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TYW32_PYRHO
ID   TYW32_PYRHO             Reviewed;         206 AA.
AC   O59533;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00266};
DE            EC=2.1.1.282 {ECO:0000255|HAMAP-Rule:MF_00266};
DE   AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw3 2 {ECO:0000255|HAMAP-Rule:MF_00266};
GN   Name=taw3-2 {ECO:0000255|HAMAP-Rule:MF_00266}; OrderedLocusNames=PH1887;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts
CC       as a component of the wyosine derivatives biosynthesis pathway.
CC       Probably methylates N-4 position of wybutosine-86 to produce
CC       wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00266};
CC   -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00266}.
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DR   EMBL; BA000001; BAA31009.1; -; Genomic_DNA.
DR   PIR; B71202; B71202.
DR   RefSeq; WP_010885947.1; NC_000961.1.
DR   AlphaFoldDB; O59533; -.
DR   SMR; O59533; -.
DR   STRING; 70601.3258326; -.
DR   EnsemblBacteria; BAA31009; BAA31009; BAA31009.
DR   GeneID; 1442729; -.
DR   KEGG; pho:PH1887; -.
DR   eggNOG; arCOG04156; Archaea.
DR   OMA; GFKYTTF; -.
DR   OrthoDB; 118297at2157; -.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031591; P:wybutosine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.1960.10; -; 1.
DR   HAMAP; MF_00266; TYW3_archaea; 1.
DR   InterPro; IPR022908; Taw3.
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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..206
FT                   /note="tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-
FT                   demethylwyosine(37)-N(4))-methyltransferase 2"
FT                   /id="PRO_0000157100"
SQ   SEQUENCE   206 AA;  23320 MW;  84A540AB4E3E7E95 CRC64;
     MKAKREALIS LFHAIKEEKV DSDIIDLLLL INSIKGIYTT SSCSGRIGIL EEPSLGAKPL
     SRWLIKVHRP MSFEEARDAL KRAREGLIFL KSQPPIFHVV AETIENAKLV HEIGLASGFK
     YTTFKAISSR FLVEINGTEY LTVPLGKDGR IIASDEYLKF AISIGNKMLE RGKSKLPRLR
     DNFEKIKKKL GEDPLFIQLK REILEI
 
 
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