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Database: UniProt
Entry: M2YD06_9MICC
LinkDB: M2YD06_9MICC
Original site: M2YD06_9MICC 
ID   M2YD06_9MICC            Unreviewed;       495 AA.
AC   M2YD06;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:EME36504.1};
GN   ORFNames=C884_00491 {ECO:0000313|EMBL:EME36504.1};
OS   Kocuria palustris PEL.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME36504.1, ECO:0000313|Proteomes:UP000009877};
RN   [1] {ECO:0000313|EMBL:EME36504.1, ECO:0000313|Proteomes:UP000009877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEL {ECO:0000313|EMBL:EME36504.1,
RC   ECO:0000313|Proteomes:UP000009877};
RX   PubMed=24504000;
RA   Sharma G., Khatri I., Subramanian S.;
RT   "Draft Genome Sequence of Kocuria palustris PEL.";
RL   Genome Announc. 2:e01261-13(2014).
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:EME36504.1}.
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DR   EMBL; ANHZ02000014; EME36504.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2YD06; -.
DR   STRING; 71999.KPaMU14_06850; -.
DR   Proteomes; UP000009877; 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:UP000009877};
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          180..494
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        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         281..287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         359
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   495 AA;  53084 MW;  B1FDBA647BE2215D CRC64;
     MDQRSYSASA PSHRSRQADP ARLAAYRTLR EVSENDAYGN LVLPQQIREQ RLDRRDAGFA
     TELAYGALRH QGTWDAILQR CVDRPLEQLD APVVDVLRLG VHQLLAMRVP DHAAIDQTVG
     LTRAEIGAGP SGLVNAVLRK VAAAPLEQWI AELNEGSTAW QRLATAHAHP EWIVRAMSQA
     LSAHGRSPEE IEALLEADNE PPSVQLVALP GLGHIQEELD DGAEPGPLTP DSAISGGGDL
     HRRAGVRTGG IRVQDSGSQL VARTLVAARP VEEGEHWLDL CAGPGGKAAL LAALAQQNGA
     TLLANEVSEH RARLVDDALA VLPEEAWQIR WGDGRDIASV LEQPDHYVAA EGFDRILVDA
     PCTGLGALRR RPEARWRRRP SDLADLTQLQ AQLLPAAAEA LRPGGLLLYA TCSPHAAETV
     VAVDDLLRAR PDLRLIDAAE PARAAALPGA LEGEADPSNP HPAGESVADG ARTVQLWPHV
     HGTDAMFMAL FTKTS
//
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