ID A0A1F8MLK6_9CHLR Unreviewed; 331 AA.
AC A0A1F8MLK6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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};
GN ORFNames=A2Y90_02625 {ECO:0000313|EMBL:OGN99493.1};
OS Chloroflexi bacterium RBG_13_52_12.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797627 {ECO:0000313|EMBL:OGN99493.1, ECO:0000313|Proteomes:UP000180308};
RN [1] {ECO:0000313|EMBL:OGN99493.1, ECO:0000313|Proteomes:UP000180308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN99493.1}.
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DR EMBL; MGMU01000106; OGN99493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MLK6; -.
DR Proteomes; UP000180308; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR003849; Preprotein_translocase_YajC.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR NCBIfam; TIGR00739; yajC; 1.
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 Pfam; PF02699; YajC; 1.
DR PRINTS; PR01853; YAJCTRNLCASE.
DR SMART; SM00729; Elp3; 1.
DR SMART; SM01323; YajC; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..269
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 272..331
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 331 AA; 36386 MW; 7BB83196A8E2DF84 CRC64;
MNKVLKLGLI AGLLITVLVL AGGCAGLLGT PAEGEEASSG SIWPMLIFLV VIFGMFYFVM
IRPQRKRQKE QQTMMAALQK GDKVITAGGI YVLLGQNVDS YGRDLPGKPD LADLLAELNN
IDGLTRLRFL TNHPKDMSRK LIEAIAGLDK VCEQINLPVQ AGSDEILKAM KRGYTVEQYL
KLVGQIREKI PVVAISTDVI VGFPGETAEQ FGRTLNLLST VKFDTVHVAA YSPRAGTAAA
RELEDDVPTD EKKERLNKIE QLQERVQAEI NARLLGKSVE ILVEGRNKGK WYGRTRTDKL
VFFSSGGDYT GQIVKVKIDK TSPWSLQGKI A
//
