ID K1R633_CRAGI Unreviewed; 354 AA.
AC K1R633;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 42.
DE RecName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|RuleBase:RU368081};
DE EC=2.8.4.5 {ECO:0000256|RuleBase:RU368081};
DE Flags: Fragment;
GN ORFNames=CGI_10015051 {ECO:0000313|EMBL:EKC36670.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC36670.1};
RN [1] {ECO:0000313|EMBL:EKC36670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC36670.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU368081}; Single-pass membrane protein
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; JH818398; EKC36670.1; -; Genomic_DNA.
DR AlphaFoldDB; K1R633; -.
DR HOGENOM; CLU_018697_4_0_1; -.
DR InParanoid; K1R633; -.
DR OMA; FMKGKPA; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR020612; Methylthiotransferase_CS.
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 PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 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; 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 Endoplasmic reticulum {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 NON_TER 354
FT /evidence="ECO:0000313|EMBL:EKC36670.1"
SQ SEQUENCE 354 AA; 40080 MW; 3A84FFF853C57FA0 CRC64;
GHSVRLYGQK KLEGKKVGGA ALSLPKIRKN PLIEIIAINT GCLNQCTYCK TKHARGELGS
YPPDEIVARA KQSFEEGVIE IWLTSEDLGA YGHDIGVTLP QLLWKLVEVI PEGARMRLGM
TNPPYILEHL EEMAKILRHP RVYSFLHVPV QSASDSVLMD MKREYCQADF RHVTDFLKER
VPGVTIATDV ICGFPTETED DFEETMKLVE EYKFPSLFIN QFFPRPGTPA AKMPRIPAQL
VKQRTKKISE LFHSYRPYDH KMSEIQQVLV TETSHDQQYY VGHNKFYDQV LVPKNENLMG
KMVTVRIVET GKHFLKGQLL SDKGIVQPDV PLPLKKGQVS GASGLVQVCR QCCK
//
