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Conserved domains on  [gi|1774222153|ref|NP_001363024|]
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tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial isoform 3 [Homo sapiens]

Protein Classification

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 ...
 1-226 3.06e-112

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: 326.01  E-value: 3.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNK-VEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLikHPECSTMSGGKAIE 79
Cdd:cd24134   110 MEAHALTARLTEEpVEFPFLVLLVSGGHCLLVLARGVGDYTILGTTLDDAPGEAFDKVARLLGL--KPLCDGLSGGAALE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQILSSAADIAATVQHTMACHLVKRTHRAI 158
Cdd:cd24134   188 ALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSLPERADIAASFQHAAVRHLEDRLRRAL 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774222153 159 LFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRA 226
Cdd:cd24134   266 KYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNGVMIAWAGIERLRA 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) ...
 1-226 3.06e-112

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: 326.01  E-value: 3.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNK-VEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLikHPECSTMSGGKAIE 79
Cdd:cd24134   110 MEAHALTARLTEEpVEFPFLVLLVSGGHCLLVLARGVGDYTILGTTLDDAPGEAFDKVARLLGL--KPLCDGLSGGAALE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQILSSAADIAATVQHTMACHLVKRTHRAI 158
Cdd:cd24134   188 ALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSLPERADIAASFQHAAVRHLEDRLRRAL 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774222153 159 LFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRA 226
Cdd:cd24134   266 KYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNGVMIAWAGIERLRA 330
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 1-225 5.65e-59

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: 189.56  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:TIGR03723 110 LEGHLLAPFLEKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAAGEAFDKVARLLGL-GYP------GGPAIDR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGNRFHFDIKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRTHR 156
Cdd:TIGR03723 183 LAKQGDPKAFKFPRPMLDRPGLDFSFSGLKtavlNLIEKLKQKGEEL----------TKADIAASFQAAVVDVLVEKTKR 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222153 157 AilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLR 225
Cdd:TIGR03723 253 A---LKKTGL----KTLVVA-GGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGYERLK 313
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-228 2.22e-58

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: 188.68  E-value: 2.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLT-NKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIE 79
Cdd:COG0533   112 LEGHLLAPFLEdPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDDAAGEAFDKVAKLLGL-GYP------GGPAID 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKPPLHHAKNCDFSFTGL-----QHVtDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRT 154
Cdd:COG0533   185 KLAKEGDPKAFRFPRPMLDRPGLDFSFSGLktavlNYI-EKLKQKGEEQ----------DKADIAASFQEAVVDVLVEKT 253

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222153 155 HRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGL 228
Cdd:COG0533   254 RRALKETGVKRL--------VVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGE 319
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-228 4.30e-58

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 187.97  E-value: 4.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:PRK09604  112 LEGHLLAPFLEEEPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDDAAGEAFDKVAKLLGL-GYP------GGPAIDK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGN--RFHFdikPPLHHAKNCDFSFTGL---------QHVTDKiimkkekeegiekgqilssaADIAATVQHTMACH 149
Cdd:PRK09604  185 LAKQGDpdAFKF---PRPMDRPGLDFSFSGLktavlntieKSEQTK--------------------ADIAASFQAAVVDV 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222153 150 LVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGL 228
Cdd:PRK09604  242 LVIKTKRA---LKQTGV----KTLVVA-GGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGYERLKAGE 312
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 1-218 1.99e-47

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: 158.70  E-value: 1.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPfLVLLISGGHCLLALVQGvSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:pfam00814  90 LEAHALAARLETGLEFP-VVLLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVARLLGL-PYP------GGPKIEK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGnrfHFDIKPPLhhaKNCDFSFTGLQHVTDKIImkkekeegiekgQILSSAADIAATVQHTMACHLVKRTHRAILF 160
Cdd:pfam00814 161 LAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLI------------EKKEPKEDIAASFQEAVFDHLAEKTERALKL 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774222153 161 CKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAW 218
Cdd:pfam00814 223 PGAKEL--------VILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 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) ...
 1-226 3.06e-112

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: 326.01  E-value: 3.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNK-VEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLikHPECSTMSGGKAIE 79
Cdd:cd24134   110 MEAHALTARLTEEpVEFPFLVLLVSGGHCLLVLARGVGDYTILGTTLDDAPGEAFDKVARLLGL--KPLCDGLSGGAALE 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKP-PLHHAKNCDFSFTGLQHVTDKIIMKKEKEEGIEkgQILSSAADIAATVQHTMACHLVKRTHRAI 158
Cdd:cd24134   188 ALAKEGDPAAFKPFPvPMSKRKDCDFSFSGLKTAVRRLIEKLEKEEGVG--LSLPERADIAASFQHAAVRHLEDRLRRAL 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774222153 159 LFCKQrdlLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRA 226
Cdd:cd24134   266 KYCRE---LPPEPKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNGVMIAWAGIERLRA 330
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 1-225 5.65e-59

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: 189.56  E-value: 5.65e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:TIGR03723 110 LEGHLLAPFLEKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAAGEAFDKVARLLGL-GYP------GGPAIDR 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGNRFHFDIKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRTHR 156
Cdd:TIGR03723 183 LAKQGDPKAFKFPRPMLDRPGLDFSFSGLKtavlNLIEKLKQKGEEL----------TKADIAASFQAAVVDVLVEKTKR 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222153 157 AilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLR 225
Cdd:TIGR03723 253 A---LKKTGL----KTLVVA-GGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGYERLK 313
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-228 2.22e-58

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: 188.68  E-value: 2.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLT-NKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIE 79
Cdd:COG0533   112 LEGHLLAPFLEdPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDDAAGEAFDKVAKLLGL-GYP------GGPAID 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKPPLHHAKNCDFSFTGL-----QHVtDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRT 154
Cdd:COG0533   185 KLAKEGDPKAFRFPRPMLDRPGLDFSFSGLktavlNYI-EKLKQKGEEQ----------DKADIAASFQEAVVDVLVEKT 253

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222153 155 HRAILFCKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGL 228
Cdd:COG0533   254 RRALKETGVKRL--------VVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGE 319
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-228 4.30e-58

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 187.97  E-value: 4.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:PRK09604  112 LEGHLLAPFLEEEPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDDAAGEAFDKVAKLLGL-GYP------GGPAIDK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGN--RFHFdikPPLHHAKNCDFSFTGL---------QHVTDKiimkkekeegiekgqilssaADIAATVQHTMACH 149
Cdd:PRK09604  185 LAKQGDpdAFKF---PRPMDRPGLDFSFSGLktavlntieKSEQTK--------------------ADIAASFQAAVVDV 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222153 150 LVKRTHRAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGL 228
Cdd:PRK09604  242 LVIKTKRA---LKQTGV----KTLVVA-GGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGYERLKAGE 312
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 1-227 9.64e-56

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: 181.91  E-value: 9.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTN-KVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIE 79
Cdd:cd24133   110 LEGHILAPFLEDpPPEFPFLALLVSGGHTQLVLVKDFGRYELLGETRDDAAGEAFDKVAKLLGL-GYP------GGPAID 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKPPLHHAKNCDFSFTGLQ----HVTDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRTH 155
Cdd:cd24133   183 KLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKtavlNYLEKNKQDGIEQ----------NKADIAASFQEAVVDVLVEKTL 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774222153 156 RAilfCKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:cd24133   253 RA---AKETGI----KRLVVA-GGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDNAAMIAAAGYYRYKRG 316
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 1-218 1.99e-47

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: 158.70  E-value: 1.99e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKVEFPfLVLLISGGHCLLALVQGvSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:pfam00814  90 LEAHALAARLETGLEFP-VVLLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVARLLGL-PYP------GGPKIEK 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGnrfHFDIKPPLhhaKNCDFSFTGLQHVTDKIImkkekeegiekgQILSSAADIAATVQHTMACHLVKRTHRAILF 160
Cdd:pfam00814 161 LAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLI------------EKKEPKEDIAASFQEAVFDHLAEKTERALKL 222

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1774222153 161 CKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAW 218
Cdd:pfam00814 223 PGAKEL--------VILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 272
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 1-217 2.65e-44

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: 151.74  E-value: 2.65e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRL-TNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIE 79
Cdd:TIGR00329 109 LLGHIYIPRLdTNIPQFPFVSLLVSGGHTQIILVKGIGDYEVLGETLDDAVGEAFDKVARLLGL-GYP------GGPKIE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQG--NRFHFDIkpPLHHAKNCDFSFTGL----QHVTDKIIMKKEKEEGiekgqilssaADIAATVQHTMACHLVKR 153
Cdd:TIGR00329 182 ELAKKGdaLPFYFPL--PYTVKPMLDFSFSGLktaaRRKIEKLGKNLNEATK----------EDIAYSFQETAFDHLIEK 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222153 154 THRAIlfcKQRDLlpqnNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIA 217
Cdd:TIGR00329 250 TKRAL---KDTNP----KELVLV-GGVSANKRLREKLETLCQELNVEFYYPPLEFCSDNGAMIA 305
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 1-226 1.70e-35

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: 128.94  E-value: 1.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKV-EFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLikhpecSTMsGGKAIE 79
Cdd:cd24097   110 MEGHLLAPMLEDNPpEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGL------DYP-GGPLLS 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  80 HLAKQGNRFHFDIKPPLHHAKNCDFSFTGLQHVTDKIIMKKEKEEgiekgqilSSAADIAATVQHTMACHLVKRTHRAil 159
Cdd:cd24097   183 KMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDE--------QTRADIARAFEDAVVDTLMIKCKRA-- 252

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774222153 160 fckqrdLLPQNNAVLVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRA 226
Cdd:cd24097   253 ------LDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKA 313
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 1-226 3.66e-34

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: 125.29  E-value: 3.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHALTIRLTNKvEFPFLVLLISGGHCLLALVQGvSDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEH 80
Cdd:cd24031   108 CIGHLEIPKLNTP-AFPPVALYVSGGNTQVIAYTG-GRYRVFGETIDIAVGNALDKFARELGL-DYP------GGPLIEK 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGNRfhfDIKPPlHHAKNCDFSFTGLQhvtdKIIMKKEKEEGIEKGQIlssaADIAATVQHTMACHLVKRTHRAILF 160
Cdd:cd24031   179 MAAQGKK---LVELP-YTVKGMDFSFSGLL----TAAARTYRDGGTDEQTR----EDIAYSFQETVFDMLVEKTERALAH 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222153 161 CKQRDLlpqnnavlVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRA 226
Cdd:cd24031   247 TNKKEV--------VLVGGVSANNRLREMLATMCEKRGGEFFYPPPEFCTDNGAMIAYAGLEMFKA 304
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 3-227 7.24e-25

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: 100.81  E-value: 7.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   3 AHALTIRLTNKVEFPfLVLLISGGHC-LLALVQGvsDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEHL 81
Cdd:cd24131   111 AHIEIGRLTTGAKDP-VTLYVSGGNTqVIAYVNG--RYRVFGETLDIGIGNALDKFAREVGL-GHP------GGPKIEKL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  82 AKQGNRFHfdikpPLHHA-KNCDFSFTGLqhvtdkiimkkekeeGIEKGQILSSAA---DIAATVQHTMACHLVKRTHRA 157
Cdd:cd24131   181 AEKGKKYV-----ELPYTvKGMDLSFSGL---------------LTAALRAYKSGArleDVCYSLQETAFAMLVEVTERA 240

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153 158 ILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:cd24131   241 LAHTGKDEVL------LV--GGVAANNRLREMLREMCEERGAKFYVPPPELCGDNGAMIAWTGLLMYKHG 302
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 3-227 1.43e-24

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: 99.43  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   3 AHALTIRLTNKVEFPfLVLLISGGHC-LLALVQGvsDFLLLGKSLDIAPGDMLDKVARRLSlIKHPecstmsGGKAIEHL 81
Cdd:cd24096   110 AHIEIGKLTTGAKDP-VVLYVSGGNTqVIAYVGK--RYRVFGETLDIGIGNCLDQFARELG-LPFP------GGPKIEKL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  82 AKQGNRFhfdIKPPlHHAKNCDFSFTGLQHVTDKIIMKKEkeegiekgqilsSAADIAATVQHTMACHLVKRTHRAILFC 161
Cdd:cd24096   180 AEKGKKL---IDLP-YTVKGMDVSFSGLLTAAERAYKSGY------------RKEDLCYSLQETAFAMLVEITERALAHT 243

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222153 162 KQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:cd24096   244 GKDEVL------LV--GGVAANNRLREMLKAMCEDRGIKFFVPPKEYCGDNGAMIAWTGLLMYKAG 301
PRK14878 PRK14878
UGMP family protein; Provisional
 3-230 1.25e-23

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 97.30  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   3 AHALTIRLTNKVEFPfLVLLISGGHCL-LALVQGvsDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEHL 81
Cdd:PRK14878  107 AHIEIGRLTTGAKDP-VVLYVSGGNTQvLAFRGG--RYRVFGETLDIAIGNALDTFAREVGL-APP------GGPAIEKC 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  82 AKQGNRFHfdikpPLHHA-KNCDFSFTGLqhVTDKIIMKKEKEegiekgqilsSAADIAATVQHTMACHLVKRTHRAILF 160
Cdd:PRK14878  177 AEKGEKYI-----ELPYVvKGQDLSFSGL--LTAALRLYKGKE----------RLEDVCYSLRETAFAMLVEVTERALAH 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153 161 CKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAGLGI 230
Cdd:PRK14878  240 TGKKEVL------LV--GGVAANRRLREKLEIMAEDRGAKFYVVPPEYAGDNGAMIAYTGLLAYKHGVTI 301
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 3-227 6.13e-23

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: 95.40  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   3 AHALTIRLTNKVEFPfLVLLISGGHC-LLALVQGvsDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAIEHL 81
Cdd:TIGR03722 108 AHIEIGRLTTGAKDP-VVLYVSGGNTqVIAYRNG--RYRVFGETLDIGLGNALDKFAREVGL-GHP------GGPKIEEL 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  82 AKQGNRFHfdikpPLHHA-KNCDFSFTGLqhvtdkiimkkekeegiekgqiLSSA----------ADIAATVQHTMACHL 150
Cdd:TIGR03722 178 AEKGKEYI-----ELPYTvKGMDLSFSGL----------------------LTAAlraykkgarlEDVCYSLQETAFAML 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774222153 151 VKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:TIGR03722 231 VEVTERALAHTGKKEVL------LV--GGVAANRRLREMLELMAEDRGAKFYVPPPEYAGDNGAMIAYTGLLMYKHG 299
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 3-227 1.42e-19

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 86.63  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   3 AHALTIRLTNKVEFPfLVLLISGGHcllALVQGVSD--FLLLGKSLDIAPGDMLDKVARRLSLIKHPecstmSGGKAIEH 80
Cdd:PTZ00340  112 AHIEMGRLVTGAENP-VVLYVSGGN---TQVIAYSEhrYRIFGETIDIAVGNCLDRFARLLNLSNDP-----APGYNIEQ 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  81 LAKQGNRFhfdIKPPlHHAKNCDFSFTGLQHVTDKII---MKKEKEEGIEKGQILSSAADIAATVQHTMACHLVKRTHRA 157
Cdd:PTZ00340  183 LAKKGKNL---IELP-YVVKGMDMSFSGILTYIEDLVehpQFKDVVSEIVPPEEEFFTDDLCFSLQETIFAMLVEVTERA 258

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153 158 ILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:PTZ00340  259 MSHCGSNEVL------IV--GGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSG 320
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
1-227 1.27e-18

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 84.94  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153   1 MEAHaLTI-RLTNKVEFPfLVLLISGGHC-LLALVQGvsDFLLLGKSLDIAPGDMLDKVARRLSLiKHPecstmsGGKAI 78
Cdd:PRK09605  109 CVAH-VEIgRLTTGAEDP-VTLYVSGGNTqVLAYLNG--RYRVFGETLDIGVGNALDKFARHVGL-PHP------GGPKI 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  79 EHLAKQGNRFhfdIKPPlHHAKNCDFSFTGlqhvtdkiimkkekeegiekgqILSSA----------ADIAATVQHTMAC 148
Cdd:PRK09605  178 EKLAKDGKKY---IDLP-YVVKGMDFSFSG----------------------LLTAAkraydageplEDVCYSLQETAFA 231

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222153 149 HLVKRTHRAILfckqrdlLPQNNAVLVAsGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:PRK09605  232 MLTEVTERALA-------HTGKDEVLLV-GGVAANNRLREMLKEMCEERGADFYVPEPRFCGDNGAMIAWLGLLMYKAG 302
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 43-227 2.38e-17

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: 79.89  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153  43 GKSLDIAPGDMLDKVARRLSLIKHPecstmSGGKAIEHLAKQGNRFHfdikpPLHHA-KNCDFSFTGLQHVTDKIIMKKE 121
Cdd:cd24132   149 GETIDIAVGNCLDRFARVLKLSNDP-----SPGYNIEQLAKKGKKLI-----ELPYTvKGMDVSFSGILSYIEKLAKKKL 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222153 122 KEEGIekgqilsSAADIAATVQHTMACHLVKRTHRAILFCKQRDLLpqnnavLVasGGVASNFYIRRALEILTNATQCTL 201
Cdd:cd24132   219 KKGEC-------TPEDLCFSLQETVFAMLVEITERAMAHCGSKEVL------IV--GGVGCNLRLQEMMGIMAEERGGKL 283

                         170       180
                  ....*....|....*....|....*.
gi 1774222153 202 LCPPPRLCTDNGIMIAWNGIERLRAG 227
Cdd:cd24132   284 FATDERYCIDNGAMIAQAGLLMFRSG 309
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 174-221 8.58e-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: 45.14  E-value: 8.58e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1774222153 174 LVASGGVASNFYIRRALEILTNATQCTLLCPPPRLCTDNGIMIAWNGI 221
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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