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Database: UniProt
Entry: A8LE23_FRASN
LinkDB: A8LE23_FRASN
Original site: A8LE23_FRASN 
ID   A8LE23_FRASN            Unreviewed;       495 AA.
AC   A8LE23;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ABW11158.1};
GN   ORFNames=Franean1_1720 {ECO:0000313|EMBL:ABW11158.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW11158.1};
RN   [1] {ECO:0000313|EMBL:ABW11158.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW11158.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA   Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT   "Complete sequence of Frankia sp. EAN1pec.";
RL   Submitted (AUG-2007) 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}.
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DR   EMBL; CP000820; ABW11158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8LE23; -.
DR   STRING; 298653.Franean1_1720; -.
DR   KEGG; fre:Franean1_1720; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_3_11; -.
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; 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; 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          191..493
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         285..291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         327
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         352
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         369
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   495 AA;  50939 MW;  EC6A201811363E0D CRC64;
     MSVSAPRRGG TTDPARLLAW EVLRAVDERG AYANLLLPAL LSGRRLSPRD RGFATELTYG
     SLRAQGTLDG VLDTVTSRPV ASVDPPVRDA LRLGAYQLLS TRVPPRAAVA STVDLVRATC
     GERPVRFANA VLRRVAARIE AAAGDIAVLL SAPDIAEDPA GHLAVVTAHP RWIVDVVLDA
     LGGDVAGAHA ALAANDTRPA VHLVARPGRI DAEALVAQAA SVGLGARRGA GSPYAVHLDG
     GDPGSLPAVA AGDASVQDEG SQLVTLALAS VPTIGRDTGL TVDLCAGPGG KAALLAALQA
     VGEPAETMRE PAAGGHRPPP ARLLALEPRA ARAGLVAASL AGFPAALAVR ADGRFPPVRP
     GMADRVLVDV PCSGLGALRR RPEARWRRTP ADVAALVPLQ RQLLVAALDL VRPGGAVAYV
     TCSPHPEETS EVVTAIAQQR GDVAILDARR CPPFAGPLFG DGAPGGLGDG PFVQLWPHLH
     GTDAMFLALL RRADR
//
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