(data stored in SCRATCH zone)

SWISSPROT: C3MF08_SINFN

ID   C3MF08_SINFN            Unreviewed;       466 AA.
AC   C3MF08;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763205};
DE            EC=2.8.4.3 {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763213};
DE   AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000256|HAMAP-Rule:MF_01864};
DE   AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000256|HAMAP-Rule:MF_01864};
GN   Name=miaB {ECO:0000256|HAMAP-Rule:MF_01864,
GN   ECO:0000313|EMBL:ACP23845.1};
GN   OrderedLocusNames=NGR_c00410 {ECO:0000313|EMBL:ACP23845.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23845.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23845.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763283}.
CC   -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA +
CC       sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced
CC       electron acceptor = 2-methylthio-N(6)-dimethylallyladenine(37) in
CC       tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine
CC       + 5'-deoxyadenosine + electron acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_01864, ECO:0000256|SAAS:SAAS00763238}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01864};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01864};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00763304}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00763209}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00763254}.
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DR   EMBL; CP001389; ACP23845.1; -; Genomic_DNA.
DR   RefSeq; WP_012706630.1; NC_012587.1.
DR   RefSeq; YP_002824598.1; NC_012587.1.
DR   ProteinModelPortal; C3MF08; -.
DR   STRING; 394.NGR_c00410; -.
DR   EnsemblBacteria; ACP23845; ACP23845; NGR_c00410.
DR   GeneID; 7790620; -.
DR   KEGG; rhi:NGR_c00410; -.
DR   PATRIC; fig|394.7.peg.2833; -.
DR   eggNOG; ENOG4105CIW; Bacteria.
DR   eggNOG; COG0621; LUCA.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; KVCEHFH; -.
DR   OrthoDB; POG091H00LG; -.
DR   Proteomes; UP000001054; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
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   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA_; 1.
DR   SFLD; SFLDG01061; methylthiotransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 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;
DR   PRODOM; C3MF08.
DR   SWISS-2DPAGE; C3MF08.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077934};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763228};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00077904};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455342};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455284};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763201};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763263}.
FT   DOMAIN       22    142       MTTase N-terminal. {ECO:0000259|PROSITE:
FT                                PS51449}.
FT   DOMAIN      404    466       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   METAL        31     31       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        67     67       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       105    105       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       183    183       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       187    187       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       190    190       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   466 AA;  51652 MW;  5D17D0A37053D5C2 CRC64;
     MTQETALLPK SPRAGDEHVP ARKVFVKTYG CQMNVYDSDR MSDALSRDGY VATDVLEDAD
     FVLLNTCHIR EKAAEKVYSE LGRLRELKKA KASEGREMVI GVAGCVAQAE GNEILRRAPA
     VDLVIGPQTY HRLPEALKRA RSGERVVETD YAIEDKFEHL PAPDKAKTRS RGVTAFLTVQ
     EGCDKFCTFC VVPYTRGAEV SRPVAQILAE AEKLVDGGVR EITLLGQNVN AWHGAGPNGR
     DWGLGDLLRR LGEIDGLARL RYTTSHPRDM DESLIEAHRS MAKLMPYLHL PVQSGSDRIL
     KAMNRRHTAA EYLALVERIR AVQPDLALSG DFIVGFPGET EADFEETMRL VEVVGYAQAF
     SFKYSTRPGT PGADLKDQVP EDVKAKRLER LQSLLVNQQR DFAAACVGRE IDLLLEKPGR
     MPGQLVGRSP WLQPVNVDAK RSQIGDIIKV RITKAGSNSL FAEMIE
//

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