ID B8J4T9_DESDA Unreviewed; 462 AA.
AC B8J4T9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ACL50219.1};
GN OrderedLocusNames=Ddes_2325 {ECO:0000313|EMBL:ACL50219.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL50219.1};
RN [1] {ECO:0000313|EMBL:ACL50219.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL50219.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) 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}.
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DR EMBL; CP001358; ACL50219.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J4T9; -.
DR STRING; 525146.Ddes_2325; -.
DR KEGG; dds:Ddes_2325; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_642097_0_0_7; -.
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 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; IPR023267; RCMT.
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 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};
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..275
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 276..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 462 AA; 49878 MW; 22C0234EE7BC99CB CRC64;
MPPMQKTAAR SFRIVCKNTH TASVEALLRA QGYEFEAEPF SPLCRRLVAE PRPLGSSLAA
FFGYIYIQDR SSMLPPLALA PAAGSAVLDM CASPGSKTGF LAQLVGRTGF VLGNEPSPSR
LATLRANLHQ CGFIHTGTCS YSGDALPLRP GSWKNILLDP PCSGWGTVEK NPQVLKLWQG
DKLDSLTSLQ RRLLRHAERL LAPGGHVVFS TCTTNVAENE DQVRFAEEHL GLVREHINPF
PGFVWEELPG GEGTLRVDGA RSQAQGFYVA LLRKPENASS HHREPKAEQA THFGPARGSD
GETAGAFLNG GRARSKNGSR PDARTGSRVP AGTPLPRSCL HGPTCDPDML PPGQAMLYGE
HVRFIPEQAA ALLPPDCAWQ GALLGKFNGG KLDAAPRLRA LMTPQPDREK SLVLEDISDI
SALLSGQSRQ TGLQGREAAL WWRDLPLGRV GLKQGRALTG FK
//
