(data stored in SCRATCH zone)

SWISSPROT: A5GRG6_SYNR3

ID   A5GRG6_SYNR3            Unreviewed;       229 AA.
AC   A5GRG6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=spoU {ECO:0000313|EMBL:CAK27475.1};
GN   Synonyms=trmH {ECO:0000256|HAMAP-Rule:MF_02060};
GN   OrderedLocusNames=SynRCC307_0572 {ECO:0000313|EMBL:CAK27475.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27475.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) 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:
CC       Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-
CC         COMP:10192, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC         EC=2.1.1.34; Evidence={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}.
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DR   EMBL; CT978603; CAK27475.1; -; Genomic_DNA.
DR   RefSeq; WP_011934990.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0572; -.
DR   EnsemblBacteria; CAK27475; CAK27475; SynRCC307_0572.
DR   KEGG; syr:SynRCC307_0572; -.
DR   eggNOG; ENOG4105FE8; Bacteria.
DR   eggNOG; COG0566; LUCA.
DR   HOGENOM; HOG000285175; -.
DR   KO; K00556; -.
DR   OMA; TAQGSQK; -.
DR   OrthoDB; 1422015at2; -.
DR   BioCyc; SSP316278:G1GJL-558-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0009020; F:tRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002938; P:tRNA guanine ribose methylation; IEA:UniProtKB-UniRule.
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; A5GRG6.
DR   SWISS-2DPAGE; A5GRG6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060,
KW   ECO:0000256|SAAS:SAAS00477853, ECO:0000313|EMBL:CAK27475.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
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:SAAS00477754, ECO:0000313|EMBL:CAK27475.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02060};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   DOMAIN       22    160       SpoU_methylase. {ECO:0000259|Pfam:
FT                                PF00588}.
FT   DOMAIN      165    219       SpoU_methylas_C. {ECO:0000259|Pfam:
FT                                PF12105}.
FT   REGION      121    125       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   BINDING      98     98       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   BINDING     141    141       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02060}.
FT   BINDING     150    150       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_02060}.
SQ   SEQUENCE   229 AA;  25468 MW;  6442D5B8D3E8A83D CRC64;
     MPLLPRRFER LRSVLKRRMA DLTVLMEAVE KPHNLSAILR TCDATGVFEA HAVSLKGRPR
     TFNSTAQGSQ KWVPIRDHDS VKDAFAELRA KGFRIYGTML GVNAVDYRSC DFTKPSAFVL
     GAEKWGLTAE AGDAVDQPVF IPMSGMVQSL NVSVAAATLL FEAVRQRQAA GLIPTQGEGL
     SPELFDQTLF EWAYPQVARW CRDTGRPYPG LSEEGELLEE LPRTVKLRC
//

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