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Database: UniProt
Entry: Q3MFH1
LinkDB: Q3MFH1
Original site: Q3MFH1 
ID   RIMO_ANAVT              Reviewed;         440 AA.
AC   Q3MFH1;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   19-FEB-2014, entry version 72.
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=Ava_0641;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA20265.1; -; Genomic_DNA.
DR   RefSeq; YP_321160.1; NC_007413.1.
DR   ProteinModelPortal; Q3MFH1; -.
DR   STRING; 240292.Ava_0641; -.
DR   EnsemblBacteria; ABA20265; ABA20265; Ava_0641.
DR   GeneID; 3678670; -.
DR   KEGG; ava:Ava_0641; -.
DR   PATRIC; 35421676; VBIAnaVar43351_1409.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224766; -.
DR   KO; K14441; -.
DR   OMA; CLMQRYR; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   ProtClustDB; CLSK893584; -.
DR   BioCyc; AVAR240292:GCY3-644-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; PF01938; TRAM; 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    440       Ribosomal protein S12
FT                                methylthiotransferase RimO.
FT                                /FTId=PRO_0000374697.
FT   DOMAIN        5    116       MTTase N-terminal.
FT   DOMAIN      372    438       TRAM.
FT   METAL        14     14       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        50     50       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       154    154       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       158    158       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       161    161       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   440 AA;  49257 MW;  BED47148BDE09650 CRC64;
     MGEKPTIAIS HLGCEKNRID TEHMLGLLVK AGYGVDTNEE LADYVIVNTC SFIESAREES
     VKTLVELAEA NKKIVITGCM AQHFQTQLLE ELPEAVAVVG TGDYHKIVNV IERAEQGERV
     TLVSAKPTYI ADETTPRYRT TTEGVAYLRV AEGCDYRCAF CIIPHLRGNQ RSRTIESIVA
     EAEQLVAQGV QEIILISQIT TNYGLDIYGK PKLAELLRAL GKINVPWIRM HYAYPTGLTP
     DVIAAIQETP NVLPYLDLPL QHSHSEVLRS MNRPWQGRVN DEIIERLKIA IPGAVLRTTF
     IVGFPGETEA QFEHLLQFVQ RHEFDHVGVF TFSAEEGTPA YKLSNQLPQE VMDERRDRLM
     ALQQPISWRK NQQEVGKTVE VLIEQENPES GKLIGRSGRF SPEVDGQVYV DGEAKLGTII
     PVKIHSADEY DLFGQVVSHN
//
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