(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ22_SHESH

ID   A8FQ22_SHESH            Unreviewed;       231 AA.
AC   A8FQ22;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 56.
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=Ssed_0332 {ECO:0000313|EMBL:ABV34945.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34945.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34945.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34945.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34945.1; -; Genomic_DNA.
DR   RefSeq; WP_012004471.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ22; -.
DR   STRING; 425104.Ssed_0332; -.
DR   EnsemblBacteria; ABV34945; ABV34945; Ssed_0332.
DR   KEGG; sse:Ssed_0332; -.
DR   eggNOG; ENOG4105FE8; Bacteria.
DR   eggNOG; COG0566; LUCA.
DR   HOGENOM; HOG000285175; -.
DR   KO; K00556; -.
DR   OMA; TDRYQHV; -.
DR   OrthoDB; POG091H00AR; -.
DR   BioCyc; SSED425104:GH7Q-341-MONOMER; -.
DR   Proteomes; UP000002015; 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; A8FQ22.
DR   SWISS-2DPAGE; A8FQ22.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060,
KW   ECO:0000256|SAAS:SAAS00120900, ECO:0000313|EMBL:ABV34945.1};
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:ABV34945.1};
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    216       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   231 AA;  26059 MW;  DDE0B2424584A759 CRC64;
     MSPERFARIN EMLDNRQPDL TLCLDKVHKT NNIAAVIRTA DAVGIHQVHA IWPDLDMRVS
     GNTASGSQQW VKTIRHDHMD EAQTQFRAQG MQILATNFSE DAVDFREIDY TRPTAIILGN
     ERDGVSPEGI AAADQHIIIP MIGMVQSLNV SVASALIMYE AQRQREAAGM YGQRRLDEDY
     CQVKLFEQGH PIYAKACRRK SIPYPKVDAL GQIVADAAWW ERMRSPQKAV K
//

If you have problems or comments...

PBIL Back to PBIL home page