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 01-MAY-2013, entry version 68.
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; CPDITLR; -.
DR ProtClustDB; CLSK893584; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0016740; F:transferase activity; IEA:HAMAP.
DR GO; GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid; IEA: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
//
