CDKAL_DROPS
ID CDKAL_DROPS Reviewed; 553 AA.
AC Q291H5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=GA19679;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00780};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|PROSITE-ProRule:PRU00780};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000071; EAL25137.1; -; Genomic_DNA.
DR RefSeq; XP_001360562.1; XM_001360525.3.
DR AlphaFoldDB; Q291H5; -.
DR SMR; Q291H5; -.
DR STRING; 7237.FBpp0276825; -.
DR EnsemblMetazoa; FBtr0278387; FBpp0276825; FBgn0079675.
DR GeneID; 4803921; -.
DR KEGG; dpo:Dpse_GA19679; -.
DR eggNOG; KOG4355; Eukaryota.
DR HOGENOM; CLU_018697_4_1_1; -.
DR InParanoid; Q291H5; -.
DR OMA; HYAYPTG; -.
DR PhylomeDB; Q291H5; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0079675; Expressed in female reproductive system and 2 other tissues.
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; IEA:InterPro.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.12160; -; 1.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
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_B.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR01578; MiaB-like-B; 1.
DR TIGRFAMs; TIGR00089; TIGR00089; 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; Iron; Iron-sulfur; Membrane; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix;
KW tRNA processing.
FT CHAIN 1..553
FT /note="Threonylcarbamoyladenosine tRNA
FT methylthiotransferase"
FT /id="PRO_0000298677"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 72..179
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT DOMAIN 207..438
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 438..500
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT REGION 21..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 221
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 225
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 553 AA; 62720 MW; 62680891300F7A89 CRC64;
MQQLEQDFPG NDIDDIEDLI SAEDVKPQER YQNKKSVTVR AKKRVQIKPE TDAEEKPTPR
PTIYESVIPG TQKVFVKTWG CAHNNSDSEY MAGQLAAYGY KLSGKDEADL WLLNSCTVKN
PSEDTFRNEI ESGMSNGKHI VVAGCVPQGA PKSDYLRGLS VIGVQQIDRV VEVVEETLKG
HSVRLLQNKK VHGRRVAGAP LSLPKVRKNP LIEIISINTG CLNQCTYCKT KHARGDLASY
PPEEIVDRAR QSFAEGCCEI WLTSEDTGAY GRDIGSSLPE LLWKLVEVIP EHCMLRVGMT
NPPYILEHLE EVAKVLQHPR VYAFLHVPVQ SGSDSVLGEM KREYCRKDFE HVVDFLRERV
PGVTIATDII CGFPTETEED FEETMTLCGR YRFPSLFINQ FFPRPGTPAA KMERIPANLV
KKRTKRLTDL FYSYEPYAQR VGEMYTVLVT EISHDKLHYV GHNKSYEQVL LPMRDNLLGT
RVHVRITSVS KFSMVGEILD DERDWTRCAK KQEAPMELTI TGRNRDKLIQ RYVGIALVVG
SLAFLLQLLI RFL
