ID N9RYL0_9GAMM Unreviewed; 338 AA.
AC N9RYL0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000256|HAMAP-Rule:MF_01862};
DE EC=2.1.1.172 {ECO:0000256|HAMAP-Rule:MF_01862};
DE AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN Name=rsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN ORFNames=F885_01038 {ECO:0000313|EMBL:ENX63039.1};
OS Acinetobacter higginsii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70347 {ECO:0000313|EMBL:ENX63039.1, ECO:0000313|Proteomes:UP000013100};
RN [1] {ECO:0000313|EMBL:ENX63039.1, ECO:0000313|Proteomes:UP000013100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 3880 {ECO:0000313|EMBL:ENX63039.1,
RC ECO:0000313|Proteomes:UP000013100};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. ANC 3880.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC rRNA in the 30S particle. {ECO:0000256|HAMAP-Rule:MF_01862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42736, Rhea:RHEA-COMP:10213, Rhea:RHEA-COMP:10214,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.172;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01862};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01862}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC {ECO:0000256|HAMAP-Rule:MF_01862}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENX63039.1}.
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DR EMBL; APSD01000015; ENX63039.1; -; Genomic_DNA.
DR RefSeq; WP_005322553.1; NZ_KB850223.1.
DR AlphaFoldDB; N9RYL0; -.
DR PATRIC; fig|1217701.3.peg.1012; -.
DR HOGENOM; CLU_049581_0_0_6; -.
DR Proteomes; UP000013100; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR HAMAP; MF_01862; 16SrRNA_methyltr_C; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR013675; Mtase_sm_N.
DR InterPro; IPR023543; rRNA_ssu_MeTfrase_C.
DR InterPro; IPR046977; RsmC/RlmG.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR PANTHER; PTHR47816:SF4; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF08468; MTS_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862,
KW ECO:0000313|EMBL:ENX63039.1};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01862};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01862};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01862, ECO:0000313|EMBL:ENX63039.1}.
FT DOMAIN 5..156
FT /note="Methyltransferase small N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08468"
FT DOMAIN 165..333
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 338 AA; 38036 MW; BE6B4C761A503C86 CRC64;
MDPRSEVVIR QQDYLSGQVL LINAPNDQLA KTLPNKVQAS VWTWNYADHQ GFISSGIRSH
FSVEFPQAQF DQVVIFVPKS KELLNYILHV VVSHLKLDQN IFLVGEKKGG VERAAKQLLQ
YGKTLKLDSA RHCQLWQMKI ERTEQLKPLE HWLKTYTVQI DQEQLNICAL PGVFSQDHLD
VGTAVLVPYL SQVKSGKIAD FGCGAGIISA YLAKLDSNRQ IFALDVDAFA LRSTELTFQR
NGLNLTQLNL QAVTGFVDAP NDLDAIVSNP PFHQGIHTNY DASEELCQRA KRHLKNSGEL
WIVANRFLNY PPLIEQSFGE CLVKADQQGF KVLYACAK
//
