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TRM56_PYRAB
ID   TRM56_PYRAB             Reviewed;         198 AA.
AC   Q9UYD1; G8ZJ01;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=tRNA (cytidine(56)-2'-O)-methyltransferase;
DE            EC=2.1.1.206;
DE   AltName: Full=tRNA ribose 2'-O-methyltransferase aTrm56;
GN   OrderedLocusNames=PYRAB15770; ORFNames=PAB1040;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   FUNCTION AS A METHYLTRANSFERASE, AND CATALYTIC ACTIVITY.
RX   PubMed=15987815; DOI=10.1261/rna.2110805;
RA   Renalier M.-H., Joseph N., Gaspin C., Thebault P., Mougin A.;
RT   "The Cm56 tRNA modification in archaea is catalyzed either by a specific
RT   2'-O-methylase, or a C/D sRNP.";
RL   RNA 11:1051-1063(2005).
CC   -!- FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose
CC       methylation of cytidine at position 56 in tRNAs.
CC       {ECO:0000269|PubMed:15987815}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42968, Rhea:RHEA-COMP:10308, Rhea:RHEA-COMP:10309,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.206;
CC         Evidence={ECO:0000269|PubMed:15987815};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000305}.
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DR   EMBL; AJ248288; CAB50481.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71034.1; -; Genomic_DNA.
DR   PIR; C75005; C75005.
DR   RefSeq; WP_010868694.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYD1; -.
DR   SMR; Q9UYD1; -.
DR   STRING; 272844.PAB1040; -.
DR   EnsemblBacteria; CAB50481; CAB50481; PAB1040.
DR   GeneID; 1495863; -.
DR   KEGG; pab:PAB1040; -.
DR   PATRIC; fig|272844.11.peg.1681; -.
DR   eggNOG; arCOG01857; Archaea.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   OMA; VVHLTMY; -.
DR   OrthoDB; 83050at2157; -.
DR   PhylomeDB; Q9UYD1; -.
DR   BRENDA; 2.1.1.206; 5242.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0002128; P:tRNA nucleoside ribose methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00077; tRNA_methyltr_aTrm56; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR002845; tRNA_mtfrase_aTrm56.
DR   PANTHER; PTHR42197; PTHR42197; 1.
DR   Pfam; PF01994; Trm56; 1.
DR   PIRSF; PIRSF016123; UCP016123; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..198
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000146933"
FT   REGION          178..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         128..135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   198 AA;  22262 MW;  D126B48B3A0D5AAC CRC64;
     MIVVLRLGHR PERDKRVTTH VALTARAFGA DGIIIVSEEV DLKVKESVED VVERWGGPFF
     VKFEKSWRKV MKEFDGVKVH LTMYGIHIDD IIDELREKLR EGRDFMVIVG AEKVPREVYE
     LADYNVAIGN QPHSEVAALA VFLDRLLEGK GLRKEFKGAK LKIIPQARGK MVVEVQKDAK
     QAEASGEGAS RKNGQLPS
 
 
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