RSMG2_SYNFM
ID RSMG2_SYNFM Reviewed; 498 AA.
AC A0LHE3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G 2;
DE EC=2.1.1.170;
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase 2;
DE Short=16S rRNA m7G methyltransferase 2;
GN Name=rsmG2; OrderedLocusNames=Sfum_1152;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 527 of 16S rRNA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.170;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. RNA methyltransferase RsmG family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the class IV-like
CC SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH
CC family. {ECO:0000305}.
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DR EMBL; CP000478; ABK16845.1; -; Genomic_DNA.
DR RefSeq; WP_011698016.1; NC_008554.1.
DR AlphaFoldDB; A0LHE3; -.
DR SMR; A0LHE3; -.
DR STRING; 335543.Sfum_1152; -.
DR EnsemblBacteria; ABK16845; ABK16845; Sfum_1152.
DR KEGG; sfu:Sfum_1152; -.
DR eggNOG; COG0357; Bacteria.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_547381_0_0_7; -.
DR OMA; HPKALRA; -.
DR OrthoDB; 1089708at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1280.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF02527; GidB; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..498
FT /note="Ribosomal RNA small subunit methyltransferase G 2"
FT /id="PRO_0000342942"
FT REGION 1..230
FT /note="Methyltransferase G"
FT REGION 231..498
FT /note="Methyltransferase TrmH family"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 498 AA; 55106 MW; 7A99CEFDBB8C0AC5 CRC64;
MRNGTIRYPG SDAAPGPDEM SAILRRCGIR LAPARIGQLW TYHQLLREFN PELNLTRIHN
FANMVLKLYV DSLLPMNLVE LPSPLMDLGT GPGMPGIPIK IAMPELEIVL AESRQKRAAF
LKMAVERLKL EKVEVVGKSV GSSFEVPVKG VITRAVESVG ATLERIAGCL DRDGLAIFMK
GPQCDAEIGE ALKRFRGEYR LWRDIHYTIP HTRNERRLVV FQRLGPPTRI RKETAMKRHG
FRKIESENND LYRDIRKLLT SRGIRKQQRA LVSGSKQVHE TLRDFPDDCL AWIAPGQEMP
PPEGAPGHMS WYQMAPALFE TLDVFGTRTP LLLIKVGEIE TWDPVEGFPA GCSVLVPFQD
PENVGAVIRS AAAFGAVQVI LLRESAHPFH PKALRASGGA VLRMKLRNGP PLENLPENLP
ILPLSAEGRD ITRHVFPAAF GLLPGLEGPG LPDNWRRKSF AIPICKDVES LNAATAAAIA
LYAWSRSGSQ TKHSPAPA