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Database: UniProt
Entry: A0A5S3P2P1_9SPHN
LinkDB: A0A5S3P2P1_9SPHN
Original site: A0A5S3P2P1_9SPHN 
ID   A0A5S3P2P1_9SPHN        Unreviewed;       412 AA.
AC   A0A5S3P2P1;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=RsmB/NOP family class I SAM-dependent RNA methyltransferase {ECO:0000313|EMBL:TMM47131.1};
GN   ORFNames=FEV51_10070 {ECO:0000313|EMBL:TMM47131.1};
OS   Qipengyuania marisflavi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Qipengyuania.
OX   NCBI_TaxID=2486356 {ECO:0000313|EMBL:TMM47131.1, ECO:0000313|Proteomes:UP000309668};
RN   [1] {ECO:0000313|EMBL:TMM47131.1, ECO:0000313|Proteomes:UP000309668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KEM-5 {ECO:0000313|EMBL:TMM47131.1,
RC   ECO:0000313|Proteomes:UP000309668};
RA   Yoon J.-H.;
RT   "Erythrobacter marisflavi sp. nov., isolated from isolated from water of an
RT   estuary environment.";
RL   Submitted (MAY-2019) 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:TMM47131.1}.
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DR   EMBL; VCAO01000005; TMM47131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5S3P2P1; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000309668; 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:UP000309668};
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          130..411
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        349
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         233..239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   412 AA;  44482 MW;  E90BE450583E8EB1 CRC64;
     MAQPPGIHAR RAALRILDAV MRRGDTLDTA FGAATKDVRK FEDKALTRAI ASEVLRWLTD
     LDTLIDSATK TNLPPDAKPR MVLRMMLAQW LRLDTPPHAV LATGLPLLAG GPRRLAHGVF
     STLAKREVTL PDAPTLPAEV SERWGERAAA IAAGLAHPPP LDLELRDSAE TVQWANQLAG
     DSLMPGHIRL PRGSAIEKLP GFADGAWWVQ DLAASLPARL LGPGEARHAL DLCAAPGGKT
     LQLAAAGWNV TALDISKRRL ELLRDNLKRT DLKAGIVRAD ALGWEPKHQF DAILLDAPCT
     ATGTARRHPD VLHRIGPRQI AEMAELQTAL LERAQSWLKP GGVLIYAVCS LEPEEGEQQA
     QRVTLGPLPI TADELPAGLS PTAEGWLRTD PGMLTEQGGL DGFFIARWRA PG
//
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