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Database: UniProt
Entry: A0A0B5D853_9CORY
LinkDB: A0A0B5D853_9CORY
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ID   A0A0B5D853_9CORY        Unreviewed;       487 AA.
AC   A0A0B5D853;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=B842_07115 {ECO:0000313|EMBL:AJE33272.1};
OS   Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33272.1, ECO:0000313|Proteomes:UP000031524};
RN   [1] {ECO:0000313|EMBL:AJE33272.1, ECO:0000313|Proteomes:UP000031524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT   isolated from a wastewater-fed microbial fuel cell.";
RL   Submitted (APR-2013) 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; CP005286; AJE33272.1; -; Genomic_DNA.
DR   RefSeq; WP_040085920.1; NZ_CP005286.1.
DR   AlphaFoldDB; A0A0B5D853; -.
DR   STRING; 1223515.B842_07115; -.
DR   KEGG; chm:B842_07115; -.
DR   HOGENOM; CLU_005316_0_3_11; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000031524; Chromosome.
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   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; 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          205..487
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         308..314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         373
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   487 AA;  53001 MW;  9B8C6122A32DD9AF CRC64;
     MSGGFRSRAK SSGQEPKRQA PKQTPKQAPR QARPQQSRKR PERRNTAGVD KPRLLAFDVL
     TRVREDDAYA NLILPRMLRE RRIVDRDAAF TTEITYGTLR TLGVLDAVIA ECSSRGLDQI
     APEVLDALRL GTYQLLYTRV EPHAAVDTTV RLVEAAGHEK AKGFANGIMR TISRTRPEKW
     IERLTPPGEI AAAAFRNAHP EWIAQSFSRV LGLGDLDAAL GADSQRPTVH LVARPGEISA
     EELALMTGGE EGEYSPYAVH LSSGDPGDLE PVREGLAAVQ DEGSQLIARA VVEAPLEGED
     RGRWLDLCAG PGGKAALMGA LARIDAAHVD AVEVSPHRAK LVEQTTRGLP VKVHVADGRD
     PGLEPGYDRV LVDAPCSGLG ALRRRPEARW RKAESDIDGL APLQYELLAS ALNLVRPGGV
     VIYSTCSPDL RETRAIVDRA VAELGAVELD AHELVAPMQD VGTHRSVQMW PHRHGTDAMF
     FAVLRRG
//
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