TRM5B_PYRAB
ID TRM5B_PYRAB Reviewed; 330 AA.
AC Q9V0Q0; G8ZGU0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase Trm5b;
DE EC=2.1.1.228 {ECO:0000269|PubMed:20382657};
DE AltName: Full=M1G-methyltransferase;
DE AltName: Full=tRNA [GM37] methyltransferase;
GN Name=trm5b {ECO:0000303|PubMed:20382657}; OrderedLocusNames=PYRAB07390;
GN ORFNames=PAB0505;
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, CATALYTIC ACTIVITY, AND GENE NAME.
RX PubMed=20382657; DOI=10.1093/molbev/msq096;
RA de Crecy-Lagard V., Brochier-Armanet C., Urbonavicius J., Fernandez B.,
RA Phillips G., Lyons B., Noma A., Alvarez S., Droogmans L., Armengaud J.,
RA Grosjean H.;
RT "Biosynthesis of wyosine derivatives in tRNA: an ancient and highly diverse
RT pathway in Archaea.";
RL Mol. Biol. Evol. 27:2062-2077(2010).
CC -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC various tRNAs. {ECO:0000269|PubMed:20382657}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC Evidence={ECO:0000269|PubMed:20382657};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000255|PROSITE-ProRule:PRU01021}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCE70135.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248285; CAB49653.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70135.1; ALT_INIT; Genomic_DNA.
DR PIR; D75117; D75117.
DR RefSeq; WP_010867861.1; NC_000868.1.
DR PDB; 5YAC; X-ray; 3.30 A; A=1-330.
DR PDBsum; 5YAC; -.
DR AlphaFoldDB; Q9V0Q0; -.
DR SMR; Q9V0Q0; -.
DR STRING; 272844.PAB0505; -.
DR EnsemblBacteria; CAB49653; CAB49653; PAB0505.
DR GeneID; 1495648; -.
DR KEGG; pab:PAB0505; -.
DR PATRIC; fig|272844.11.peg.779; -.
DR eggNOG; arCOG00033; Archaea.
DR HOGENOM; CLU_022610_0_1_2; -.
DR OMA; HYYDIQH; -.
DR OrthoDB; 55502at2157; -.
DR PhylomeDB; Q9V0Q0; -.
DR BioCyc; MetaCyc:MON-18046; -.
DR BRENDA; 2.1.1.228; 5242.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR040601; Trm5_N.
DR Pfam; PF02475; Met_10; 1.
DR Pfam; PF18093; Trm5_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..330
FT /note="tRNA (guanine(37)-N1)-methyltransferase Trm5b"
FT /id="PRO_0000407848"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 211..212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 238..239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5YAC"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 129..141
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:5YAC"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:5YAC"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 268..280
FT /evidence="ECO:0007829|PDB:5YAC"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:5YAC"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:5YAC"
SQ SEQUENCE 330 AA; 37852 MW; BFB08D93E08773A0 CRC64;
MTLAVKVPLK EGEIVRRRLI ELGALDNTYK IKREGNFLLI PVKFPVKGFE VVEAELEQVS
RRPNSYREIV NVPQELRRFL PTSFDIIGNI AIIEIPEELK GYAKEIGRAI VEVHKNVKAV
YMKGSKIEGE YRTRELIHIA GENITETIHR ENGIRLKLDV AKVYFSPRLA TERMRVFKMA
QEGEVVFDMF AGVGPFSILL AKKAELVFAC DINPWAIKYL EENIKLNKVN NVVPILGDSR
EIEVKADRII MNLPKYAHEF LEHAISCIND GGVIHYYGFG PEGDPYGWHL ERIRELANKF
GVKVEVLGKR VIRNYAPRQY NIAIDFRVSF
