GenomeNet

Database: UniProt
Entry: A0A1I5X5M0_9FIRM
LinkDB: A0A1I5X5M0_9FIRM
Original site: A0A1I5X5M0_9FIRM 
ID   A0A1I5X5M0_9FIRM        Unreviewed;       457 AA.
AC   A0A1I5X5M0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NOL1/NOP2/sun family putative RNA methylase {ECO:0000313|EMBL:SFQ27295.1};
GN   ORFNames=SAMN05444406_12220 {ECO:0000313|EMBL:SFQ27295.1};
OS   Caldicoprobacter faecalis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Caldicoprobacteraceae;
OC   Caldicoprobacter.
OX   NCBI_TaxID=937334 {ECO:0000313|EMBL:SFQ27295.1, ECO:0000313|Proteomes:UP000198577};
RN   [1] {ECO:0000313|EMBL:SFQ27295.1, ECO:0000313|Proteomes:UP000198577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20678 {ECO:0000313|EMBL:SFQ27295.1,
RC   ECO:0000313|Proteomes:UP000198577};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOXR01000022; SFQ27295.1; -; Genomic_DNA.
DR   RefSeq; WP_025747753.1; NZ_FOXR01000022.1.
DR   AlphaFoldDB; A0A1I5X5M0; -.
DR   STRING; 937334.SAMN05444406_12220; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000198577; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; 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; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000198577};
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          23..302
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         110..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   457 AA;  51725 MW;  990E16584D4A728D CRC64;
     MSNLPEDFVD KMKGLLGPEY PKFMACFKNP PYQGLRVNTL KIAIEDFLSL APFELKPVPW
     AEGGFYYGDQ DRPGKHPYYY AGLYYIQEPS AMAPAELLGV RPGHKVLDLC AAPGGKSFQI
     AARLKGKGFL LANEIDASRV IVLGENLERL GVRNAAITQE TPGRLAAVFK NYFDRILVDA
     PCSGEGMFRK RPDMCSVWSY TLPDRISVRQ KSILKHAAEM LAPGGRMVYS TCTFSPEENE
     GVVDWFLKEH PDFSLVEDVH FKWFDRGVPE WVNGSPELVK TFRLWPHKIK GEGHFMALFE
     KKADGGASTL PLFYKRRGIS KLPVEYECFM KEYMREFIED HLYVHKDQLY WIPPSLPDLS
     GLKVLRPGFR LGTIRKGRFI PGHALAMSAR KESVVQSIDF SSDSKEVMQY LEGFTLTGFD
     GKGWVLITVD GYSLGWGKLS DGLLKNYYPK GLRRVLT
//
DBGET integrated database retrieval system