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TYW3_SCHPO
ID   TYW3_SCHPO              Reviewed;         237 AA.
AC   Q9UTA5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 3;
DE            Short=tRNA-yW-synthesizing protein 3;
DE            EC=2.1.1.282;
DE   AltName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase;
GN   Name=tyw3; ORFNames=SPAC25B8.15c;
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]
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).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts
CC       as a component of the wybutosine biosynthesis pathway. Wybutosine is a
CC       hyper modified guanosine with a tricyclic base found at the 3'-position
CC       adjacent to the anticodon of eukaryotic phenylalanine tRNA. Probably
CC       methylates N-4 position of wybutosine-86 to produce wybutosine-72 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC         tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC         carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC         COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC   -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB61781.1; -; Genomic_DNA.
DR   PIR; T50202; T50202.
DR   RefSeq; NP_594475.1; NM_001019904.2.
DR   AlphaFoldDB; Q9UTA5; -.
DR   SMR; Q9UTA5; -.
DR   BioGRID; 279180; 1.
DR   STRING; 4896.SPAC25B8.15c.1; -.
DR   iPTMnet; Q9UTA5; -.
DR   MaxQB; Q9UTA5; -.
DR   PaxDb; Q9UTA5; -.
DR   EnsemblFungi; SPAC25B8.15c.1; SPAC25B8.15c.1:pep; SPAC25B8.15c.
DR   GeneID; 2542730; -.
DR   KEGG; spo:SPAC25B8.15c; -.
DR   PomBase; SPAC25B8.15c; tyw3.
DR   VEuPathDB; FungiDB:SPAC25B8.15c; -.
DR   eggNOG; KOG1228; Eukaryota.
DR   HOGENOM; CLU_047426_0_0_1; -.
DR   InParanoid; Q9UTA5; -.
DR   OMA; YITREYM; -.
DR   PhylomeDB; Q9UTA5; -.
DR   UniPathway; UPA00375; -.
DR   PRO; PR:Q9UTA5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; ISO:PomBase.
DR   GO; GO:0030488; P:tRNA methylation; ISO:PomBase.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; ISO:PomBase.
DR   Gene3D; 3.30.1960.10; -; 1.
DR   InterPro; IPR003827; tRNA_yW-synthesising.
DR   InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR   Pfam; PF02676; TYW3; 1.
DR   SUPFAM; SSF111278; SSF111278; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..237
FT                   /note="tRNA wybutosine-synthesizing protein 3"
FT                   /id="PRO_0000281848"
SQ   SEQUENCE   237 AA;  26997 MW;  29A6CF0D0C720997 CRC64;
     MNIKGIDVSF DAQKKEILEG LKSSVPDASP KGHPDSPIFP LLDVINSHPD WVTTSSCSGR
     ISVYVQGANS RKGGGYWLFV SHQAHEELPP VLEDEKVEYG KVPSSPVEGN REIQYAFEPM
     ILHVQTRSLA NAQHLQRVAA SCGFRETGIQ GSEQKFIVAI RTSLRMDIPI GCLTASEKLQ
     FYITREYMCF LFKRSVEYFT ENGNRMARLK EQLERQVEKR MKPRRKLRNM DDYLVQS
 
 
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