(data stored in SCRATCH zone)

SWISSPROT: D3VHU1_XENNA

ID   D3VHU1_XENNA            Unreviewed;       437 AA.
AC   D3VHU1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|SAAS:SAAS01079081};
DE            EC=2.1.1.176 {ECO:0000256|HAMAP-Rule:MF_01856};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN   Name=rsmB {ECO:0000256|HAMAP-Rule:MF_01856,
GN   ECO:0000313|EMBL:CBJ88430.1};
GN   Synonyms=sun {ECO:0000256|HAMAP-Rule:MF_01856};
GN   OrderedLocusNames=XNC1_0348 {ECO:0000313|EMBL:CBJ88430.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88430.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88430.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01856,
CC       ECO:0000256|SAAS:SAAS01079038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219,
CC         Rhea:RHEA-COMP:10220, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         EC=2.1.1.176; Evidence={ECO:0000256|HAMAP-Rule:MF_01856,
CC         ECO:0000256|SAAS:SAAS01116325};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01856,
CC       ECO:0000256|SAAS:SAAS00029836}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|PROSITE-
CC       ProRule:PRU01023, ECO:0000256|SAAS:SAAS00546407}.
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DR   EMBL; FN667742; CBJ88430.1; -; Genomic_DNA.
DR   RefSeq; WP_013183232.1; NC_014228.1.
DR   STRING; 406817.XNC1_0348; -.
DR   EnsemblBacteria; CBJ88430; CBJ88430; XNC1_0348.
DR   KEGG; xne:XNC1_0348; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   HAMAP; MF_01856; 16SrRNA_methyltr_B; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR023541; rRNA_ssu_MeTfrase_B_ent.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHU1.
DR   SWISS-2DPAGE; D3VHU1.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00423093};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|PROSITE-ProRule:PRU01023, ECO:0000256|SAAS:SAAS00221280,
KW   ECO:0000313|EMBL:CBJ88430.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|PROSITE-
KW   ProRule:PRU01023, ECO:0000256|SAAS:SAAS01090267};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|SAAS:SAAS00149471};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01856,
KW   ECO:0000256|PROSITE-ProRule:PRU01023, ECO:0000256|SAAS:SAAS00500162};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01856, ECO:0000256|PROSITE-
KW   ProRule:PRU01023, ECO:0000256|SAAS:SAAS00221314,
KW   ECO:0000313|EMBL:CBJ88430.1}.
FT   DOMAIN      164    429       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   REGION      254    260       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856,
FT                                ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   COILED      276    296       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    375    375       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01856, ECO:0000256|PROSITE-ProRule:
FT                                PRU01023}.
FT   BINDING     277    277       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856,
FT                                ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     303    303       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856,
FT                                ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     322    322       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01856,
FT                                ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   437 AA;  49672 MW;  A9CFEDCEFD355C22 CRC64;
     MKNTYNLRSI AAKAITQVLE QGQSLSSVIP ELQQRVSDKD KALLQELCFG VMRVLPQLEW
     FMSQLMAKPL KGKQRIFHYL IMVGLYQLTY TRIPAHAALA ETVNGAINLK RPQLKGLING
     VLRQFQRQQQ ELVERSNKHI NQHLHPKWLQ ERIQKSYPQN WQTIIDANNQ KPPMWLRVNQ
     LHHTANEYLS LLENANIEAE LDTKHPNAIR LLNPCPVHSL PGFNQGWVTI QDRSAQGCAE
     LLTPCNGEFI LDLCAAPGGK TTHILEIAPK SKVLAIDIDE QRLKRVKENL QRLNLHAVVK
     TGDGRLPHEW AAGEQFDRIL LDAPCSATGV IRRHPDIKWL RRNEDIDQLV TLQSEILDAI
     WPYLKKNGTL VYATCSILPQ ENSEQIKAFL KRHTDAVLSE TGSLEKPGTQ IIPEVEGGDG
     FFYARLIKPI ISLSRSR
//

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