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Database: UniProt
Entry: A0A0B0EPF7_9BACT
LinkDB: A0A0B0EPF7_9BACT
Original site: A0A0B0EPF7_9BACT 
ID   A0A0B0EPF7_9BACT        Unreviewed;       196 AA.
AC   A0A0B0EPF7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=SCABRO_01726 {ECO:0000313|EMBL:KHE92515.1};
OS   Candidatus Scalindua brodae.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Scalindua.
OX   NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE92515.1, ECO:0000313|Proteomes:UP000030652};
RN   [1] {ECO:0000313|EMBL:KHE92515.1, ECO:0000313|Proteomes:UP000030652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU1 {ECO:0000313|EMBL:KHE92515.1};
RA   Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT   "Draft genome of anammox bacterium scalindua brodae, obtained using
RT   differential coverage binning of sequence data from two enrichment
RT   reactors.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KHE92515.1}.
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DR   EMBL; JRYO01000121; KHE92515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B0EPF7; -.
DR   PATRIC; fig|237368.3.peg.1880; -.
DR   eggNOG; COG0621; Bacteria.
DR   Proteomes; UP000030652; 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..121
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          124..196
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
SQ   SEQUENCE   196 AA;  21744 MW;  F7E95489F9F8D639 CRC64;
     MPGVCEYLHM PAQSGSDRIL KKMRRQYTSA HYMELVEMAK SIVPGIKISS DFIVGFPGET
     EEDFQDTVNL LNDVRCQNSF IFKYSPRTGT AAIELSDDVI EEAKKSRNHI LLELQEKIST
     EENRKMHGKS VEVLAEGESK SNAGRLIGRT RQNQVVVFSP PEGINQADIS SALPGTLVNI
     EIVDSTALTL FGVINE
//
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