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Database: UniProt
Entry: A0A090IGL3_9GAMM
LinkDB: A0A090IGL3_9GAMM
Original site: A0A090IGL3_9GAMM 
ID   A0A090IGL3_9GAMM        Unreviewed;       378 AA.
AC   A0A090IGL3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000256|HAMAP-Rule:MF_01551};
DE            EC=2.1.1.186 {ECO:0000256|HAMAP-Rule:MF_01551};
DE   AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01551};
DE   AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000256|HAMAP-Rule:MF_01551};
GN   Name=rlmM {ECO:0000256|HAMAP-Rule:MF_01551,
GN   ECO:0000313|EMBL:CED61765.1};
GN   ORFNames=MVIS_3872 {ECO:0000313|EMBL:CED61765.1}, NVI5450_2210
GN   {ECO:0000313|EMBL:SGY99581.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED61765.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CED61765.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hjerde Erik;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SGY99581.1, ECO:0000313|Proteomes:UP000183794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NVI 5450 {ECO:0000313|EMBL:SGY99581.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01551}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42788, Rhea:RHEA-COMP:10244, Rhea:RHEA-COMP:10245,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.186;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01551};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01551}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. RlmM subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01551}.
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DR   EMBL; LN554852; CED61765.1; -; Genomic_DNA.
DR   EMBL; FPLD01000060; SGY99581.1; -; Genomic_DNA.
DR   RefSeq; WP_045111844.1; NZ_FRDV01000086.1.
DR   STRING; 80854.MVIS_3872; -.
DR   KEGG; mvs:MVIS_3872; -.
DR   PATRIC; fig|80854.5.peg.4097; -.
DR   HOGENOM; CLU_043780_0_0_6; -.
DR   OrthoDB; 154490at2; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
DR   Proteomes; UP000183794; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2300.20; -; 1.
DR   Gene3D; 3.30.70.2810; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01551; 23SrRNA_methyltr_M; 1.
DR   InterPro; IPR040739; RlmM_FDX.
DR   InterPro; IPR048646; RlmM_THUMP-like.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR011224; rRNA_MeTrfase_M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR37524; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE M; 1.
DR   PANTHER; PTHR37524:SF2; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE M; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF18125; RlmM_FDX; 1.
DR   Pfam; PF21239; RLMM_N; 1.
DR   PIRSF; PIRSF028774; UCP028774; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01551};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01551}; Reference proteome {ECO:0000313|Proteomes:UP000032438};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01551};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01551};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01551}.
FT   DOMAIN          1..71
FT                   /note="RlmM ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18125"
FT   DOMAIN          84..163
FT                   /note="Ribosomal RNA large subunit methyltransferase M
FT                   THUMP-like"
FT                   /evidence="ECO:0000259|Pfam:PF21239"
FT   DOMAIN          185..298
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-1"
FT   BINDING         187
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-2"
FT   BINDING         220..223
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-2"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-2"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-2"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-2"
SQ   SEQUENCE   378 AA;  43065 MW;  1470D26FE1EC0FD3 CRC64;
     MNGILLYCRP GYEKECAAEI QARATAMEAY GFAKVTLNSG YVVFECHSAE DVDSIAKKLP
     LSSLIFARQM IALHARVDDM PLYDRVNPVV AACDGIEAMG ELRVEMPDTN EGKELSKFCR
     KYTVPLRQSL RKGDHLLPKE NKNRPVLHVF FITNTSVYIG YSYSFNNSPL PMGIMRLKFP
     SKAPSRSTLK LEEAFHTFIP ADQWDKRIGG AMRAVDLGAC PGGWTYQLVQ RSMFVVAIDN
     GAMADSLMET GQVKHFEEDG FKYEPAKTTI AWTNRKLNGN KIKVPENPPV DMLVCDMIEK
     PERVARLMCK WLLNAWCKEA IFNLKLPLKR RYHTLEDCLA ILDKQLDDRF VIQAKHLYHD
     RDEVTVHVAW AHFIPEDK
//
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