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Database: UniProt
Entry: A0A074JMN6_9RHOB
LinkDB: A0A074JMN6_9RHOB
Original site: A0A074JMN6_9RHOB 
ID   A0A074JMN6_9RHOB        Unreviewed;       423 AA.
AC   A0A074JMN6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=DT23_15990 {ECO:0000313|EMBL:KEO58911.1};
OS   Thioclava indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO58911.1, ECO:0000313|Proteomes:UP000027471};
RN   [1] {ECO:0000313|EMBL:KEO58911.1, ECO:0000313|Proteomes:UP000027471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DT23-4 {ECO:0000313|EMBL:KEO58911.1,
RC   ECO:0000313|Proteomes:UP000027471};
RX   PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA   Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT   "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT   Ocean.";
RL   Antonie Van Leeuwenhoek 107:297-304(2015).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEO58911.1}.
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DR   EMBL; AUNB01000031; KEO58911.1; -; Genomic_DNA.
DR   RefSeq; WP_038131245.1; NZ_AUNB01000031.1.
DR   AlphaFoldDB; A0A074JMN6; -.
DR   STRING; 1353528.DT23_15990; -.
DR   eggNOG; COG0144; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000027471; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000027471};
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          132..422
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         240..246
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         261
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   423 AA;  45173 MW;  DD9DAB653EC88246 CRC64;
     MARPDPARFA ALGLIIGVTE DHESLSEQIS QDALDGLEPP QRARAQRLAT TTLRHLARAD
     GVLKPHLRRK PSADIMALLR LATVELLEEN QAPHGVVDAA VTLAKSAGPK TSSFSGLVNA
     VLRKVSVETE AWAKQRAPEM PGWLRGRVMA AYGKRAAQTM EAAHLAGAPL DLSVKSEASK
     WAETLGAELL PTGSLRLPAQ GKITDLPGFE TGDWWVQDAA AALPAKLLAP TPGARVLDLC
     AAPGGKTLQL AATGAQVTAL DISGPRLERL VENLERTGLE AEIIAADALN WQPDAPYDAI
     LLDAPCSATG TIRRHPDLPY VKNGASIKPL FALQADLLDR ALGWLKPGGS LVYATCSLLP
     EEGEAQIKAA LERHADLIVT PPDLPGIEPD WITPEGGLRL RPDFWADRGG MDGFYMARLQ
     RLA
//
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