ID G7V9M8_THELD Unreviewed; 440 AA.
AC G7V9M8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:AER66578.1};
GN OrderedLocusNames=Tlie_0845 {ECO:0000313|EMBL:AER66578.1};
OS Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314).
OC Bacteria; Synergistota; Synergistia; Synergistales; Thermovirgaceae;
OC Thermovirga.
OX NCBI_TaxID=580340 {ECO:0000313|EMBL:AER66578.1, ECO:0000313|Proteomes:UP000005868};
RN [1] {ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Saunders E.,
RA Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.-M.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Thermovirga lienii DSM 17291.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AER66578.1, ECO:0000313|Proteomes:UP000005868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC {ECO:0000313|Proteomes:UP000005868};
RX PubMed=22768366; DOI=10.4056/sigs.2726028;
RA Goker M., Saunders E., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Genome sequence of the moderately thermophilic, amino-acid-degrading and
RT sulfur-reducing bacterium Thermovirga lienii type strain (Cas60314(T)).";
RL Stand. Genomic Sci. 6:230-239(2012).
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; CP003096; AER66578.1; -; Genomic_DNA.
DR RefSeq; WP_014162997.1; NC_016148.1.
DR AlphaFoldDB; G7V9M8; -.
DR STRING; 580340.Tlie_0845; -.
DR KEGG; tli:Tlie_0845; -.
DR eggNOG; COG0144; Bacteria.
DR HOGENOM; CLU_005316_0_3_0; -.
DR OMA; RVNRQHH; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000005868; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
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; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22807:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005868};
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 167..439
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 378
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 309
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 440 AA; 49331 MW; D2007A641280AC79 CRC64;
MRGIEVALEV WRDVNEGLFA SEALRKKSLG LPEGDRVLAS TLVYVSIRRA SFWKYLVKEY
SGRSLREFSP AAGDALVLGV AGIAELRRFH PASLVNALVE FVKKKGSRRE VSVVNAVLRR
AAREAKKDLE RFLHSPQLKD LCLVCGVPYW VGTSLSDSWG RKEARQLLKL MTMRSYVSLR
LSPGVDKREV ISNLEGSGYR AWESSLLDYS IRLASSAFPP NLYGYDKGWI TPQTESSMMV
AEVVSSNYEG GAILDMCCGR GVKTAQIAQV LTGAPIEAWE LSQGRLKAAE REMERLRIKR
DSIIFKRGDA LELNPNEKPS LIFLDAPCSG SGTWARHPDG KLRQSKEKLQ HLTDLQRAML
LRALEMVKPG GKVVYSTCSL LRPENELVVG EVVGKVPDVV EIPVSWPYDY VRRGRPWGYY
VWPALPWVDG FYVAVLKKRP
//