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Database: UniProt
Entry: A0A4Q1ZVT2_9FIRM
LinkDB: A0A4Q1ZVT2_9FIRM
Original site: A0A4Q1ZVT2_9FIRM 
ID   A0A4Q1ZVT2_9FIRM        Unreviewed;       446 AA.
AC   A0A4Q1ZVT2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:RXV60020.1};
GN   ORFNames=DWB64_14010 {ECO:0000313|EMBL:RXV60020.1};
OS   Fusibacter sp. A1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=2283630 {ECO:0000313|EMBL:RXV60020.1, ECO:0000313|Proteomes:UP000290764};
RN   [1] {ECO:0000313|EMBL:RXV60020.1, ECO:0000313|Proteomes:UP000290764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:RXV60020.1,
RC   ECO:0000313|Proteomes:UP000290764};
RA   Yadav S., Villanueva L., Damste J.S.S.;
RT   "Draft genome sequence of Fusibacter sp. A1 isolated from Black Sea.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {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   -!- 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:RXV60020.1}.
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DR   EMBL; QQWI01000009; RXV60020.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q1ZVT2; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000290764; 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: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; 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; 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:UP000290764};
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          22..298
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        231
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         109..115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   446 AA;  50281 MW;  9C79090506951A1C CRC64;
     MHLPEKFISQ MKDVFGNDFD AYLASFSLPR EAGLRVNLNK ITPEEFEKIC PFKLERIPWT
     TDGYYVDPDL RPAKHPFYHA GLYYMQEPSA MAPVNTMHIE NGERILDLCS APGGKTLQIA
     NRVGESGLVV SNDISASRLR AVVKNIEQFG LKNVIITSEQ VDKLANLQRE FYDRILVDAP
     CSGEGMFRKD PSIAASWSEA SNDEYHAIQS SLAEGVQPML KGGGQFLYST CTFSPVENES
     VIEGLLNAHS ELTIEDIDSE YFEDGIAIGG DERLRSAKRL YPFKLRGEGH FLASLIKDGR
     LEANVNPQKD QPAPEELQAF MKEVLHEPIV GSFRVHNDKI LLDPQAVPDL KGIRVLRRGW
     LLGELVKGRF EPAQSFAMGL KKEWIKNTIT FGYEEIEVVK YLKCETLHVD YPNGWYVVCM
     GDFPLGWAKV VNGQLKNKYP AAWRMV
//
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