ID MIAB_DICNV Reviewed; 456 AA.
AC A5EXA7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE EC=2.-.-.-;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; OrderedLocusNames=DNO_1245;
OS Dichelobacter nodosus (strain VCS1703A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Dichelobacter.
OX NCBI_TaxID=246195;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VCS1703A;
RX PubMed=17468768; DOI=10.1038/nbt1302;
RA Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T.,
RA Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H.,
RA Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y.,
RA Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J.,
RA Adler B., Songer J.G., Rood J.I., Paulsen I.T.;
RT "Genome sequence and identification of candidate vaccine antigens from
RT the animal pathogen Dichelobacter nodosus.";
RL Nat. Biotechnol. 25:569-575(2007).
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC (dimethylallyl)adenosine (i(6)A), leading to the formation of 2-
CC methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37
CC in tRNAs that read codons beginning with uridine (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 -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC subfamily.
CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain.
CC -!- SIMILARITY: Contains 1 TRAM domain.
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DR EMBL; CP000513; ABQ14300.1; -; Genomic_DNA.
DR RefSeq; YP_001210121.1; NC_009446.1.
DR ProteinModelPortal; A5EXA7; -.
DR STRING; 246195.DNO_1245; -.
DR EnsemblBacteria; ABQ14300; ABQ14300; DNO_1245.
DR GeneID; 5122130; -.
DR KEGG; dno:DNO_1245; -.
DR PATRIC; 21786844; VBIDicNod48475_1238.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224767; -.
DR KO; K06168; -.
DR OMA; GIDRIRY; -.
DR BioCyc; DNOD246195:GHHS-1251-MONOMER; -.
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:0006400; P:tRNA modification; IEA:HAMAP.
DR Gene3D; 3.80.30.20; -; 1.
DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 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; IPR006463; MiaB_methiolase.
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; TIGR01574; miaB-methiolase; 1.
DR TIGRFAMs; TIGR00089; TIGR00089; 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; tRNA processing.
FT CHAIN 1 456 (Dimethylallyl)adenosine tRNA
FT methylthiotransferase MiaB.
FT /FTId=PRO_0000374269.
FT DOMAIN 6 123 MTTase N-terminal.
FT DOMAIN 381 444 TRAM.
FT METAL 15 15 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 52 52 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 86 86 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 160 160 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 164 164 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 167 167 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 456 AA; 51013 MW; B20D924B8494970D CRC64;
MQTVLKHVYI ETYGCQMNEY DSSKMLAVLK NSHGITPVAT PEEADVLLLN TCSVREKAQE
KVFSQLGRWK SLKERKPHLI IGVGGCVASQ EGEMIRRRAP EVDVVFGPQT LHRLPNLIEE
AQRSRGGVVD VSFPEIEKFD HLPEPRAEGP TAYVSVMEGC SKYCTYCVVP YTRGAEISRP
FDDVLAECAT LAAQGVREIN LLGQNVNAYR GAMHDGTIAD LALLIEYVAA IPNIGRIRFT
TSHPSEFSDA LIETYRRVPK LVSHLHLPVQ SGSNRILALM KRDYKVAEYQ EKLAKIRAIR
PDISFSSDFI VGFPGEEEED FQATMDLIEA VFFDTSYSFI YSQRPGTPAS TMPDRVPLTV
KKERLARLQA RILEMAASIS EAMVGTEQWV LVDRLSRKSE REVSGRTENN RVVNFSAPAS
LIGRFAKVQI TAAYKNSLRG RLIEAELLPD PVVYTR
//
