ID A0A117KX62_9FIRM Unreviewed; 182 AA.
AC A0A117KX62;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|ARBA:ARBA00033765};
DE EC=2.8.4.3 {ECO:0000256|ARBA:ARBA00033765};
DE Flags: Fragment;
GN ORFNames=XD50_0912 {ECO:0000313|EMBL:KUK10900.1};
OS Clostridia bacterium 41_269.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK10900.1, ECO:0000313|Proteomes:UP000053409};
RN [1] {ECO:0000313|Proteomes:UP000053409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine
CC (i(6)A), leading to the formation of 2-methylthio-N6-
CC (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read
CC codons beginning with uridine. {ECO:0000256|ARBA:ARBA00003234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK10900.1}.
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DR EMBL; LGEZ01000008; KUK10900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117KX62; -.
DR STRING; 1635275.XD50_0912; -.
DR PATRIC; fig|1635275.3.peg.604; -.
DR Proteomes; UP000053409; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 1..112
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 115..180
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUK10900.1"
SQ SEQUENCE 182 AA; 20610 MW; 48A49BD9B3485F6C CRC64;
MPLQSGSNRI LKLMGRNYTV EDYGKIVEKA REYMPDISIM SDVIVGFPGE KEIDHQATIN
AVRSFGINKI HVFPYSPRPG TPAEAIKEHV RPDIKKQRVE EMNRLSEVLS LDFHKKLLGK
KLEVLVEKTC IENGIGIAEG FSEYYALVRF KFNDKSILGK IVPVKAEEAY TWGLKGSIKK
DV
//
