ID B1VDP1_CORU7 Unreviewed; 513 AA.
AC B1VDP1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Putative tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:CAQ04939.1};
GN OrderedLocusNames=cu0979 {ECO:0000313|EMBL:CAQ04939.1};
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ04939.1, ECO:0000313|Proteomes:UP000001727};
RN [1] {ECO:0000313|EMBL:CAQ04939.1, ECO:0000313|Proteomes:UP000001727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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}.
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DR EMBL; AM942444; CAQ04939.1; -; Genomic_DNA.
DR RefSeq; WP_012360227.1; NC_010545.1.
DR AlphaFoldDB; B1VDP1; -.
DR STRING; 504474.cu0979; -.
DR GeneID; 60603758; -.
DR KEGG; cur:cu0979; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR HOGENOM; CLU_005316_0_3_11; -.
DR OMA; RVNRQHH; -.
DR Proteomes; UP000001727; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; 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:UP000001727};
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 219..513
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 447
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 322..328
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 371
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 513 AA; 54678 MW; 015E13E8E1B40B91 CRC64;
MSSFRSRSES ARSGKARPNT ASRGTGRAKQ RESGRARGYQ QRRPEHRQEK SRRAGTGDKA
RDAAFAVLRQ VTEEDAYGNL ALPAVLRERG ISGRDANFAT ELTYGTLRAT GLLDAIIAKA
AGRPVAKIDS VALDALRIGA YQLLRTRVEP HAAVDTSVEL VKANGGGKAS GFVNGVLRTI
SRSTPEQWLD RVAPGSDLAN MALRYAHPEW IAAAFNQSLG GSSEKPAADL AEALEADDAR
PTVHLAARPG QISAEELALI TGGEQGRWSD YAVYLDSGAP GELEAITQGL ASVQDEGSQL
ISLALVQAPL GREDRGRWLD LCAGPGGKTA FIGSWAQAEQ ATVDATEISA HRAELVAKST
KELPVRVRTG DGRNLAGVRD LELPEEGFDR VLVDAPCTGL GALRRRPEAR WRKQETDVTE
LVPLQRELLR SAWEATAPGG VVIYSTCSPH PLETTQLVDS FCRDTGAEPI DLGAEVPALA
AAAAAGGAVG PYIQLWPHRH GTDAMFIAGI RKA
//