GenomeNet

Database: UniProt
Entry: A0A0A1GXE2_9LACO
LinkDB: A0A0A1GXE2_9LACO
Original site: A0A0A1GXE2_9LACO 
ID   A0A0A1GXE2_9LACO        Unreviewed;       448 AA.
AC   A0A0A1GXE2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=23S rRNA methyltransferase {ECO:0000313|EMBL:BAP85603.1};
GN   ORFNames=LOOC260_110640 {ECO:0000313|EMBL:BAP85603.1};
OS   Paucilactobacillus hokkaidonensis JCM 18461.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Paucilactobacillus.
OX   NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP85603.1, ECO:0000313|Proteomes:UP000031620};
RN   [1] {ECO:0000313|EMBL:BAP85603.1, ECO:0000313|Proteomes:UP000031620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LOOC260 {ECO:0000313|EMBL:BAP85603.1,
RC   ECO:0000313|Proteomes:UP000031620};
RA   Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT   "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT   LOOC260T.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP014680; BAP85603.1; -; Genomic_DNA.
DR   RefSeq; WP_041093502.1; NZ_AP014680.1.
DR   AlphaFoldDB; A0A0A1GXE2; -.
DR   STRING; 1291742.LOOC260_110640; -.
DR   KEGG; lho:LOOC260_110640; -.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   Proteomes; UP000031620; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          1..296
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        226
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         104..110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   448 AA;  50893 MW;  65248ECA98BE3D79 CRC64;
     MKLPIEFIHK YQQLLGDEAK EFLASFQEKS YSGYRINPLK PDFVIDQNYL TNEKIEYCDT
     GFFGSVNGKS IDHTVGYLYS QEPSAMYVGE VADPKPNERV LDLCAAPGGK STHLVSKMNN
     EGLLVSNEIF KKRATILAEN LERWGAKNTI ITNESPEKLA PRFLNFFDRI LVDAPCSGEG
     MFRKDPEAVS YWNIDYPLEC ANRQRKILAS AMEMLKPGGT LIYSTCTFAP EEDEQIIAWL
     LTNYPTLSVE PIKKYTNMDS GRPEWADNNS ELAKTVRLFP HHIKGEGHFI AKLKLAGNDI
     SNKNQFQQTS KLTKEQVTLF NDFTQTVLNQ INFNSLITFG DQLYSIPDGV PSLDHLSVIR
     PGLHLGTFKK KRFEPSFALA LALDSSSVKN KIKITEEQWR EYVHGDTIKL DHDLEKGWYL
     LTCQGHSVCF GKAVNRTVKN FYPKGLRF
//
DBGET integrated database retrieval system