNOG; KOG2018; Eukaryota.
DR   GeneTree; ENSGT00940000176473; -.
DR   HOGENOM; CLU_013325_9_3_1; -.
DR   InParanoid; P38756; -.
DR   OMA; YIFEELW; -.
DR   BioCyc; YEAST:G3O-31068-MON; -.
DR   PRO; PR:P38756; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38756; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061503; F:tRNA threonylcarbamoyladenosine dehydratase; IMP:SGD.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0061504; P:cyclic threonylcarbamoyladenosine biosynthetic process; IMP:SGD.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR43267; PTHR43267; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..429
FT                   /note="tRNA threonylcarbamoyladenosine dehydratase 1"
FT                   /id="PRO_0000120585"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
SQ   SEQUENCE   429 AA;  48883 MW;  3D764E2E98100F0E CRC64;
     MANNTWKLIA TTALISVFST QLAKSVWKEY KLSCAANKNK TVSRPRQYDD HLFREQLARN
     YAFLGEEGMR KIKEQYIVIV GAGEVGSWVC TMLIRSGCQK IMIIDPENIS IDSLNTHCCA
     VLSDIGKPKV QCLKEHLSKI APWSEIKARA KAWTKENSHD LIFADGESPT FIVDCLDNLE
     SKVDLLEYAH HNKIDVISSM GVATKSDPTR VSINDISMTE FDPISRCVRR KLRKRGIATG
     ISVVFSNEML DPRRDDILSP IDCEHRAINA VRDEALRHLP ELGTMPGIFG LSIATWILTK
     VSGYPMKENE VKNRLKFYDS ILETFQKQMA RLNENKERSS LLGLEEVGYI VEEMFRGKSP
     ISGYSTKLAL TKWEANKEIS LTNVVLMTKE EQEIHEKRIL LDGEKLTAVY SEEVLDFIER
     LFKEEEYYS
 
 
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