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Database: UniProt
Entry: A0A1M7TJV9_9RHOB
LinkDB: A0A1M7TJV9_9RHOB
Original site: A0A1M7TJV9_9RHOB 
ID   A0A1M7TJV9_9RHOB        Unreviewed;       500 AA.
AC   A0A1M7TJV9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SHN71001.1};
GN   ORFNames=SAMN05216200_10770 {ECO:0000313|EMBL:SHN71001.1};
OS   Oceanicella actignis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Oceanicella.
OX   NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN71001.1, ECO:0000313|Proteomes:UP000184066};
RN   [1] {ECO:0000313|EMBL:SHN71001.1, ECO:0000313|Proteomes:UP000184066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN71001.1,
RC   ECO:0000313|Proteomes:UP000184066};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; FRDL01000007; SHN71001.1; -; Genomic_DNA.
DR   RefSeq; WP_072747699.1; NZ_FRDL01000007.1.
DR   AlphaFoldDB; A0A1M7TJV9; -.
DR   STRING; 1189325.SAMN04488119_10771; -.
DR   Proteomes; UP000184066; 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:UP000184066};
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          199..499
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         297..303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         360
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   500 AA;  52305 MW;  B0BD868EA05B5FA8 CRC64;
     MSDSSAPRTP GRRRRATARP AAKAGAGARG AKARSAPGSD PGSAPESGPD SASAVGAGQG
     ARREALRLIL GVVEQRRMLS ELIERAPADL PPEERARAGA LAAATLRRMG QADALIRRFA
     RRRPPPQALA ALRLAAVELH ALGAPAHAAV DGAVAALRAM RGAERFAGLV NAVARRMAAE
     GGPIWASLDA ARTNTPGWLW GRLSSAYGAG AARRMAEAHL RAAPLDLTPR DGARAEALAR
     ALDARLLPCG TLRLARRAQI SALPGFAEGE WWVQDAAAAL PARILAPQAG ERVLDMCAAP
     GGKTMQMAAA GAKVTALDAS AARLERLAQN LARTGLSARV VAADALEWTP DAPFDAILLD
     APCSATGTIR RHPDLPRLLP EGPDLPALTA MQDALLDRAW GWLRPGGRLV FATCSLLPEE
     GERRAAAFRA RTPDAAPLEW SPRALGGPDF WRDAAGDLRV RPDWSPEAGP DADPRADPDR
     APGEHGGMDG FFAAGFVKRA
//
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