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Database: UniProt
Entry: A0A2S8B3W8_9SPHN
LinkDB: A0A2S8B3W8_9SPHN
Original site: A0A2S8B3W8_9SPHN 
ID   A0A2S8B3W8_9SPHN        Unreviewed;       433 AA.
AC   A0A2S8B3W8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:PQM27043.1};
GN   ORFNames=CVO77_18965 {ECO:0000313|EMBL:PQM27043.1};
OS   Sphingopyxis lindanitolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=2054227 {ECO:0000313|EMBL:PQM27043.1, ECO:0000313|Proteomes:UP000238954};
RN   [1] {ECO:0000313|Proteomes:UP000238954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WS5A3p {ECO:0000313|Proteomes:UP000238954};
RA   Kaminski M.A.;
RT   "The complete genome sequence of Sphingopyxis pomeranensis sp. nov. strain
RT   WS5A3p.";
RL   Submitted (NOV-2017) 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}.
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:PQM27043.1}.
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DR   EMBL; PHFW01000003; PQM27043.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8B3W8; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000238954; 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}; Reference proteome {ECO:0000313|Proteomes:UP000238954};
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          154..430
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         247..253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         268
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   433 AA;  46096 MW;  FBE05DD7FFBDC3C3 CRC64;
     MADRRPRRGR GPAEADPPGT ASRRAALRLL DAVLRRGDPL DIAAHAATQG LPPADRAFAI
     AIASETLRWM GDIDALIDGA TSQVLADDVK SRTVLRLALA QLLILKTSPH AVVSTALPLV
     AGGPRRLVHA LLSRAQQEEW SLPESANLPE AVAERWADQW GDAIVAAAAA AWSGPPPIDL
     SFAAEPGDEE WADAAVLAPL HRRLPRGQAI EAMPGFREGG WWVQDLAASL PARLLGAGNG
     RRLLDLCAAP GGKTMQLAAA GWDVVAVDSS AKRLERLSDN LARTALSADV VQGDIRTWEP
     DASAEAVLLD APCSATGIFR RHPDVLHRIE PRQIDELAEL QGELLARAAQ WVTPGGTLLY
     ATCSLERAEG EDQVAAFLDW HRDWTIDPVT PEELPAGIIP DDSGFVRTLP GMLADAGGLD
     GFFIARLRAP SAA
//
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