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Database: UniProt
Entry: D8JAH0_HALJB
LinkDB: D8JAH0_HALJB
Original site: D8JAH0_HALJB 
ID   D8JAH0_HALJB            Unreviewed;       414 AA.
AC   D8JAH0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|RuleBase:RU368081};
DE            EC=2.8.4.5 {ECO:0000256|RuleBase:RU368081};
GN   OrderedLocusNames=HacjB3_06505 {ECO:0000313|EMBL:ADJ14692.1};
GN   ORFNames=C497_04902 {ECO:0000313|EMBL:ELY39590.1};
OS   Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS   4019 / B3).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halalkalicoccus.
OX   NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ14692.1, ECO:0000313|Proteomes:UP000000390};
RN   [1] {ECO:0000313|EMBL:ADJ14692.1, ECO:0000313|Proteomes:UP000000390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|EMBL:ADJ14692.1}, and DSM 18796 / CECT 7217 /
RC   JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RX   PubMed=20601480; DOI=10.1128/JB.00663-10;
RA   Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT   "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT   halophilic archaeon.";
RL   J. Bacteriol. 192:4528-4529(2010).
RN   [2] {ECO:0000313|Proteomes:UP000011645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY39590.1, ECO:0000313|Proteomes:UP000011645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3 {ECO:0000313|EMBL:ELY39590.1,
RC   ECO:0000313|Proteomes:UP000011645};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC       threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-
CC       methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in
CC       tRNAs that read codons beginning with adenine.
CC       {ECO:0000256|ARBA:ARBA00002399, ECO:0000256|RuleBase:RU368081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + AH2 + N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine =
CC         2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:37075, Rhea:RHEA-COMP:10163,
CC         Rhea:RHEA-COMP:11092, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:74420; EC=2.8.4.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000730,
CC         ECO:0000256|RuleBase:RU368081};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU368081};
CC       Note=Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|RuleBase:RU368081};
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008616,
CC       ECO:0000256|RuleBase:RU368081}.
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DR   EMBL; CP002062; ADJ14692.1; -; Genomic_DNA.
DR   EMBL; AOHV01000013; ELY39590.1; -; Genomic_DNA.
DR   RefSeq; WP_008414924.1; NZ_AXZD01000007.1.
DR   AlphaFoldDB; D8JAH0; -.
DR   STRING; 795797.HacjB3_06505; -.
DR   GeneID; 9419106; -.
DR   KEGG; hje:HacjB3_06505; -.
DR   PATRIC; fig|795797.18.peg.1297; -.
DR   eggNOG; arCOG01358; Archaea.
DR   HOGENOM; CLU_018697_4_2_2; -.
DR   OMA; CEHFHIP; -.
DR   OrthoDB; 372134at2157; -.
DR   Proteomes; UP000000390; Chromosome.
DR   Proteomes; UP000011645; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-UniRule.
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; IPR006466; MiaB-like_arc_euk.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   NCBIfam; TIGR01578; MiaB-like-B; 1.
DR   NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR   PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR   PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 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   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU368081};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368081};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368081};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU368081};
KW   Transferase {ECO:0000256|RuleBase:RU368081};
KW   tRNA processing {ECO:0000256|RuleBase:RU368081}.
FT   DOMAIN          2..107
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51449"
FT   DOMAIN          117..356
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          351..414
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
SQ   SEQUENCE   414 AA;  45646 MW;  36EA271494D5BB5D CRC64;
     MARYHIETYG CTSNRGESRA IESALRDAGH YRAAGPAEAD VAILNTCTVV EKTETNMLRR
     AKELEEETTD LIVTGCMALA QSEAFSDVDA RVMHWDEVPQ AALNGECPTP GPGVEPVLEG
     VVGILPIARG CMSNCSYCIT KHATGRVDSP TIEANVEKAR ALVHAGAKEL RITGQDTGVY
     GWDDGERSLP ELLSRICAIE GEFRVRLGMA NPGGIHGIHE ELAEVFAENE KLYDFIHAPV
     QSGSDEVLEE MRRQHKVEKF REIVKTFDRE LDHWTLSTDF IVGFPTETEA DHELSMDLLR
     EIRPEKVNVT RFSKRPKTDA ADMKGLGGTI KKERSKAMSE AKREIVGEVY EGMVGDTCEV
     LCVQPGTGDS VKCRDPAYRQ VIVQNASEYG IEPGDFFEAE ITASQTMYAF GKPV
//
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