tRNA N6-adenosine threonylcarbamoyltransferase is part of the enzyme complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
6-321
0e+00
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.
:
Pssm-ID: 466982 Cd Length: 309 Bit Score: 644.60 E-value: 0e+00
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
6-321
0e+00
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.
Pssm-ID: 466982 Cd Length: 309 Bit Score: 644.60 E-value: 0e+00
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
8-344
2.37e-155
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274747 Cd Length: 322 Bit Score: 438.61 E-value: 2.37e-155
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
31-311
1.28e-108
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234
Pssm-ID: 395656 Cd Length: 272 Bit Score: 318.17 E-value: 1.28e-108
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
8-323
4.58e-57
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440299 Cd Length: 333 Bit Score: 188.29 E-value: 4.58e-57
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
6-321
0e+00
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.
Pssm-ID: 466982 Cd Length: 309 Bit Score: 644.60 E-value: 0e+00
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
6-321
2.84e-158
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called kinase-associated endopeptidase 1, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, kinase-associated endopeptidase 1 (Kae1), t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is the mammalian orthologue of kinase-associated endopeptidase Kae1. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.
Pssm-ID: 466946 Cd Length: 301 Bit Score: 445.34 E-value: 2.84e-158
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
8-344
2.37e-155
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 274747 Cd Length: 322 Bit Score: 438.61 E-value: 2.37e-155
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
5-340
3.10e-153
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and similar proteins mainly from archaea and bacteria; Kae1 (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.
Pssm-ID: 466981 Cd Length: 323 Bit Score: 433.23 E-value: 3.10e-153
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
7-319
2.55e-142
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine threonylcarbamoyltransferase; tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The family includes different orthologous of tRNA N6-adenosine threonylcarbamoyltransferase, such as bacterial kinase-associated endopeptidase 1 (Kae1) and TsaD (also known as YgjD) protein, mammalian O-sialoglycoprotein endopeptidase (OSGEP) and yeast protein Kae1, as well as mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.
Pssm-ID: 466881 Cd Length: 304 Bit Score: 404.94 E-value: 2.55e-142
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
31-311
1.28e-108
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234
Pssm-ID: 395656 Cd Length: 272 Bit Score: 318.17 E-value: 1.28e-108
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
8-311
1.45e-91
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted O-sialoglycoprotein endopeptidase (glycoprotease, EC 3.4.24.57) of Pasteurella haemolytica, a pathogen. A member from Riemerella anatipestifer, associated with cohemolysin activity, likewise is exported without benefit of a classical signal peptide and shows glycoprotease activity on the test substrate glycophorin. However, archaeal members of this subfamily show unrelated activities as demonstrated in Pyrococcus abyssi: DNA binding, iron binding, apurinic endonuclease activity, genomic association with a kinase domain, and no glycoprotease activity. This family thus pulls together a set of proteins as a homology group that appears to be near-universal in life, yet heterogeneous in assayed function between bacteria and archaea. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 129429 [Multi-domain] Cd Length: 305 Bit Score: 275.77 E-value: 1.45e-91
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
8-323
1.91e-66
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Pssm-ID: 466983 Cd Length: 328 Bit Score: 212.34 E-value: 1.91e-66
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
8-319
7.98e-61
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial members of a protein family that is widely distributed. In a few pathogenic species, the protein is exported in a way that may represent an exceptional secondary function. This model plus companion (archaeal) model TIGR03722 together span the prokaryotic member sequences of TIGR00329, a protein family that appears universal in life, and whose broad function is unknown. A member of TIGR03722 has been characterized as a DNA-binding protein with apurinic endopeptidase activity. In contrast, the rare characterized members of the present family show O-sialoglycoprotein endopeptidase (EC. 3.4.24.57) activity after export. These include glycoprotease (gcp) from Pasteurella haemolytica A1 and a cohemolysin from Riemerella anatipestifer (GB|AAG39646.1). The member from Staphylococcus aureus is essential and is related to cell wall dynamics and the modulation of autolysis, but members are also found in the Mycoplasmas (which lack a cell wall). A reasonable hypothesis is that virulence-related activities after export are secondary to a bacterial domain-wide unknown function. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274748 Cd Length: 313 Bit Score: 197.26 E-value: 7.98e-61
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
8-323
4.58e-57
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440299 Cd Length: 333 Bit Score: 188.29 E-value: 4.58e-57
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
8-319
1.94e-54
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) and similar proteins from eukayotes; The family includes mammalian OSGEPL1 and yeast QRI7, which are the mitochondrial orthologs of the universal Kae1/ TsaD (also known as YgjD) protein. OSGEPL1/QRI7 (EC 2.3.1.234), also called mitochondrial tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. It is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. It is involved in mitochondrial genome maintenance.
Pssm-ID: 466984 Cd Length: 330 Bit Score: 181.18 E-value: 1.94e-54
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
7-315
1.66e-51
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA N6-adenosine threonylcarbamoyltransferase Kae1/TsaD, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ), as well as proteins from the NodU/CmcH subfamily. tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TsaB is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7) is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2) functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12) acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. nodulation protein NolNO (EC 2.1.3.-) is involved in the O-carbamoylation of nod factors. The NodU/CmcH subfamily proteins consist of two domains. Only the N-terminal domain shows similarity with Kae1/TsaB-like domain, which belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466851 [Multi-domain] Cd Length: 186 Bit Score: 169.17 E-value: 1.66e-51
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
8-320
1.62e-45
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. The family also includes mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.
Pssm-ID: 466947 Cd Length: 313 Bit Score: 157.83 E-value: 1.62e-45
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
52-116
2.51e-09
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440827 Cd Length: 227 Bit Score: 56.78 E-value: 2.51e-09
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
52-116
9.35e-09
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ) and similar proteins; TsaB, also called t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, it can act as a protease that specifically degrades TsaD in vitro; therefore, TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. TsaB does not show sialoglycoprotease activity against glycophorin A.
Pssm-ID: 466882 [Multi-domain] Cd Length: 205 Bit Score: 54.59 E-value: 9.35e-09
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
8-116
1.66e-07
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274750 [Multi-domain] Cd Length: 204 Bit Score: 51.11 E-value: 1.66e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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