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Database: UniProt
Entry: A0A0N0XLH2_9NEIS
LinkDB: A0A0N0XLH2_9NEIS
Original site: A0A0N0XLH2_9NEIS 
ID   A0A0N0XLH2_9NEIS        Unreviewed;       454 AA.
AC   A0A0N0XLH2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:KPC54060.1};
DE            EC=2.1.1.176 {ECO:0000313|EMBL:KPC54060.1};
GN   Name=rsmB_1 {ECO:0000313|EMBL:KPC54060.1};
GN   ORFNames=WG78_05405 {ECO:0000313|EMBL:KPC54060.1};
OS   Amantichitinum ursilacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chitinibacteraceae; Amantichitinum.
OX   NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC54060.1, ECO:0000313|Proteomes:UP000037939};
RN   [1] {ECO:0000313|EMBL:KPC54060.1, ECO:0000313|Proteomes:UP000037939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGB-41 {ECO:0000313|EMBL:KPC54060.1,
RC   ECO:0000313|Proteomes:UP000037939};
RA   Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT   "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT   chitin-degrading bacterium.";
RL   Submitted (JUL-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|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:KPC54060.1}.
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DR   EMBL; LAQT01000003; KPC54060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0XLH2; -.
DR   STRING; 857265.WG78_05405; -.
DR   PATRIC; fig|857265.3.peg.1106; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000037939; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
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:UP000037939};
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          142..420
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          424..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         256
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   454 AA;  49500 MW;  DE502A3F2FC474F0 CRC64;
     MILTPIQYDA VLEALDQILP FSAPADVCMS RMFRENKRLG ARDRTAIAET VFALLRNLPK
     LKWVAGDDAG GRLWLLALHS AVEKRNMKEL ATTYRENQLD IAQKWKALDW NTAPLAVRAN
     LTEWIVEALQ AEGRSEEEIL AVGNSLAHNA ALDIRANILK TKRDTLLEQL KAEEFPAEAT
     PYSPWGIRLV GKPNLARHPL FLAGNFEVQD EGSQLLAILT GVKRGQMVTD FCAGAGGKTL
     AIGAVMQSTG RLYAFDISEK RLANLKPRLA RSGLSNVQPQ LIASEHDQKI KRLAGKMDAV
     LVDAPCSGLG TLRRNPDLKY RQSPKSVNEL NQLQQSILAS ASRLVKAGGR LVYATCSILD
     RENKEVVDAF LATHPDFERI DVRDLLAKEK IELALTGTDL QLTPMQHGTD GFYAAVLQRK
     AAGAKPAPAD AAEEGETVAD AVPATEADAG ADAE
//
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