TAW22_PYRAB
ID TAW22_PYRAB Reviewed; 333 AA.
AC Q9V2G1; G8ZFU8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=tRNA (guanine(37)-N1)/4-demethylwyosine(37)-methyltransferase Taw22 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:27852927, ECO:0000305|PubMed:20382657};
DE EC=2.1.1.228 {ECO:0000269|PubMed:20382657, ECO:0000269|PubMed:27852927};
DE AltName: Full=M1G-methyltransferase;
DE AltName: Full=tRNA [GM37] methyltransferase;
DE AltName: Full=tRNA(Phe):m1G/imG2 methyltransferase {ECO:0000303|PubMed:27852927};
GN Name=taw22 {ECO:0000303|PubMed:27852927};
GN Synonyms=trm5a {ECO:0000303|PubMed:20382657}; OrderedLocusNames=PYRAB01130;
GN ORFNames=PAB2272;
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-133; PHE-165; GLU-173;
RP ARG-174; GLU-213; PRO-260 AND PRO-262.
RX PubMed=27852927; DOI=10.1261/rna.057059.116;
RA Urbonavicius J., Rutkiene R., Lopato A., Tauraite D., Stankeviciute J.,
RA Aucynaite A., Kaliniene L., van Tilbeurgh H., Meskys R.;
RT "Evolution of tRNAPhe:imG2 methyltransferases involved in the biosynthesis
RT of wyosine derivatives in Archaea.";
RL RNA 22:1871-1883(2016).
RN [5] {ECO:0007744|PDB:5HJI, ECO:0007744|PDB:5HJJ, ECO:0007744|PDB:5HJK, ECO:0007744|PDB:5HJM}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND SAM ANALOGS.
RX PubMed=27629654; DOI=10.1038/srep33553;
RA Wang C., Jia Q., Chen R., Wei Y., Li J., Ma J., Xie W.;
RT "Crystal structures of the bifunctional tRNA methyltransferase Trm5a.";
RL Sci. Rep. 6:33553-33553(2016).
CC -!- FUNCTION: Catalyzes both the N1-methylation of guanosine and the C7-
CC methylation of 4-demethylwyosine (imG-14) at position 37 in tRNA(Phe).
CC {ECO:0000269|PubMed:20382657, ECO:0000269|PubMed:27852927}.
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, ECO:0000269|PubMed:27852927};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC H(+) + isowyosine(37) in tRNA(Phe) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53056, Rhea:RHEA-COMP:10164, Rhea:RHEA-COMP:13445,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:64315, ChEBI:CHEBI:136979;
CC Evidence={ECO:0000269|PubMed:27852927, ECO:0000305|PubMed:20382657};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Less efficient than Trm5b and appears to be selective
CC for methylating tRNA(Phe). {ECO:0000305|PubMed:20382657}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000255|PROSITE-ProRule:PRU01021}.
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DR EMBL; AJ248283; CAB49037.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69489.1; -; Genomic_DNA.
DR PIR; F75198; F75198.
DR RefSeq; WP_010867237.1; NC_000868.1.
DR PDB; 5HJI; X-ray; 2.20 A; A=1-333.
DR PDB; 5HJJ; X-ray; 2.00 A; A=1-333.
DR PDB; 5HJK; X-ray; 2.00 A; A=1-333.
DR PDB; 5HJM; X-ray; 1.76 A; A=1-333.
DR PDB; 5WT1; X-ray; 2.60 A; A/B=1-333.
DR PDB; 5WT3; X-ray; 3.20 A; A=1-333.
DR PDBsum; 5HJI; -.
DR PDBsum; 5HJJ; -.
DR PDBsum; 5HJK; -.
DR PDBsum; 5HJM; -.
DR PDBsum; 5WT1; -.
DR PDBsum; 5WT3; -.
DR AlphaFoldDB; Q9V2G1; -.
DR SMR; Q9V2G1; -.
DR STRING; 272844.PAB2272; -.
DR EnsemblBacteria; CAB49037; CAB49037; PAB2272.
DR GeneID; 1495000; -.
DR KEGG; pab:PAB2272; -.
DR PATRIC; fig|272844.11.peg.126; -.
DR eggNOG; arCOG00033; Archaea.
DR HOGENOM; CLU_022610_0_1_2; -.
DR OMA; FNPRMKG; -.
DR OrthoDB; 55502at2157; -.
DR PhylomeDB; Q9V2G1; -.
DR BioCyc; MetaCyc:MON-18045; -.
DR BRENDA; 2.1.1.228; 5242.
DR BRENDA; 2.1.1.282; 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 Pfam; PF02475; Met_10; 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..333
FT /note="tRNA (guanine(37)-N1)/4-demethylwyosine(37)-
FT methyltransferase Taw22"
FT /id="PRO_0000407847"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021,
FT ECO:0000305|PubMed:27852927"
FT BINDING 191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:27852927"
FT BINDING 213..214
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021,
FT ECO:0000305|PubMed:27852927"
FT BINDING 243..244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021,
FT ECO:0000305|PubMed:27852927"
FT MUTAGEN 133
FT /note="R->A: Strong decrease in both activities."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 165
FT /note="F->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 173
FT /note="E->A: Decrease in both activities."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 174
FT /note="R->A: Decrease in both activities."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 213
FT /note="E->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 260
FT /note="P->N: Lack of tRNA(Phe):m1G methyltransferase
FT activity, but does not affect tRNA(Phe):imG2
FT methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:27852927"
FT MUTAGEN 262
FT /note="P->A: Strong decrease in both activities."
FT /evidence="ECO:0000269|PubMed:27852927"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5WT1"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5WT1"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:5HJM"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5HJM"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5WT3"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 234..242
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 275..286
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5HJM"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 307..319
FT /evidence="ECO:0007829|PDB:5HJM"
FT STRAND 322..332
FT /evidence="ECO:0007829|PDB:5HJM"
SQ SEQUENCE 333 AA; 38478 MW; E2691A16D455F5C0 CRC64;
MSGVKVRRED AKKVLELLKS VGILDGKRKA IRDEKYVIFP VTDTNIAKSL GLEVVDVELP
MRPERQIYKN LEDLLPREIF KKLGRLDIVG DIAIVSIPDE ILSEREVIVS AIRKLYPKVK
VIARRGFHSG LYRIRELEVI WGENRLHTIH KENGVLIKVD LSKVFFNPRM KGERYRIAQL
VNDGERILVP FAGVIPYPLV IARFKNVEVY AVEINEFAVK LAEENLELNR DRLKGKIKII
HGDVFEVLPN LPNFDRVVSP TPKGVDALSL TLSKAEKFLH YYDFVHESEI ERFRERVLEE
CRRQGKECRV SVRKVSDYKP HVYKVCADVE ILS
