TAW22_NANEQ
ID TAW22_NANEQ Reviewed; 297 AA.
AC Q74NE4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=tRNA (guanine(37)-N1)/4-demethylwyosine(37)-methyltransferase Taw22 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:27852927};
DE EC=2.1.1.228 {ECO:0000269|PubMed:27852927};
DE AltName: Full=tRNA(Phe):m1G/imG2 methyltransferase {ECO:0000303|PubMed:27852927};
GN Name=taw22 {ECO:0000303|PubMed:27852927};
GN OrderedLocusNames=NEQ228 {ECO:0000312|EMBL:AAR39082.1};
OS Nanoarchaeum equitans (strain Kin4-M).
OC Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC Nanoarchaeaceae; Nanoarchaeum.
OX NCBI_TaxID=228908;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kin4-M;
RX PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA Stetter K.O., Short J.M., Noorderwier M.;
RT "The genome of Nanoarchaeum equitans: insights into early archaeal
RT evolution and derived parasitism.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
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: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: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};
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}.
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DR EMBL; AE017199; AAR39082.1; -; Genomic_DNA.
DR AlphaFoldDB; Q74NE4; -.
DR SMR; Q74NE4; -.
DR STRING; 228908.NEQ228; -.
DR EnsemblBacteria; AAR39082; AAR39082; NEQ228.
DR KEGG; neq:NEQ228; -.
DR PATRIC; fig|228908.8.peg.234; -.
DR HOGENOM; CLU_022610_0_0_2; -.
DR BRENDA; 2.1.1.228; 8261.
DR BRENDA; 2.1.1.282; 8261.
DR Proteomes; UP000000578; 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 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 Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..297
FT /note="tRNA (guanine(37)-N1)/4-demethylwyosine(37)-
FT methyltransferase Taw22"
FT /id="PRO_0000439044"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9V2G1"
FT BINDING 128..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
SQ SEQUENCE 297 AA; 35106 MW; E8F172424BD4F66D CRC64;
MSYDIIGEIA IIYPPVDDLD KIVNKILKHH KYVKAIYLKT DKLETELRLP KLKLLYGEPI
LETTYKENKC VFKLRVDKVY FSPRLSTERK EFIDLVKDNE KILIPFAGVN PYPIVIAKHR
KVQIKSIELN PWAVKYGIIN TKLNKVNVDT ILADFGIAWK YIRNLHNKEG IVTKYVNELL
KAKPELDLVY TNEEYYDLLN QYYNTKLIEE LKPGIEYFDR IIMPLPKGGE HFIFEALVLA
KKYIHLYSFA HEKEIEQKVK EIIDIASQLR EIKHYDYKIV GDIGVRKYRI RINIYLI
