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Conserved domains on  [gi|1774222090|ref|NP_001363030|]
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tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial isoform 8 [Homo sapiens]

Protein Classification

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD( domain architecture ID 1009776)

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD 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

CATH:  3.30.420.40
EC:  2.3.1.234
Gene Ontology:  GO:0002949|GO:0061711|GO:0005506
SCOP:  4002236

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 2-174 1.61e-74

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24134:

Pssm-ID: 483947  Cd Length: 330  Bit Score: 228.17  E-value: 1.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLikHPECSTMSGGKAIEHLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQIL 80
Cdd:cd24134   164 FDKVARLLGL--KPLCDGLSGGAALEALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSAADIAATVQHTMACHLVKRTHRAILFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:cd24134   240 PERADIAASFQHAAVRHLEDRLRRALKYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDN 316

                         170
                  ....*....|....
gi 1774222090 161 GIMIAWNGIERLRA 174
Cdd:cd24134   317 GVMIAWAGIERLRA 330
 
Name Accession Description Interval E-value
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 2-174 1.61e-74

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: 228.17  E-value: 1.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLikHPECSTMSGGKAIEHLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQIL 80
Cdd:cd24134   164 FDKVARLLGL--KPLCDGLSGGAALEALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSAADIAATVQHTMACHLVKRTHRAILFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:cd24134   240 PERADIAASFQHAAVRHLEDRLRRALKYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDN 316

                         170
                  ....*....|....
gi 1774222090 161 GIMIAWNGIERLRA 174
Cdd:cd24134   317 GVMIAWAGIERLRA 330
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 3-176 2.77e-35

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: 127.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHFDIKPPLHHAKNCDFSFTGL-----QHVtDKIIMKKEKEegiekg 77
Cdd:COG0533   167 DKVAKLLGL-GYP------GGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLktavlNYI-EKLKQKGEEQ------ 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  78 qilsSAADIAATVQHTMACHLVKRTHRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLC 157
Cdd:COG0533   233 ----DKADIAASFQEAVVDVLVEKTRRALKETGVKRL--------VVAGGVAANSRLRERLEELAEKRGIRLFFPPLELC 300

                         170
                  ....*....|....*....
gi 1774222090 158 TDNGIMIAWNGIERLRAGL 176
Cdd:COG0533   301 TDNAAMIAAAGYERLKAGE 319
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
3-176 4.27e-34

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 124.03  E-value: 4.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGN--RFHFdikPPLHHAKNCDFSFTGL---------QHVTDKiimkkeke 71
Cdd:PRK09604  166 DKVAKLLGL-GYP------GGPAIDKLAKQGDpdAFKF---PRPMDRPGLDFSFSGLktavlntieKSEQTK-------- 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  72 egiekgqilssaADIAATVQHTMACHLVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLC 151
Cdd:PRK09604  228 ------------ADIAASFQAAVVDVLVIKTKRA---LKQTGV----KTLVVA-GGVAANSGLRERLAELAKKRGIEVFI 287

                         170       180
                  ....*....|....*....|....*
gi 1774222090 152 PPPRLCTDNGIMIAWNGIERLRAGL 176
Cdd:PRK09604  288 PPLKLCTDNAAMIAAAGYERLKAGE 312
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-173 1.35e-33

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: 122.15  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGN--RFHFdiKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiek 76
Cdd:TIGR03723 164 DKVARLLGL-GYP------GGPAIDRLAKQGDpkAFKF--PRPMLDRPGLDFSFSGLKtavlNLIEKLKQKGEEL----- 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  77 gqilsSAADIAATVQHTMACHLVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRL 156
Cdd:TIGR03723 230 -----TKADIAASFQAAVVDVLVEKTKRA---LKKTGL----KTLVVA-GGVAANSRLRERLEELAEKRGLEVFFPPLEL 296

                         170
                  ....*....|....*..
gi 1774222090 157 CTDNGIMIAWNGIERLR 173
Cdd:TIGR03723 297 CTDNAAMIAAAGYERLK 313
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 1-166 7.28e-28

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: 106.31  E-value: 7.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGnrfHFDIKPPLhhaKNCDFSFTGLQHVTDKIImkkekeegiekgQIL 80
Cdd:pfam00814 140 AFDKVARLLGL-PYP------GGPKIEKLAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLI------------EKK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSAADIAATVQHTMACHLVKRTHRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:pfam00814 195 EPKEDIAASFQEAVFDHLAEKTERALKLPGAKEL--------VILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDN 266


                  ....*.
gi 1774222090 161 GIMIAW 166
Cdd:pfam00814 267 GAMIAW 272
 
Name Accession Description Interval E-value
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 2-174 1.61e-74

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: 228.17  E-value: 1.61e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLikHPECSTMSGGKAIEHLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQIL 80
Cdd:cd24134   164 FDKVARLLGL--KPLCDGLSGGAALEALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSL 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSAADIAATVQHTMACHLVKRTHRAILFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:cd24134   240 PERADIAASFQHAAVRHLEDRLRRALKYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDN 316

                         170
                  ....*....|....
gi 1774222090 161 GIMIAWNGIERLRA 174
Cdd:cd24134   317 GVMIAWAGIERLRA 330
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 3-176 2.77e-35

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: 127.05  E-value: 2.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHFDIKPPLHHAKNCDFSFTGL-----QHVtDKIIMKKEKEegiekg 77
Cdd:COG0533   167 DKVAKLLGL-GYP------GGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLktavlNYI-EKLKQKGEEQ------ 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  78 qilsSAADIAATVQHTMACHLVKRTHRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLC 157
Cdd:COG0533   233 ----DKADIAASFQEAVVDVLVEKTRRALKETGVKRL--------VVAGGVAANSRLRERLEELAEKRGIRLFFPPLELC 300

                         170
                  ....*....|....*....
gi 1774222090 158 TDNGIMIAWNGIERLRAGL 176
Cdd:COG0533   301 TDNAAMIAAAGYERLKAGE 319
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
3-176 4.27e-34

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 124.03  E-value: 4.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGN--RFHFdikPPLHHAKNCDFSFTGL---------QHVTDKiimkkeke 71
Cdd:PRK09604  166 DKVAKLLGL-GYP------GGPAIDKLAKQGDpdAFKF---PRPMDRPGLDFSFSGLktavlntieKSEQTK-------- 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  72 egiekgqilssaADIAATVQHTMACHLVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLC 151
Cdd:PRK09604  228 ------------ADIAASFQAAVVDVLVIKTKRA---LKQTGV----KTLVVA-GGVAANSGLRERLAELAKKRGIEVFI 287

                         170       180
                  ....*....|....*....|....*
gi 1774222090 152 PPPRLCTDNGIMIAWNGIERLRAGL 176
Cdd:PRK09604  288 PPLKLCTDNAAMIAAAGYERLKAGE 312
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-173 1.35e-33

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: 122.15  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGN--RFHFdiKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiek 76
Cdd:TIGR03723 164 DKVARLLGL-GYP------GGPAIDRLAKQGDpkAFKF--PRPMLDRPGLDFSFSGLKtavlNLIEKLKQKGEEL----- 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  77 gqilsSAADIAATVQHTMACHLVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRL 156
Cdd:TIGR03723 230 -----TKADIAASFQAAVVDVLVEKTKRA---LKKTGL----KTLVVA-GGVAANSRLRERLEELAEKRGLEVFFPPLEL 296

                         170
                  ....*....|....*..
gi 1774222090 157 CTDNGIMIAWNGIERLR 173
Cdd:TIGR03723 297 CTDNAAMIAAAGYERLK 313
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-175 2.69e-33

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: 121.82  E-value: 2.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   3 DKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHFDIKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiekgq 78
Cdd:cd24133   165 DKVAKLLGL-GYP------GGPAIDKLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKtavlNYLEKNKQDGIEQ------- 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  79 ilsSAADIAATVQHTMACHLVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCT 158
Cdd:cd24133   231 ---NKADIAASFQEAVVDVLVEKTLRA---AKETGI----KRLVVA-GGVAANSRLREKLEEAAEKRGLEVYIPPPELCT 299

                         170
                  ....*....|....*..
gi 1774222090 159 DNGIMIAWNGIERLRAG 175
Cdd:cd24133   300 DNAAMIAAAGYYRYKRG 316
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 1-166 7.28e-28

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: 106.31  E-value: 7.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGnrfHFDIKPPLhhaKNCDFSFTGLQHVTDKIImkkekeegiekgQIL 80
Cdd:pfam00814 140 AFDKVARLLGL-PYP------GGPKIEKLAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLI------------EKK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSAADIAATVQHTMACHLVKRTHRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:pfam00814 195 EPKEDIAASFQEAVFDHLAEKTERALKLPGAKEL--------VILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDN 266


                  ....*.
gi 1774222090 161 GIMIAW 166
Cdd:pfam00814 267 GAMIAW 272
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 1-165 2.59e-25

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: 100.12  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQG--NRFHFDIkpPLHHAKNCDFSFTGL----QHVTDKIIMKKEKEEGi 74
Cdd:TIGR00329 162 AFDKVARLLGL-GYP------GGPKIEELAKKGdaLPFYFPL--PYTVKPMLDFSFSGLktaaRRKIEKLGKNLNEATK- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  75 ekgqilssaADIAATVQHTMACHLVKRTHRAIlfcKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPP 154
Cdd:TIGR00329 232 ---------EDIAYSFQETAFDHLIEKTKRAL---KDTNP----KELVLV-GGVSANKRLREKLETLCQELNVEFYYPPL 294

                         170
                  ....*....|.
gi 1774222090 155 RLCTDNGIMIA 165
Cdd:TIGR00329 295 EFCSDNGAMIA 305
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 2-174 2.73e-20

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: 86.77  E-value: 2.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLiKHPecstmsGGKAIEHLAKQGNRfhfDIKPPlHHAKNCDFSFTGLQhvtdKIIMKKEKEEGIEKGQIls 81
Cdd:cd24031   159 LDKFARELGL-DYP------GGPLIEKMAAQGKK---LVELP-YTVKGMDFSFSGLL----TAAARTYRDGGTDEQTR-- 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  82 saADIAATVQHTMACHLVKRTHRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNG 161
Cdd:cd24031   222 --EDIAYSFQETVFDMLVEKTERALAHTNKKEV--------VLVGGVSANNRLREMLATMCEKRGGEFFYPPPEFCTDNG 291

                         170
                  ....*....|...
gi 1774222090 162 IMIAWNGIERLRA 174
Cdd:cd24031   292 AMIAYAGLEMFKA 304
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 1-175 8.15e-18

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: 80.01  E-value: 8.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHfdikpPLHHA-KNCDFSFTGLqhVTDKIimkkekeegiekgQI 79
Cdd:cd24131   159 ALDKFAREVGL-GHP------GGPKIEKLAEKGKKYV-----ELPYTvKGMDLSFSGL--LTAAL-------------RA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  80 LSSAA---DIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRL 156
Cdd:cd24131   212 YKSGArleDVCYSLQETAFAMLVEVTERALAHTGKDEVL------LV--GGVAANNRLREMLREMCEERGAKFYVPPPEL 283

                         170
                  ....*....|....*....
gi 1774222090 157 CTDNGIMIAWNGIERLRAG 175
Cdd:cd24131   284 CGDNGAMIAWTGLLMYKHG 302
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 1-175 3.52e-16

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: 75.16  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSlIKHPecstmsGGKAIEHLAKQGNRFhfdIKPPlHHAKNCDFSFTGLQHVTDKIIMKKEkeegiekgqil 80
Cdd:cd24096   158 CLDQFARELG-LPFP------GGPKIEKLAEKGKKL---IDLP-YTVKGMDVSFSGLLTAAERAYKSGY----------- 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 sSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:cd24096   216 -RKEDLCYSLQETAFAMLVEITERALAHTGKDEVL------LV--GGVAANNRLREMLKAMCEDRGIKFFVPPKEYCGDN 286

                         170
                  ....*....|....*
gi 1774222090 161 GIMIAWNGIERLRAG 175
Cdd:cd24096   287 GAMIAWTGLLMYKAG 301
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 2-174 3.58e-16

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: 75.40  E-value: 3.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLikhpecSTMsGGKAIEHLAKQGNRFHFDIKPPLHHAKNCDFSFTGLQHVTDKIIMKKEKEEgiekgqilS 81
Cdd:cd24097   164 FDKTAKLLGL------DYP-GGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDE--------Q 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  82 SAADIAATVQHTMACHLVKRTHRAilfckqrdLLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNG 161
Cdd:cd24097   229 TRADIARAFEDAVVDTLMIKCKRA--------LDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNG 300

                         170
                  ....*....|...
gi 1774222090 162 IMIAWNGIERLRA 174
Cdd:cd24097   301 AMIAYAGMVRFKA 313
PRK14878 PRK14878
UGMP family protein; Provisional
 1-178 1.09e-15

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 74.19  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHfdikpPLHHA-KNCDFSFTGLqhVTDKIIMKKEKEegiekgqi 79
Cdd:PRK14878  155 ALDTFAREVGL-APP------GGPAIEKCAEKGEKYI-----ELPYVvKGQDLSFSGL--LTAALRLYKGKE-------- 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  80 lsSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTD 159
Cdd:PRK14878  213 --RLEDVCYSLRETAFAMLVEVTERALAHTGKKEVL------LV--GGVAANRRLREKLEIMAEDRGAKFYVVPPEYAGD 282

                         170
                  ....*....|....*....
gi 1774222090 160 NGIMIAWNGIERLRAGLGI 178
Cdd:PRK14878  283 NGAMIAYTGLLAYKHGVTI 301
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 1-175 1.20e-15

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: 73.83  E-value: 1.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFHfdikpPLHHA-KNCDFSFTGLqhvtdkiimkkekeegiekgqi 79
Cdd:TIGR03722 156 ALDKFAREVGL-GHP------GGPKIEELAEKGKEYI-----ELPYTvKGMDLSFSGL---------------------- 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  80 LSSA----------ADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTL 149
Cdd:TIGR03722 202 LTAAlraykkgarlEDVCYSLQETAFAMLVEVTERALAHTGKKEVL------LV--GGVAANRRLREMLELMAEDRGAKF 273

                         170       180
                  ....*....|....*....|....*.
gi 1774222090 150 LCPPPRLCTDNGIMIAWNGIERLRAG 175
Cdd:TIGR03722 274 YVPPPEYAGDNGAMIAYTGLLMYKHG 299
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 2-175 7.16e-14

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 69.30  E-value: 7.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLIKHPecstmSGGKAIEHLAKQGNRFhfdIKPPlHHAKNCDFSFTGLQHVTDKII---MKKEKEEGIEKGQ 78
Cdd:PTZ00340  161 LDRFARLLNLSNDP-----APGYNIEQLAKKGKNL---IELP-YVVKGMDMSFSGILTYIEDLVehpQFKDVVSEIVPPE 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  79 ILSSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCT 158
Cdd:PTZ00340  232 EEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVL------IV--GGVGCNLRLQEMMQQMAKERGGKLFAMDERYCI 303

                         170
                  ....*....|....*..
gi 1774222090 159 DNGIMIAWNGIERLRAG 175
Cdd:PTZ00340  304 DNGAMIAYAGLLEYLSG 320
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
1-175 1.45e-13

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 68.76  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   1 MLDKVARRLSLiKHPecstmsGGKAIEHLAKQGNRFhfdIKPPlHHAKNCDFSFTGlqhvtdkiimkkekeegiekgqIL 80
Cdd:PRK09605  159 ALDKFARHVGL-PHP------GGPKIEKLAKDGKKY---IDLP-YVVKGMDFSFSG----------------------LL 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 SSA----------ADIAATVQHTMACHLVKRTHRAILfckqrdlLPQNNAVLVAsGGVASNFYIRRALEILTNATQCTLL 150
Cdd:PRK09605  206 TAAkraydageplEDVCYSLQETAFAMLTEVTERALA-------HTGKDEVLLV-GGVAANNRLREMLKEMCEERGADFY 277

                         170       180
                  ....*....|....*....|....*
gi 1774222090 151 CPPPRLCTDNGIMIAWNGIERLRAG 175
Cdd:PRK09605  278 VPEPRFCGDNGAMIAWLGLLMYKAG 302
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 2-175 2.01e-13

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: 67.57  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090   2 LDKVARRLSLIKHPecstmSGGKAIEHLAKQGNRFHfdikpPLHHA-KNCDFSFTGLQHVTDKIIMKKEKEEGIekgqil 80
Cdd:cd24132   160 LDRFARVLKLSNDP-----SPGYNIEQLAKKGKKLI-----ELPYTvKGMDVSFSGILSYIEKLAKKKLKKGEC------ 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222090  81 sSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDN 160
Cdd:cd24132   224 -TPEDLCFSLQETVFAMLVEITERAMAHCGSKEVL------IV--GGVGCNLRLQEMMGIMAEERGGKLFATDERYCIDN 294

                         170
                  ....*....|....*
gi 1774222090 161 GIMIAWNGIERLRAG 175
Cdd:cd24132   295 GAMIAQAGLLMFRSG 309
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 122-169 3.73e-06

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: 45.52  E-value: 3.73e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1774222090 122 LVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGI 169
Cdd:cd24001   139 LVLVGGVSANNRLREKLATMCEKRGDKFFVPPGEFCIDNGAMIAYAGL 186
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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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