OSGEP_HUMAN
ID OSGEP_HUMAN Reviewed; 335 AA.
AC Q9NPF4; Q6IAC3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000305|PubMed:28805828};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE Short=t(6)A synthase;
DE AltName: Full=O-sialoglycoprotein endopeptidase {ECO:0000255|HAMAP-Rule:MF_03180};
DE Short=hOSGEP {ECO:0000303|PubMed:12039036};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180};
GN Name=OSGEP {ECO:0000255|HAMAP-Rule:MF_03180, ECO:0000303|PubMed:12039036};
GN Synonyms=GCPL1;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=12039036; DOI=10.1016/s0378-1119(02)00429-8;
RA Seki Y., Ikeda S., Kiyohara H., Ayabe H., Seki T., Matsui H.;
RT "Sequencing analysis of a putative human O-sialoglycoprotein endopeptidase
RT gene (OSGEP) and analysis of a bidirectional promoter between the OSGEP and
RT APEX genes.";
RL Gene 285:101-108(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Wigelsworth D.J., Coadwell J., Rawlings N.D., Barrett A.J.;
RT "Cloning and sequencing of putative human sialoglycoprotease.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Carcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [6]
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 [7]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, INTERACTION WITH PRAME, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22912744; DOI=10.1371/journal.pone.0042822;
RA Costessi A., Mahrour N., Sharma V., Stunnenberg R., Stoel M.A., Tijchon E.,
RA Conaway J.W., Conaway R.C., Stunnenberg H.G.;
RT "The human EKC/KEOPS complex is recruited to Cullin2 ubiquitin ligases by
RT the human tumour antigen PRAME.";
RL PLoS ONE 7:E42822-E42822(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX.
RX PubMed=27903914; DOI=10.1093/nar/gkw1181;
RA Wan L.C., Maisonneuve P., Szilard R.K., Lambert J.P., Ng T.F., Manczyk N.,
RA Huang H., Laister R., Caudy A.A., Gingras A.C., Durocher D., Sicheri F.;
RT "Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a
RT core subunit homologous to yeast Gon7.";
RL Nucleic Acids Res. 45:805-817(2017).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE EKC/KEOPS COMPLEX,
RP INVOLVEMENT IN GAMOS3, AND VARIANT GAMOS3 GLN-325.
RX PubMed=28272532; DOI=10.1038/ejhg.2017.30;
RA Edvardson S., Prunetti L., Arraf A., Haas D., Bacusmo J.M., Hu J.F.,
RA Ta-Shma A., Dedon P.C., de Crecy-Lagard V., Elpeleg O.;
RT "tRNA N6-adenosine threonylcarbamoyltransferase defect due to KAE1/TCS3
RT (OSGEP) mutation manifest by neurodegeneration and renal tubulopathy.";
RL Eur. J. Hum. Genet. 25:545-551(2017).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
RP EKC/KEOPS COMPLEX, INVOLVEMENT IN GAMOS3, VARIANTS GAMOS3 PHE-14; GLU-78;
RP MET-107; ARG-110; THR-111; THR-139; ALA-177; ARG-198; GLN-247; CYS-280;
RP HIS-280; LEU-280; GLN-325 AND TRP-325, AND CHARACTERIZATION OF VARIANTS
RP GAMOS3 PHE-14; ARG-110; THR-111; ARG-198; GLN-247; LEU-280 AND GLN-325.
RX PubMed=28805828; DOI=10.1038/ng.3933;
RA Braun D.A., Rao J., Mollet G., Schapiro D., Daugeron M.C., Tan W.,
RA Gribouval O., Boyer O., Revy P., Jobst-Schwan T., Schmidt J.M.,
RA Lawson J.A., Schanze D., Ashraf S., Ullmann J.F.P., Hoogstraten C.A.,
RA Boddaert N., Collinet B., Martin G., Liger D., Lovric S., Furlano M.,
RA Guerrera I.C., Sanchez-Ferras O., Hu J.F., Boschat A.C., Sanquer S.,
RA Menten B., Vergult S., De Rocker N., Airik M., Hermle T., Shril S.,
RA Widmeier E., Gee H.Y., Choi W.I., Sadowski C.E., Pabst W.L., Warejko J.K.,
RA Daga A., Basta T., Matejas V., Scharmann K., Kienast S.D., Behnam B.,
RA Beeson B., Begtrup A., Bruce M., Ch'ng G.S., Lin S.P., Chang J.H.,
RA Chen C.H., Cho M.T., Gaffney P.M., Gipson P.E., Hsu C.H., Kari J.A.,
RA Ke Y.Y., Kiraly-Borri C., Lai W.M., Lemyre E., Littlejohn R.O., Masri A.,
RA Moghtaderi M., Nakamura K., Ozaltin F., Praet M., Prasad C., Prytula A.,
RA Roeder E.R., Rump P., Schnur R.E., Shiihara T., Sinha M.D., Soliman N.A.,
RA Soulami K., Sweetser D.A., Tsai W.H., Tsai J.D., Topaloglu R., Vester U.,
RA Viskochil D.H., Vatanavicharn N., Waxler J.L., Wierenga K.J., Wolf M.T.F.,
RA Wong S.N., Leidel S.A., Truglio G., Dedon P.C., Poduri A., Mane S.,
RA Lifton R.P., Bouchard M., Kannu P., Chitayat D., Magen D., Callewaert B.,
RA van Tilbeurgh H., Zenker M., Antignac C., Hildebrandt F.;
RT "Mutations in KEOPS-complex genes cause nephrotic syndrome with primary
RT microcephaly.";
RL Nat. Genet. 49:1529-1538(2017).
RN [12] {ECO:0007744|PDB:6GWJ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH GON7 AND LAGE3,
RP IDENTIFICATION IN THE EKC/KEOPS COMPLEX, AND CHARACTERIZATION OF VARIANT
RP GAMOS3 GLN-325.
RX PubMed=31481669; DOI=10.1038/s41467-019-11951-x;
RA Arrondel C., Missoury S., Snoek R., Patat J., Menara G., Collinet B.,
RA Liger D., Durand D., Gribouval O., Boyer O., Buscara L., Martin G.,
RA Machuca E., Nevo F., Lescop E., Braun D.A., Boschat A.C., Sanquer S.,
RA Guerrera I.C., Revy P., Parisot M., Masson C., Boddaert N., Charbit M.,
RA Decramer S., Novo R., Macher M.A., Ranchin B., Bacchetta J., Laurent A.,
RA Collardeau-Frachon S., van Eerde A.M., Hildebrandt F., Magen D.,
RA Antignac C., van Tilbeurgh H., Mollet G.;
RT "Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to
RT Galloway-Mowat syndrome.";
RL Nat. Commun. 10:3967-3967(2019).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely
CC plays a direct catalytic role in this reaction, but requires other
CC protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-
CC Rule:MF_03180, ECO:0000269|PubMed:28272532,
CC ECO:0000269|PubMed:28805828, ECO:0000305|PubMed:22912744,
CC ECO:0000305|PubMed:27903914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000305|PubMed:28805828};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03180};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7,
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes. Interacts
CC with PRAME. {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:27903914,
CC ECO:0000269|PubMed:28805828, ECO:0000269|PubMed:31481669}.
CC -!- INTERACTION:
CC Q9NPF4; O95817: BAG3; NbExp=3; IntAct=EBI-1056510, EBI-747185;
CC Q9NPF4; Q14657: LAGE3; NbExp=4; IntAct=EBI-1056510, EBI-1052105;
CC Q9NPF4; Q96S44: TP53RK; NbExp=4; IntAct=EBI-1056510, EBI-739588;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:28805828}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03180,
CC ECO:0000269|PubMed:22912744, ECO:0000269|PubMed:28805828}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in heart,
CC placenta, liver, kidney, lung, brain, skeletal muscle and pancreas.
CC {ECO:0000269|PubMed:12039036}.
CC -!- DISEASE: Galloway-Mowat syndrome 3 (GAMOS3) [MIM:617729]: A form of
CC Galloway-Mowat syndrome, a severe renal-neurological disease
CC characterized by early-onset nephrotic syndrome associated with
CC microcephaly, central nervous system abnormalities, developmental
CC delays, and a propensity for seizures. Brain anomalies include gyration
CC defects ranging from lissencephaly to pachygyria and polymicrogyria,
CC and cerebellar hypoplasia. Most patients show facial dysmorphism
CC characterized by a small, narrow forehead, large/floppy ears, deep-set
CC eyes, hypertelorism and micrognathia. Additional variable features are
CC visual impairment and arachnodactyly. Most patients die in early
CC childhood. {ECO:0000269|PubMed:28272532, ECO:0000269|PubMed:28805828,
CC ECO:0000269|PubMed:31481669}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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DR EMBL; AB047823; BAB33147.1; -; Genomic_DNA.
DR EMBL; AB050442; BAB33172.1; -; mRNA.
DR EMBL; AJ271669; CAB71031.1; -; mRNA.
DR EMBL; AK000418; BAA91150.1; -; mRNA.
DR EMBL; CR457232; CAG33513.1; -; mRNA.
DR EMBL; BC032310; AAH32310.1; -; mRNA.
DR CCDS; CCDS9549.1; -.
DR RefSeq; NP_060277.1; NM_017807.3.
DR PDB; 6GWJ; X-ray; 1.95 A; K=1-335.
DR PDBsum; 6GWJ; -.
DR AlphaFoldDB; Q9NPF4; -.
DR SASBDB; Q9NPF4; -.
DR SMR; Q9NPF4; -.
DR BioGRID; 120779; 140.
DR CORUM; Q9NPF4; -.
DR IntAct; Q9NPF4; 39.
DR MINT; Q9NPF4; -.
DR STRING; 9606.ENSP00000206542; -.
DR GlyGen; Q9NPF4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPF4; -.
DR PhosphoSitePlus; Q9NPF4; -.
DR BioMuta; OSGEP; -.
DR DMDM; 47605574; -.
DR EPD; Q9NPF4; -.
DR jPOST; Q9NPF4; -.
DR MassIVE; Q9NPF4; -.
DR MaxQB; Q9NPF4; -.
DR PaxDb; Q9NPF4; -.
DR PeptideAtlas; Q9NPF4; -.
DR PRIDE; Q9NPF4; -.
DR ProteomicsDB; 81984; -.
DR Antibodypedia; 22030; 173 antibodies from 24 providers.
DR DNASU; 55644; -.
DR Ensembl; ENST00000206542.9; ENSP00000206542.4; ENSG00000092094.11.
DR GeneID; 55644; -.
DR KEGG; hsa:55644; -.
DR MANE-Select; ENST00000206542.9; ENSP00000206542.4; NM_017807.4; NP_060277.1.
DR UCSC; uc001vxf.4; human.
DR CTD; 55644; -.
DR DisGeNET; 55644; -.
DR GeneCards; OSGEP; -.
DR HGNC; HGNC:18028; OSGEP.
DR HPA; ENSG00000092094; Low tissue specificity.
DR MalaCards; OSGEP; -.
DR MIM; 610107; gene.
DR MIM; 617729; phenotype.
DR neXtProt; NX_Q9NPF4; -.
DR OpenTargets; ENSG00000092094; -.
DR Orphanet; 2065; Galloway-Mowat syndrome.
DR PharmGKB; PA32834; -.
DR VEuPathDB; HostDB:ENSG00000092094; -.
DR eggNOG; KOG2708; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_2_2_1; -.
DR InParanoid; Q9NPF4; -.
DR OMA; MRIMCEE; -.
DR OrthoDB; 829465at2759; -.
DR PhylomeDB; Q9NPF4; -.
DR TreeFam; TF313621; -.
DR PathwayCommons; Q9NPF4; -.
DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol.
DR SignaLink; Q9NPF4; -.
DR BioGRID-ORCS; 55644; 685 hits in 1090 CRISPR screens.
DR ChiTaRS; OSGEP; human.
DR GeneWiki; OSGEP; -.
DR GenomeRNAi; 55644; -.
DR Pharos; Q9NPF4; Tbio.
DR PRO; PR:Q9NPF4; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9NPF4; protein.
DR Bgee; ENSG00000092094; Expressed in right hemisphere of cerebellum and 171 other tissues.
DR ExpressionAtlas; Q9NPF4; baseline and differential.
DR Genevisible; Q9NPF4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:UniProtKB.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; Metal-binding; Nucleus; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..335
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000096984"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT VARIANT 14
FT /note="I -> F (in GAMOS3; strongly reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs1555331969)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080357"
FT VARIANT 78
FT /note="K -> E (in GAMOS3; dbSNP:rs200347983)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080358"
FT VARIANT 107
FT /note="V -> M (in GAMOS3; dbSNP:rs140583554)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080359"
FT VARIANT 110
FT /note="C -> R (in GAMOS3; strongly reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs140076803)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080360"
FT VARIANT 111
FT /note="I -> T (in GAMOS3; strongly reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs1443735811)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080361"
FT VARIANT 139
FT /note="I -> T (in GAMOS3; dbSNP:rs1334263407)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080362"
FT VARIANT 177
FT /note="G -> A (in GAMOS3; dbSNP:rs778931753)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080363"
FT VARIANT 198
FT /note="K -> R (in GAMOS3; reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080364"
FT VARIANT 247
FT /note="R -> Q (in GAMOS3; reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs773173317)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080365"
FT VARIANT 280
FT /note="R -> C (in GAMOS3; dbSNP:rs374322839)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080366"
FT VARIANT 280
FT /note="R -> H (in GAMOS3; dbSNP:rs144732839)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080367"
FT VARIANT 280
FT /note="R -> L (in GAMOS3; reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs144732839)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080368"
FT VARIANT 325
FT /note="R -> Q (in GAMOS3; reduced formation of a
FT threonylcarbamoyl group on adenosine at position 37
FT (t(6)A37) in tRNAs; dbSNP:rs753237335)"
FT /evidence="ECO:0000269|PubMed:28272532,
FT ECO:0000269|PubMed:28805828, ECO:0000269|PubMed:31481669"
FT /id="VAR_080369"
FT VARIANT 325
FT /note="R -> W (in GAMOS3; dbSNP:rs761839638)"
FT /evidence="ECO:0000269|PubMed:28805828"
FT /id="VAR_080370"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 10..20
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 42..64
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 205..221
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 226..252
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:6GWJ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:6GWJ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:6GWJ"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6GWJ"
SQ SEQUENCE 335 AA; 36427 MW; 54DCBBB26C03E8FB CRC64;
MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR AVILDLLQEA
LTESGLTSQD IDCIAYTKGP GMGAPLVSVA VVARTVAQLW NKPLVGVNHC IGHIEMGRLI
TGATSPTVLY VSGGNTQVIA YSEHRYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI
EQMAKRGKKL VELPYTVKGM DVSFSGILSF IEDVAHRMLA TGECTPEDLC FSLQETVFAM
LVEITERAMA HCGSQEALIV GGVGCNVRLQ EMMATMCQER GARLFATDER FCIDNGAMIA
QAGWEMFRAG HRTPLSDSGV TQRYRTDEVE VTWRD
