(data stored in ACNUC7421 zone)

SWISSPROT: Q3IDH1_PSEHT

ID   Q3IDH1_PSEHT            Unreviewed;       431 AA.
AC   Q3IDH1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 84.
DE   SubName: Full=16S rRNA m5C967 methyltransferase, S-adenosyl-L-methionine-dependent {ECO:0000313|EMBL:CAI85135.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:CAI85135.1};
GN   Name=rsmB {ECO:0000313|EMBL:CAI85135.1};
GN   OrderedLocusNames=PSHAa0021 {ECO:0000313|EMBL:CAI85135.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85135.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85135.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|SAAS:SAAS00672432}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC       rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC       rRNA. {ECO:0000256|SAAS:SAAS00672435}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00633808}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023,
CC       ECO:0000256|SAAS:SAAS00637407}.
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DR   EMBL; CR954246; CAI85135.1; -; Genomic_DNA.
DR   RefSeq; WP_011326753.1; NC_007481.1.
DR   ProteinModelPortal; Q3IDH1; -.
DR   STRING; 326442.PSHAa0021; -.
DR   EnsemblBacteria; CAI85135; CAI85135; PSHAa0021.
DR   KEGG; pha:PSHAa0021; -.
DR   PATRIC; fig|326442.8.peg.23; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   OrthoDB; POG091H02E2; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
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; Q3IDH1.
DR   SWISS-2DPAGE; Q3IDH1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637415, ECO:0000313|EMBL:CAI85135.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637422};
KW   rRNA processing {ECO:0000256|SAAS:SAAS00633795};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637399};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637429, ECO:0000313|EMBL:CAI85135.1}.
FT   DOMAIN      165    430       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    375    375       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     277    277       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     303    303       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     322    322       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   431 AA;  48293 MW;  8AB62F69475C069D CRC64;
     MSNVPNVRAL AAETLYNVVD KGASLNQELP FASQGLPPKD KALLQQICYG VLRYLPSLEN
     YCQHLVEEPL KGKRRIFQFL LYVGIYQLQH MRVPPHAAIS ETVNALQQLR ALGLKGLINA
     ILRSFQRQQL ELEEKAKLIP VCLYNHPNWF IKQVKEAYPD SWEDLLAENQ QQAPMWLRVN
     QAQYSTQEYS DMLTANDIEH TLNPDFIDGI KLAKPRDVFS LPEFDTGACS VQDAAAQLAA
     RFLEPKDDDT ILDACAAPGG KTCHILELAD AEVLALDSDA TRLERVKQNL TRIGLGADLQ
     CGDASQPHTW WDEKQFDRIL LDVPCSATGV IRRHPDIKWL RRASDIADLA ALQGDILDSI
     WPLLKPGGTL VYATCSVLPQ ENQQQVAKFL ANNNDVEHIP LHDKDTPTTP GLQLLPGESD
     GFYYAKLVKK I
//

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