ID A0A0P8Y5R0_9PROT Unreviewed; 443 AA.
AC A0A0P8Y5R0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=JI56_03775 {ECO:0000313|EMBL:KPU81942.1};
OS SAR11 cluster bacterium PRT-SC02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=1527298 {ECO:0000313|EMBL:KPU81942.1, ECO:0000313|Proteomes:UP000050662};
RN [1] {ECO:0000313|EMBL:KPU81942.1, ECO:0000313|Proteomes:UP000050662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRT-SC02 {ECO:0000313|EMBL:KPU81942.1};
RA Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT Rico Trench Inferred From Single Cell Genomes.";
RL Submitted (AUG-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:KPU81942.1}.
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DR EMBL; JPUP01000096; KPU81942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8Y5R0; -.
DR PATRIC; fig|1527298.3.peg.741; -.
DR Proteomes; UP000050662; Unassembled WGS sequence.
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:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 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; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006463; MiaB_methiolase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR NCBIfam; TIGR01574; miaB-methiolase; 1.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 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; PF00919; UPF0004; 1.
DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01061; methylthiotransferase; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51449; MTTASE_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000050662};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPU81942.1}.
FT DOMAIN 3..119
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 144..370
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 373..435
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 443 AA; 51388 MW; 6E2573E5C0AD1BC4 CRC64;
MQKKIFIKTF GCQMNEYDSD RIIDLIKING YEKTLHSDQA DCYIINTCHI REKATEKVFH
DIGRVKKKFR NRKKPILIIS GCVAQAEGDI LIQKEKYIDA VIGPQSYQNI NEIIKNIENR
NIRTESTEFD VVQKFDSLNK IKKLSNKISS YLTIQEGCDK FCKFCVVPYT RGPEYSRGFE
EIINEAEVLV SKGAKEIVLL GQNVNAYSNN KKKLSDIIYK LDEIKNLKRI RFTTSHPIDM
TDDLIEAFKY SSKLMPFLHL PVQSGSSKIL KLMNRKHTVN YYYDIINKLK KANPSMKFSS
DFIIGYPGET KEDFNETIRL MSKIKFINTY SFIFSPRPGT PASKLKSVDK NQALIRLQEF
QKLSEKIKYN YKNELLGKTV RVLVENRLKN QNKYFGKDEF SNSVIIESTR DLTGLEIDIK
VSKINTNTLF GKYDKKKDEY EAA
//
