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Database: UniProt/TrEMBL
Entry: D3SDG2_THISK
LinkDB: D3SDG2_THISK
Original site: D3SDG2_THISK 
ID   D3SDG2_THISK            Unreviewed;       451 AA.
AC   D3SDG2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   SubName: Full=Sun protein {ECO:0000313|EMBL:ADC72761.1};
GN   OrderedLocusNames=TK90_2271 {ECO:0000313|EMBL:ADC72761.1};
OS   Thioalkalivibrio sp. (strain K90mix).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396595 {ECO:0000313|EMBL:ADC72761.1, ECO:0000313|Proteomes:UP000009099};
RN   [1] {ECO:0000313|Proteomes:UP000009099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K90mix {ECO:0000313|Proteomes:UP000009099};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Foster B., Sun H., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Sorokin D.Y., Muyzer G., Woyke T.;
RT   "Complete sequence of chromosome of Thioalkalivibrio sp. K90mix.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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:SAAS00629182}.
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; CP001905; ADC72761.1; -; Genomic_DNA.
DR   RefSeq; WP_012983633.1; NC_013889.1.
DR   ProteinModelPortal; D3SDG2; -.
DR   STRING; 396595.TK90_2271; -.
DR   EnsemblBacteria; ADC72761; ADC72761; TK90_2271.
DR   KEGG; tkm:TK90_2271; -.
DR   eggNOG; ENOG4105CYJ; Bacteria.
DR   eggNOG; COG0144; LUCA.
DR   HOGENOM; HOG000037300; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   OrthoDB; POG091H02E2; -.
DR   BioCyc; TSP396595:GH8D-2295-MONOMER; -.
DR   Proteomes; UP000009099; Chromosome.
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; IPR031341; Methyltr_RsmF_N.
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; PF17125; Methyltr_RsmF_N; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009099};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00629174};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637415};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009099};
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}.
FT   DOMAIN      177    451       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    389    389       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     291    291       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     317    317       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     336    336       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   451 AA;  48693 MW;  C541497347E3BB32 CRC64;
     MAGKRAGRIV PSRVDSRSPR QRALEAAEGV VLQGHSLTRA VEHATEGLNA RDAAWVQALA
     YTTLRWYPQL SALVNGFLER PLRKKDAVIG VLLAQGLAEL MHFSTRDHAA VRETAELARA
     IHRPGAVGLI NAVLRRAQRE QDALEAAVRE DPALRFAVPE WLLETIRASW PDDWETLLEA
     ATRPAPMTLR VNLSRTSREE ALQALVAAGH PAQAHPQLEA ALTLDEPADV AQLPGFAEGR
     LSVQDASAQW AAVLLDPQPG ERVLDACAAP GGKTGHLLER AGGDLQLTAL DSDAERLVQV
     RENLDRLGFA AQLTAADVAD PDAWWDGRPF DAILLDVPCS ATGVIRRHPD IKTLRRADDI
     PRLAAEQARI LEAAWGLLRP GGRLLYATCS LLSEENDAVV AGFLERMPDA RALEPEGGPP
     IAGAHARSVG WALPLGLEGG DGFYYALLTK D
//
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