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Database: UniProt
Entry: A0A0R2QYB1_9ACTN
LinkDB: A0A0R2QYB1_9ACTN
Original site: A0A0R2QYB1_9ACTN 
ID   A0A0R2QYB1_9ACTN        Unreviewed;       463 AA.
AC   A0A0R2QYB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ABR78_07925 {ECO:0000313|EMBL:KRO53682.1};
OS   Acidimicrobiia bacterium BACL6 MAG-120910-bin40.
OC   Bacteria; Actinomycetota; Acidimicrobiia.
OX   NCBI_TaxID=1655586 {ECO:0000313|EMBL:KRO53682.1, ECO:0000313|Proteomes:UP000050903};
RN   [1] {ECO:0000313|EMBL:KRO53682.1, ECO:0000313|Proteomes:UP000050903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL6 MAG-120910-bin40 {ECO:0000313|EMBL:KRO53682.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-2015) 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KRO53682.1}.
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DR   EMBL; LIBI01000009; KRO53682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2QYB1; -.
DR   STRING; 1655586.ABR78_07925; -.
DR   Proteomes; UP000050903; 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; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR038135; Methylthiotransferase_N_sf.
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; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDG01061; methylthiotransferase; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRO53682.1}.
FT   DOMAIN          1..110
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51449"
FT   DOMAIN          137..381
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          383..447
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  51471 MW;  0B599D2C790B95A3 CRC64;
     MNAHDSERIS GLLEQDGMER AESEDDADLV VLNTCCIREN ADEKLYGSLG WLKPWKEKGI
     ELGRERQIMV AGCLAQKDKD QVRKRAPYVD VVMGTHNVHR AIDLLEHASM RGGITEIFDE
     AVIDDHALFP SALPVRRERS YNAWVTIQIG CDNTCTYCIV PSVRGKEISR PFSDIVDEVA
     ALARDGVTEI SLLGQNVNSY GRDLSLDARR AGDTEIKLRP QFAELLRAVG AVDGIRRVRY
     VSPHPKDMNL ETLMAMAETP AVCEHLHYPL QSGSDRVLTL MHRGYTAQKY LEKIAQARSL
     ITDAAVTTDI IVGFPGETEA DFVQSLEVAA EAQFDSAYLF IFSPREGTEA AKMAEHFIAP
     EVMSSRYDRM KVVLDHSAII KHEARIGRIE EVIVEGRNKR DAGAFTGRTR QNKLVHFKSA
     DALRAGTYAT VEITSAARFH LSGQLIEVGA EPTHKVRLSV QAL
//
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