GenomeNet

Database: UniProt
Entry: D6YTR0_WADCW
LinkDB: D6YTR0_WADCW
Original site: D6YTR0_WADCW 
ID   D6YTR0_WADCW            Unreviewed;       421 AA.
AC   D6YTR0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:ADI37521.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ADI37521.1};
GN   Name=rsmB1 {ECO:0000313|EMBL:ADI37521.1};
GN   OrderedLocusNames=wcw_0146 {ECO:0000313|EMBL:ADI37521.1};
OS   Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX   NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37521.1, ECO:0000313|Proteomes:UP000001505};
RN   [1] {ECO:0000313|EMBL:ADI37521.1, ECO:0000313|Proteomes:UP000001505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX   PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA   Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA   Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT   "The Waddlia genome: a window into chlamydial biology.";
RL   PLoS ONE 5:E10890-E10890(2010).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001928; ADI37521.1; -; Genomic_DNA.
DR   RefSeq; WP_013181249.1; NZ_LVEB01000005.1.
DR   AlphaFoldDB; D6YTR0; -.
DR   STRING; 716544.wcw_0146; -.
DR   KEGG; wch:wcw_0146; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_1_0; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000001505; 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:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 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:UP000001505};
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          158..421
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        374
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   421 AA;  47249 MW;  3B3290C1959FBEBE CRC64;
     MDITKTKNPR EAAYLALLSS AREESFLIDS LAQWQAKCRP SIQDYHLARE VAYGTTRMAL
     ALDHLALQLA DKKKLALKLR EKILFRMGLY QFHYMDKIPL YAIVDETIKI AKIHCHESFV
     KFLNACLRKV EEIDPQLPKG ETVPELSIRY SYPAYYVQEL VQNFGLEKAE EIMEAGNRPS
     QTMFRVRPQA SRPKEANGEI DFLAGTRCGM GVIRDPSLIS NISSSSDYYI QNATPAELMS
     SLAQDFGAPK NILDLCSSPG GKLILAHDLY PDAELSANDV SSGKLKPLSE NCAKYGISTT
     LSSVRGEEFP LAQKFDLVIL DVPCSNTGVL NKRPEARWRL SQKTLEQLEE IQLQLLRRGI
     ELLDKGGELW YLTCSVLKRE NGRLIDKVCQ ELSLETRLKE AILPNADGWD GGFGCALRKI
     G
//
DBGET integrated database retrieval system