(data stored in ACNUC7421 zone)

SWISSPROT: C6AYB8_RHILS

ID   C6AYB8_RHILS            Unreviewed;       473 AA.
AC   C6AYB8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
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   OrderedLocusNames=Rleg_0031 {ECO:0000313|EMBL:ACS54342.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54342.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54342.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54342.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001622; ACS54342.1; -; Genomic_DNA.
DR   RefSeq; WP_012755779.1; NC_012850.1.
DR   ProteinModelPortal; C6AYB8; -.
DR   EnsemblBacteria; ACS54342; ACS54342; Rleg_0031.
DR   KEGG; rlg:Rleg_0031; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; KVCEHFH; -.
DR   OrthoDB; POG091H00LG; -.
DR   Proteomes; UP000002256; 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; C6AYB8.
DR   SWISS-2DPAGE; C6AYB8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077934};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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   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       26    146       MTTase N-terminal. {ECO:0000259|PROSITE:
FT                                PS51449}.
FT   DOMAIN      408    470       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   METAL        35     35       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        71     71       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       109    109       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       187    187       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       191    191       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       194    194       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   473 AA;  52830 MW;  0F11218C857363B4 CRC64;
     MTQDSALLQA PEAIPSDSLH DGSNSRKVFI KTYGCQMNVY DSMRMSDALA RDGYEPTDDM
     EEADLVLLNT CHIREKAAEK VYSALGRLRD MKKKKAADGR EMMIGVAGCV AQAEGEEILR
     RAPAVDVVIG PQTYHRLPEA LRLAKQGQRV VDTEYAIEDK FEHLPIAESR RIRARGVTAF
     LTVQEGCDKF CTFCVVPYTR GSEVSRPVSQ IVEEAEKLAD SGVREITLLG QNVNAWHGAG
     PQGEAWSLGD LLYRLAEIPG LARLRYTTSH PRDMDDRLIN AHRDLSALMP YLHLPVQSGS
     DRILKAMNRR HTAAEYLTLI ERIRTVRPDI ALSGDFITGF PGETDEDFKD TLRLVEEVRY
     AQAFSFKYST RPGTPGAELK DQVPEEIKAE RLERLQMLLL KQQQEFAESC IGKEIDLLLE
     KPGRMPEQLI GRSPWLQSVN VDAKASQIGD IIKVRITGTG TNSLFAERAE AAV
//

If you have problems or comments...

PBIL Back to PBIL home page