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Database: UniProt
Entry: A0A0G9MVG0_9SPHN
LinkDB: A0A0G9MVG0_9SPHN
Original site: A0A0G9MVG0_9SPHN 
ID   A0A0G9MVG0_9SPHN        Unreviewed;       412 AA.
AC   A0A0G9MVG0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SAM-dependent methlyltransferase {ECO:0000313|EMBL:KLE34594.1};
GN   ORFNames=AAW00_10370 {ECO:0000313|EMBL:KLE34594.1};
OS   Aurantiacibacter luteus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=1581420 {ECO:0000313|EMBL:KLE34594.1, ECO:0000313|Proteomes:UP000053464};
RN   [1] {ECO:0000313|EMBL:KLE34594.1, ECO:0000313|Proteomes:UP000053464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA37 {ECO:0000313|EMBL:KLE34594.1,
RC   ECO:0000313|Proteomes:UP000053464};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter luteus KA37.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KLE34594.1}.
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DR   EMBL; LBHB01000002; KLE34594.1; -; Genomic_DNA.
DR   RefSeq; WP_047004241.1; NZ_LBHB01000002.1.
DR   AlphaFoldDB; A0A0G9MVG0; -.
DR   STRING; 1581420.AAW00_10370; -.
DR   PATRIC; fig|1581420.6.peg.2126; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000053464; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; 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:UP000053464};
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          133..410
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        348
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         232..238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         295
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   412 AA;  43675 MW;  CB7A03762E7415F0 CRC64;
     MPQIPGLPPR RAALKMLDAV LRRGETMEQA GGAANGLPSF SDRALARAVA GEVLRWLVDL
     DALIDSATRE VLPSDAKARM VLRMMLAQWL RLETPPHAVV ATALPLLDGG PKRLAHGVFA
     TLTRKEASLP HSPTLPAEVA ARWGERAEAI ATGLAVPPPL DLTLRDPSQT ATVAEQLGGT
     SLAPGHVRLP RGTAVETLPG FDDGAWWVQD LAASIPARLL GAGEGRRVLD LCAAPGGKTL
     QLASMGWQVT ALDNSSRRLE RLRQNLERTG LAAAIVEADA MGWHPDEQFD AILLDAPCTA
     TGTCRRNPDV IHRIGPRQIE AATTLQTQLL ERAANWLAPG GTLVYAVCSL EREEGEGVAA
     TCDLLPAPVT ADELPAGIQP TAEGQVRTDP GMLAEEGGLD GFFVARFRAS QA
//
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