TAW21_SACS2
ID TAW21_SACS2 Reviewed; 262 AA.
AC Q97W08;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=tRNA 4-demethylwyosine(37)-methyltransferase Taw21 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:27852927};
DE AltName: Full=tRNA(Phe):imG2 methyltransferase {ECO:0000303|PubMed:27852927};
GN Name=taw21 {ECO:0000303|PubMed:27852927};
GN OrderedLocusNames=SSO2439 {ECO:0000312|EMBL:AAK42582.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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 the C7-methylation of 4-demethylwyosine (imG-14) at
CC position 37 in tRNA(Phe). {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; AE006641; AAK42582.1; -; Genomic_DNA.
DR PIR; G90415; G90415.
DR AlphaFoldDB; Q97W08; -.
DR SMR; Q97W08; -.
DR STRING; 273057.SSO2439; -.
DR EnsemblBacteria; AAK42582; AAK42582; SSO2439.
DR KEGG; sso:SSO2439; -.
DR PATRIC; fig|273057.12.peg.2520; -.
DR eggNOG; arCOG00033; Archaea.
DR HOGENOM; CLU_022610_0_0_2; -.
DR InParanoid; Q97W08; -.
DR OMA; HYYDIQH; -.
DR PhylomeDB; Q97W08; -.
DR BRENDA; 2.1.1.282; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
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..262
FT /note="tRNA 4-demethylwyosine(37)-methyltransferase Taw21"
FT /id="PRO_0000439043"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9V2G1"
FT BINDING 148..149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 175..176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
SQ SEQUENCE 262 AA; 30468 MW; 4288B9F19B62E822 CRC64;
MKTLIKRLQD QQDIWKRIEI VGDIVIIGVP FNKKPEDLVE IANEILSTFP YVKSVWGRHR
DVNGTYRLST YVHLAGEKRS ETVYKEHKCK YFLDFTKVFF SEKLSYEHLR VATQVKRDEI
IINMFSGFGP FSILSAVLGR PKIVYSIDLN PYAYYYMMVN VELNKAYEVL PIYGDAFKRI
YELEDADRII APLPELADKA YEVALQKVKK GGIIHLYTEV ETNKGEDPVR IAMNKYRGSY
FGRIVRSVNP HKYHVVVDIK AN
