CDKAL_CAEEL
ID CDKAL_CAEEL Reviewed; 425 AA.
AC Q8MXQ7;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase;
DE EC=2.8.4.5 {ECO:0000250|UniProtKB:Q91WE6};
DE AltName: Full=CDKAL1-like protein;
DE AltName: Full=tRNA-t(6)A37 methylthiotransferase;
GN ORFNames=Y92H12BL.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000250|UniProtKB:Q91WE6}.
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:0000250|UniProtKB:Q91WE6};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000305}.
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DR EMBL; FO081632; CCD72949.1; -; Genomic_DNA.
DR RefSeq; NP_740783.2; NM_170800.3.
DR AlphaFoldDB; Q8MXQ7; -.
DR SMR; Q8MXQ7; -.
DR STRING; 6239.Y92H12BL.1; -.
DR EPD; Q8MXQ7; -.
DR PaxDb; Q8MXQ7; -.
DR PeptideAtlas; Q8MXQ7; -.
DR EnsemblMetazoa; Y92H12BL.1a.1; Y92H12BL.1a.1; WBGene00022363.
DR GeneID; 190786; -.
DR KEGG; cel:CELE_Y92H12BL.1; -.
DR UCSC; Y92H12BL.1; c. elegans.
DR CTD; 190786; -.
DR WormBase; Y92H12BL.1a; CE36347; WBGene00022363; -.
DR eggNOG; KOG4355; Eukaryota.
DR HOGENOM; CLU_018697_4_2_1; -.
DR InParanoid; Q8MXQ7; -.
DR OMA; HFHIPLQ; -.
DR OrthoDB; 835984at2759; -.
DR PhylomeDB; Q8MXQ7; -.
DR PRO; PR:Q8MXQ7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022363; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q8MXQ7; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IBA:GO_Central.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC.
DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR006466; MiaB-like_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR01578; MiaB-like-B; 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; Iron; Iron-sulfur; Membrane; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix;
KW tRNA processing.
FT CHAIN 1..425
FT /note="Threonylcarbamoyladenosine tRNA
FT methylthiotransferase"
FT /id="PRO_0000298675"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 60..295
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 293..355
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 425 AA; 48627 MW; BB3C1C1EBAB42EAD CRC64;
MAGCVSQAAP SEPWLQNVSI VGVKQIDRIV EVVGETLKGN KVRLLTRNRP DAVLSLPKMR
KNELIEVLSI STGCLNNCTY CKTKMARGDL VSYPLADLVE QARAAFHDEG VKELWLTSED
LGAWGRDIGL VLPDLLRELV KVIPDGSMMR LGMTNPPYIL DHLEEIAEIL NHPKVYAFLH
IPVQSASDAV LNDMKREYSR RHFEQIADYM IANVPNIYIA TDMILAFPTE TLEDFEESME
LVRKYKFPSL FINQYYPRSG TPAARLKKID TVEARKRTAA MSELFRSYTR YTDERIGELH
RVLVTEVAAD KLHGVGHNKS YEQILVPLEY CKMGEWIEVR VTAVTKFSMI SKPASIQEDQ
QPLSLMHLFP LAVFCLVLIT LYSVDRFLYP GFFEEWLPFL ADAHHDEQQA EMWEHHDNSD
PVFYE
