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Database: UniProt
Entry: A0A261F410_9BIFI
LinkDB: A0A261F410_9BIFI
Original site: A0A261F410_9BIFI 
ID   A0A261F410_9BIFI        Unreviewed;       518 AA.
AC   A0A261F410;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NOL1/NOP2/sun family {ECO:0000313|EMBL:OZG53656.1};
GN   ORFNames=ALMA_1221 {ECO:0000313|EMBL:OZG53656.1};
OS   Alloscardovia macacae.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Alloscardovia.
OX   NCBI_TaxID=1160091 {ECO:0000313|EMBL:OZG53656.1, ECO:0000313|Proteomes:UP000243657};
RN   [1] {ECO:0000313|EMBL:OZG53656.1, ECO:0000313|Proteomes:UP000243657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24762 {ECO:0000313|EMBL:OZG53656.1,
RC   ECO:0000313|Proteomes:UP000243657};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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: 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:OZG53656.1}.
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DR   EMBL; MWWT01000008; OZG53656.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261F410; -.
DR   Proteomes; UP000243657; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
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:UP000243657};
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          215..518
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        447
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         323..329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         348
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         394
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   518 AA;  55939 MW;  BFE04A9627AD3D4E CRC64;
     MSKAKTLAKR VRQGRMPQQA PNARSVAYSV LTKVQEQDSY ANLLLPHVLG GSELSTDDKR
     FVTDAVYGTL RWRGLLDAVI VSAHGRSLNS INKRLVNVLR LGAYQWLFMN GAEYAVVNES
     VKLAKKRAGQ QTTGFVNAVM RKIVARTLDQ WRETLSQESS YEDEAERLAV QYSHPAWIVR
     ELAAAWNAGG YAPEPSVKES GVNEELEGLE GLEAMLAADN EAPAVTLCVR PSLADMDAVY
     DEVEALGGRV QRGELSPYAL RVRGVNPQNL ASVTEGRVGV EDEGSQLAAL ALALAPVEDA
     DGVKGAEGTE DAAERGERWL DMCAGPGGKT ALLASIAQEV GATLSANEPH EHRRELVREN
     LKAIDAGTLG EISGRDGREF GATFPGAFDR VLVDAPCSGL GALRRRPEAR WRKTAESVQE
     LASLQKELLN SALDATRSGG VVAYVTCSPV LAETRDIVSA VLSARSDASR LDVPSVLEEL
     NSSIPLPASV DSASPRDMQL FENIHDTDQM FIALIRKI
//
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