TRCM_PYRAB
ID TRCM_PYRAB Reviewed; 311 AA.
AC Q9V106; G8ZJ90;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA (cytosine(49)-C(5))-methyltransferase;
DE EC=2.1.1.-;
GN OrderedLocusNames=PYRAB06230; ORFNames=PAB1947;
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, TRNA-BINDING, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP SUBUNIT.
RX PubMed=17470432; DOI=10.1074/jbc.m607459200;
RA Auxilien S., El Khadali F., Rasmussen A., Douthwaite S., Grosjean H.;
RT "Archease from Pyrococcus abyssi improves substrate specificity and
RT solubility of a tRNA m5C methyltransferase.";
RL J. Biol. Chem. 282:18711-18721(2007).
CC -!- FUNCTION: Catalyzes AdoMet-dependent formation of m5C in tRNA. In the
CC presence of protein archease, specifically methylates the cytosine at
CC position 49 (m5C49) of tRNA. In the absence of archease, catalyzes the
CC formation of m5C at many locations in tRNAs or rRNAs.
CC {ECO:0000269|PubMed:17470432}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(49) in tRNA precursor + S-adenosyl-L-methionine = 5-
CC methylcytidine(49) in tRNA precursor + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54140, Rhea:RHEA-COMP:13804, Rhea:RHEA-
CC COMP:13805, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:17470432};
CC -!- ACTIVITY REGULATION: Substrate specificity and tendency to aggregate
CC are influenced by archease. {ECO:0000269|PubMed:17470432}.
CC -!- SUBUNIT: Forms a tripartite complex with archease and tRNA. Binds only
CC the oligomeric forms of the archease. {ECO:0000269|PubMed:17470432}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AJ248284; CAB49545.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70017.1; -; Genomic_DNA.
DR PIR; B75183; B75183.
DR RefSeq; WP_010867747.1; NC_000868.1.
DR AlphaFoldDB; Q9V106; -.
DR SMR; Q9V106; -.
DR STRING; 272844.PAB1947; -.
DR EnsemblBacteria; CAB49545; CAB49545; PAB1947.
DR GeneID; 1495530; -.
DR KEGG; pab:PAB1947; -.
DR PATRIC; fig|272844.11.peg.663; -.
DR eggNOG; arCOG00973; Archaea.
DR HOGENOM; CLU_005316_7_0_2; -.
DR OMA; PQDNDTE; -.
DR OrthoDB; 32049at2157; -.
DR PhylomeDB; Q9V106; -.
DR BRENDA; 2.1.1.B43; 5242.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; RNA-binding; S-adenosyl-L-methionine;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..311
FT /note="tRNA (cytosine(49)-C(5))-methyltransferase"
FT /id="PRO_0000406990"
FT ACT_SITE 239
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 118..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 311 AA; 35747 MW; F34CA8839F39B962 CRC64;
MDYKEEFKKI NKKLVERYSK LDDSEEFWAY LYKPLRPSIR INTLKGNLKE IKALLEEKFE
LEPIPWTKGE GFYIKSYDVN YGQLIEYSLG LIIPQEASSM IPPVVLDPKP SEVILDMAAA
PGSKTTQMAQ YMENEGCIIA NDAKRDRANI LIANLTRAGV LIAKVTVKDG AYFARYENTF
DRVLLDAPCS SVGMIRKNFK FARTWSIGKV YYHSRLQKRL ILAAYKSLKP GGVLVYSTCT
VDPLENEEVV DFLLQKTDAK LEKVKLPLKT SEPVIEWEGR KYSDEVRKTI RIHPQDNDTE
AFYIAKIRKP R
