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Database: UniProt
Entry: A0L1C8
LinkDB: A0L1C8
Original site: A0L1C8 
ID   RIMO_SHESA              Reviewed;         480 AA.
AC   A0L1C8;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   14-MAY-2014, entry version 59.
DE   RecName: Full=Ribosomal protein S12 methylthiotransferase RimO;
DE            Short=S12 MTTase;
DE            Short=S12 methylthiotransferase;
DE            EC=2.-.-.-;
DE   AltName: Full=Ribosome maturation factor RimO;
GN   Name=rimO; OrderedLocusNames=Shewana3_3627;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid
CC       residue of ribosomal protein S12 (By similarity).
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 MTTase N-terminal domain.
CC   -!- SIMILARITY: Contains 1 TRAM domain.
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DR   EMBL; CP000469; ABK49847.1; -; Genomic_DNA.
DR   RefSeq; YP_871253.1; NC_008577.1.
DR   ProteinModelPortal; A0L1C8; -.
DR   STRING; 94122.Shewana3_3627; -.
DR   EnsemblBacteria; ABK49847; ABK49847; Shewana3_3627.
DR   GeneID; 4476226; -.
DR   KEGG; shn:Shewana3_3627; -.
DR   PATRIC; 23575266; VBISheSp134792_3998.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224766; -.
DR   KO; K14441; -.
DR   OMA; PHDPFID; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; SSP94122:GJ9K-3740-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01865; MTTase_RimO; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR023970; MeThioTfrase/rSAM.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR005840; Ribosomal_S12_MeSTrfase_RimO.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR11918; PTHR11918; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00089; TIGR00089; 1.
DR   TIGRFAMs; TIGR01125; TIGR01125; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS50926; TRAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    480       Ribosomal protein S12
FT                                methylthiotransferase RimO.
FT                                /FTId=PRO_0000375005.
FT   DOMAIN       37    147       MTTase N-terminal.
FT   DOMAIN      405    471       TRAM.
FT   METAL        46     46       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        82     82       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       111    111       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       179    179       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       183    183       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       186    186       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   480 AA;  53567 MW;  F189346A0B984BCF CRC64;
     MTVETFNPKQ TTTLETPAKT LEAASADLAN AESATGNRIG FVSLGCPKNL VDSERILTQL
     RIDGYEVTNS YDNADLVIVN TCGFIDAAVE ESLDAVREAL EENGKVIVTG CLGAKENQIR
     EVHPDVLEIT GPHSYEAVLK HVHKYVPKPE HNPFTSLIPQ TGVKLTPKHY AYLKISEGCD
     NRCTFCIIPA LRGDLDSRPA GSVLDEAKRL VESGVQEILV VSQDTSAYGK DKGGRTDFWN
     GMPVKQDITS LARQLGKMGA WVRLHYIYPY PWVDDLIPLM AEGLILPYLD IPMQHASPRI
     LKMMKRPGRV DRQLEAIQRW REICPDLVIR STFIVGFPGE TEEDFEMLLD FLREARLDRV
     GCFKYSEVEG AVANTIAELI SEDVKEDRYH RFMEVQAEIS AERLARFVGR TMDILIDDVD
     EEGAIGRSFA DAPEIDGMVF INGETELEPG MLVRAVITHS DEHDLWAELV DADAEDDIEA
//
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