CDKAL_HUMAN
ID CDKAL_HUMAN Reviewed; 579 AA.
AC Q5VV42; A8K6S0; Q6P385; Q6ZR27; Q9NXB3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Threonylcarbamoyladenosine tRNA methylthiotransferase;
DE EC=2.8.4.5 {ECO:0000250|UniProtKB:Q91WE6};
DE AltName: Full=CDK5 regulatory subunit-associated protein 1-like 1;
DE AltName: Full=tRNA-t(6)A37 methylthiotransferase;
GN Name=CDKAL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM.
RX PubMed=17460697; DOI=10.1038/ng2043;
RA Steinthorsdottir V., Thorleifsson G., Reynisdottir I., Benediktsson R.,
RA Jonsdottir T., Walters G.B., Styrkarsdottir U., Gretarsdottir S.,
RA Emilsson V., Ghosh S., Baker A., Snorradottir S., Bjarnason H., Ng M.C.,
RA Hansen T., Bagger Y., Wilensky R.L., Reilly M.P., Adeyemo A., Chen Y.,
RA Zhou J., Gudnason V., Chen G., Huang H., Lashley K., Doumatey A., So W.Y.,
RA Ma R.C., Andersen G., Borch-Johnsen K., Jorgensen T.,
RA van Vliet-Ostaptchouk J.V., Hofker M.H., Wijmenga C., Christiansen C.,
RA Rader D.J., Rotimi C., Gurney M., Chan J.C., Pedersen O., Sigurdsson G.,
RA Gulcher J.R., Thorsteinsdottir U., Kong A., Stefansson K.;
RT "A variant in CDKAL1 influences insulin response and risk of type 2
RT diabetes.";
RL Nat. Genet. 39:770-775(2007).
RN [6]
RP INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM.
RX PubMed=17463246; DOI=10.1126/science.1142358;
RA Saxena R., Voight B.F., Lyssenko V., Burtt N.P., de Bakker P.I., Chen H.,
RA Roix J.J., Kathiresan S., Hirschhorn J.N., Daly M.J., Hughes T.E.,
RA Groop L., Altshuler D., Almgren P., Florez J.C., Meyer J., Ardlie K.,
RA Bengtsson Bostrom K., Isomaa B., Lettre G., Lindblad U., Lyon H.N.,
RA Melander O., Newton-Cheh C., Nilsson P., Orho-Melander M., Rastam L.,
RA Speliotes E.K., Taskinen M.R., Tuomi T., Guiducci C., Berglund A.,
RA Carlson J., Gianniny L., Hackett R., Hall L., Holmkvist J., Laurila E.,
RA Sjogren M., Sterner M., Surti A., Svensson M., Svensson M., Tewhey R.,
RA Blumenstiel B., Parkin M., Defelice M., Barry R., Brodeur W., Camarata J.,
RA Chia N., Fava M., Gibbons J., Handsaker B., Healy C., Nguyen K., Gates C.,
RA Sougnez C., Gage D., Nizzari M., Gabriel S.B., Chirn G.W., Ma Q.,
RA Parikh H., Richardson D., Ricke D., Purcell S.;
RT "Genome-wide association analysis identifies loci for type 2 diabetes and
RT triglyceride levels.";
RL Science 316:1331-1336(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23048041; DOI=10.1074/jbc.m112.376558;
RA Brambillasca S., Altkrueger A., Colombo S., Friedrich A., Eickelmann P.,
RA Mark M., Borgese N., Solimena M.;
RT "CDK5 regulatory subunit associated protein 1-like 1 (CDKAL1) is a tail-
RT anchored protein in the endoplasmic reticulum (ER) of insulinoma cells.";
RL J. Biol. Chem. 287:41808-41819(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-122 AND THR-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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 -!- INTERACTION:
CC Q5VV42; P54252: ATXN3; NbExp=3; IntAct=EBI-10194801, EBI-946046;
CC Q5VV42; P06239: LCK; NbExp=3; IntAct=EBI-10194801, EBI-1348;
CC Q5VV42; O76024: WFS1; NbExp=3; IntAct=EBI-10194801, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23048041}; Single-pass membrane protein
CC {ECO:0000255}. Note=Is a tail-anchored protein that exploits the TCR40
CC pathway for insertion into the endoplasmic reticulum.
CC {ECO:0000269|PubMed:23048041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5VV42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VV42-2; Sequence=VSP_027450, VSP_027453;
CC Name=3;
CC IsoId=Q5VV42-3; Sequence=VSP_027451, VSP_027452;
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic islets.
CC {ECO:0000269|PubMed:23048041}.
CC -!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]:
CC A multifactorial disorder of glucose homeostasis caused by a lack of
CC sensitivity to the body's own insulin. Affected individuals usually
CC have an obese body habitus and manifestations of a metabolic syndrome
CC characterized by diabetes, insulin resistance, hypertension and
CC hypertriglyceridemia. The disease results in long-term complications
CC that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:17460697, ECO:0000269|PubMed:17463246}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC87494.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK000349; BAA91102.1; -; mRNA.
DR EMBL; AK128546; BAC87494.1; ALT_FRAME; mRNA.
DR EMBL; AK291735; BAF84424.1; -; mRNA.
DR EMBL; AL022717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55426.1; -; Genomic_DNA.
DR EMBL; BC064145; AAH64145.1; -; mRNA.
DR EMBL; BC121020; AAI21021.1; -; mRNA.
DR EMBL; BC121021; AAI21022.1; -; mRNA.
DR CCDS; CCDS4546.1; -. [Q5VV42-1]
DR RefSeq; NP_060244.2; NM_017774.3. [Q5VV42-1]
DR AlphaFoldDB; Q5VV42; -.
DR SMR; Q5VV42; -.
DR BioGRID; 120247; 250.
DR IntAct; Q5VV42; 45.
DR MINT; Q5VV42; -.
DR STRING; 9606.ENSP00000274695; -.
DR iPTMnet; Q5VV42; -.
DR MetOSite; Q5VV42; -.
DR PhosphoSitePlus; Q5VV42; -.
DR SwissPalm; Q5VV42; -.
DR BioMuta; CDKAL1; -.
DR DMDM; 74747199; -.
DR EPD; Q5VV42; -.
DR jPOST; Q5VV42; -.
DR MassIVE; Q5VV42; -.
DR MaxQB; Q5VV42; -.
DR PaxDb; Q5VV42; -.
DR PeptideAtlas; Q5VV42; -.
DR PRIDE; Q5VV42; -.
DR ProteomicsDB; 65438; -. [Q5VV42-1]
DR ProteomicsDB; 65439; -. [Q5VV42-2]
DR ProteomicsDB; 65440; -. [Q5VV42-3]
DR Antibodypedia; 2738; 247 antibodies from 32 providers.
DR DNASU; 54901; -.
DR Ensembl; ENST00000274695.8; ENSP00000274695.4; ENSG00000145996.11. [Q5VV42-1]
DR Ensembl; ENST00000378610.1; ENSP00000367873.1; ENSG00000145996.11. [Q5VV42-1]
DR Ensembl; ENST00000613575.4; ENSP00000481755.1; ENSG00000145996.11. [Q5VV42-3]
DR GeneID; 54901; -.
DR KEGG; hsa:54901; -.
DR MANE-Select; ENST00000274695.8; ENSP00000274695.4; NM_017774.3; NP_060244.2.
DR UCSC; uc003ndb.2; human. [Q5VV42-1]
DR CTD; 54901; -.
DR DisGeNET; 54901; -.
DR GeneCards; CDKAL1; -.
DR HGNC; HGNC:21050; CDKAL1.
DR HPA; ENSG00000145996; Low tissue specificity.
DR MIM; 125853; phenotype.
DR MIM; 611259; gene.
DR neXtProt; NX_Q5VV42; -.
DR OpenTargets; ENSG00000145996; -.
DR PharmGKB; PA134871999; -.
DR VEuPathDB; HostDB:ENSG00000145996; -.
DR eggNOG; KOG4355; Eukaryota.
DR GeneTree; ENSGT00940000155952; -.
DR HOGENOM; CLU_018697_4_1_1; -.
DR InParanoid; Q5VV42; -.
DR OMA; HYAYPTG; -.
DR OrthoDB; 835984at2759; -.
DR PhylomeDB; Q5VV42; -.
DR TreeFam; TF317476; -.
DR PathwayCommons; Q5VV42; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q5VV42; -.
DR BioGRID-ORCS; 54901; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; CDKAL1; human.
DR GeneWiki; CDKAL1; -.
DR GenomeRNAi; 54901; -.
DR Pharos; Q5VV42; Tbio.
DR PRO; PR:Q5VV42; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VV42; protein.
DR Bgee; ENSG00000145996; Expressed in buccal mucosa cell and 127 other tissues.
DR Genevisible; Q5VV42; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
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:1990145; P:maintenance of translational fidelity; IEA:Ensembl.
DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central.
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; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDG01061; methylthiotransferase; 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 1: Evidence at protein level;
KW 4Fe-4S; Alternative splicing; Diabetes mellitus; Endoplasmic reticulum;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW Transmembrane helix; tRNA processing.
FT CHAIN 1..579
FT /note="Threonylcarbamoyladenosine tRNA
FT methylthiotransferase"
FT /id="PRO_0000298670"
FT TRANSMEM 556..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 64..172
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT DOMAIN 200..431
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 431..493
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 138
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 214
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 218
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 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 MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..94
FT /note="MPSASCDTLLDDIEDIVSQEDSKPQDRHFVRKDVVPKVRRRNTQKYLQEEEN
FT SPPSDSTIPGIQKIWIRTWGCSHNNSDGEYMAGQLAAYGYKI -> MLSRRYEGEIPKN
FT ICKRKKTVHQV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027450"
FT VAR_SEQ 96..97
FT /note="EN -> GE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027451"
FT VAR_SEQ 98..579
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027452"
FT VAR_SEQ 413..433
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027453"
FT VARIANT 484
FT /note="K -> R (in dbSNP:rs9460608)"
FT /id="VAR_052705"
FT CONFLICT 211
FT /note="N -> S (in Ref. 1; BAA91102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 65111 MW; 90818A8A0A19FD1C CRC64;
MPSASCDTLL DDIEDIVSQE DSKPQDRHFV RKDVVPKVRR RNTQKYLQEE ENSPPSDSTI
PGIQKIWIRT WGCSHNNSDG EYMAGQLAAY GYKITENASD ADLWLLNSCT VKNPAEDHFR
NSIKKAQEEN KKIVLAGCVP QAQPRQDYLK GLSIIGVQQI DRVVEVVEET IKGHSVRLLG
QKKDNGRRLG GARLDLPKIR KNPLIEIISI NTGCLNACTY CKTKHARGNL ASYPIDELVD
RAKQSFQEGV CEIWLTSEDT GAYGRDIGTN LPTLLWKLVE VIPEGAMLRL GMTNPPYILE
HLEEMAKILN HPRVYAFLHI PVQSASDSVL MEMKREYCVA DFKRVVDFLK EKVPGITIAT
DIICGFPGET DQDFQETVKL VEEYKFPSLF INQFYPRPGT PAAKMEQVPA QVKKQRTKDL
SRVFHSYSPY DHKIGERQQV LVTEESFDSK FYVAHNQFYE QVLVPKNPAF MGKMVEVDIY
ESGKHFMKGQ PVSDAKVYTP SISKPLAKGE VSGLTKDFRN GLGNQLSSGS HTSAASQCDS
ASSRMVLPMP RLHQDCALRM SVGLALLGLL FAFFVKVYN
