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Database: UniProt
Entry: B1VDP1_CORU7
LinkDB: B1VDP1_CORU7
Original site: B1VDP1_CORU7 
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
//
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