(data stored in SCRATCH zone)

SWISSPROT: C5B9B1_EDWI9

ID   C5B9B1_EDWI9            Unreviewed;       230 AA.
AC   C5B9B1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
DE            EC=2.1.1.34 {ECO:0000256|HAMAP-Rule:MF_02060};
DE   AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
GN   Name=trmH {ECO:0000256|HAMAP-Rule:MF_02060};
GN   OrderedLocusNames=NT01EI_0031 {ECO:0000313|EMBL:ACR67291.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67291.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position
CC       18 in tRNA. {ECO:0000256|HAMAP-Rule:MF_02060}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanosine(18) in
CC       tRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine(18) in
CC       tRNA. {ECO:0000256|HAMAP-Rule:MF_02060}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase TrmH family.
CC       {ECO:0000256|HAMAP-Rule:MF_02060}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02060}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001600; ACR67291.1; -; Genomic_DNA.
DR   RefSeq; WP_015869515.1; NC_012779.2.
DR   ProteinModelPortal; C5B9B1; -.
DR   STRING; 634503.NT01EI_0031; -.
DR   EnsemblBacteria; ACR67291; ACR67291; NT01EI_0031.
DR   GeneID; 7959350; -.
DR   KEGG; eic:NT01EI_0031; -.
DR   PATRIC; fig|634503.3.peg.28; -.
DR   eggNOG; ENOG4105FE8; Bacteria.
DR   eggNOG; COG0566; LUCA.
DR   HOGENOM; HOG000285175; -.
DR   KO; K00556; -.
DR   OMA; TDRYQHV; -.
DR   OrthoDB; POG091H00AR; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002938; P:tRNA guanine ribose methylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_02060; tRNA_methyltr_TrmH; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR022724; rRNA_MeTrfase_SpoU_C.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR033671; TrmH.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   Pfam; PF12105; SpoU_methylas_C; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B9B1.
DR   SWISS-2DPAGE; C5B9B1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060,
KW   ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:ACR67291.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_02060};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_02060};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02060,
KW   ECO:0000256|SAAS:SAAS00121476, ECO:0000313|EMBL:ACR67291.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02060};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   DOMAIN       20    159       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   DOMAIN      163    217       SpoU_methylas_C. {ECO:0000259|Pfam:
FT                                PF12105}.
FT   BINDING      96     96       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   BINDING     139    139       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   BINDING     148    148       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02060}.
SQ   SEQUENCE   230 AA;  25269 MW;  6972A0E00E31B1E2 CRC64;
     MTPQRYARIC QMMAARQPDL TVCMEQVHKP HNVSAVIRTA DAVGVHQVHA VWPGKSMRTL
     VSTAAGSNSW VSVKTHRDIA AAVGELKGQG MQILATNLSA TAVDFREIDY TRPTCILMGQ
     EKRGISAEAL QLADRDIIIP MVGMVQSLNV SVASALILYE AQRQRQQAGM YGRSQPSLNE
     EQQQRLLWEG GYPVLASVAR RKGLARPHIA NDGQIDAPQA WWDAMQAARS
//

If you have problems or comments...

PBIL Back to PBIL home page