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Conserved domains on  [gi|71402413|ref|XP_804123|]
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O-sialoglycoprotein endopeptidase, putative [Trypanosoma cruzi]

Protein Classification

tRNA N6-adenosine threonylcarbamoyltransferase( domain architecture ID 11488418)

tRNA N6-adenosine threonylcarbamoyltransferase is part of the enzyme complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 9-373 0e+00

O-sialoglycoprotein endopeptidase-like protein; Provisional


:

Pssm-ID: 240369  Cd Length: 345  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    9 ILALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:PTZ00340   1 FLALGIEGSANKLGVGIVTSDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   89 GMGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNC 168
Cdd:PTZ00340  81 GMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  169 LDRAARFLGLPNDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKDRDKCSSalassvslstqr 248
Cdd:PTZ00340 161 LDRFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDVVSEIV------------ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  249 rtlpngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDA 328
Cdd:PTZ00340 229 ---------PPEEEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDE 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 71402413  329 RYCIDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSWR 373
Cdd:PTZ00340 300 RYCIDNGAMIAYAGLLEYLSGGFTPLKDATVTQRFRTDEVDVTWR 344
 
Name Accession Description Interval E-value
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 9-373 0e+00

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    9 ILALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:PTZ00340   1 FLALGIEGSANKLGVGIVTSDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   89 GMGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNC 168
Cdd:PTZ00340  81 GMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  169 LDRAARFLGLPNDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKDRDKCSSalassvslstqr 248
Cdd:PTZ00340 161 LDRFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDVVSEIV------------ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  249 rtlpngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDA 328
Cdd:PTZ00340 229 ---------PPEEEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDE 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 71402413  329 RYCIDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSWR 373
Cdd:PTZ00340 300 RYCIDNGAMIAYAGLLEYLSGGFTPLKDATVTQRFRTDEVDVTWR 344
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 10-349 0e+00

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.


Pssm-ID: 466982  Cd Length: 309  Bit Score: 601.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  10 LALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24132   1 IALGIEGSANKLGVGIVRSDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCL 169
Cdd:cd24132  81 MGAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 170 DRAARFLGLPNDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKdrdkcssalassvslstqrr 249
Cdd:cd24132 161 DRFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKK-------------------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 250 tlpngvlcavdEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDAR 329
Cdd:cd24132 221 -----------GECTPEDLCFSLQETVFAMLVEITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATDER 289

                       330       340
                ....*....|....*....|
gi 71402413 330 YCIDNGCMIAYAGLLEYKAG 349
Cdd:cd24132 290 YCIDNGAMIAQAGLLMFRSG 309
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 12-372 1.66e-148

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: 422.44  E-value: 1.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    12 LGIEGSANKIGVGIVDEAGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMG 91
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVDEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    92 APLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDR 171
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   172 AARFLGLPndPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSfmeALLQhpqfkdrdkcssalassvslstqrrtl 251
Cdd:TIGR03722 160 FAREVGLG--HPGGPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT---AALR--------------------------- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   252 pngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYC 331
Cdd:TIGR03722 208 ------AYKKGARLEDVCYSLQETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYA 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 71402413   332 IDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSW 372
Cdd:TIGR03722 282 GDNGAMIAYTGLLMYKHGVTIPVEESRVRQRWRTDEVEVPW 322
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 31-340 1.45e-100

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: 298.53  E-value: 1.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    31 NVLSNERETYIT--PAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMGAPLAVCCTVAKTLSLLW 108
Cdd:pfam00814   1 EILANVILSQKDlhAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   109 SVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDRAARFLGLPNDPAPgyNI 188
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--KI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   189 EQCAKRGRlfIELPYVVKGMDMSFSGLLSFmeallqhpqfkdrdkcssalassvslstqrrtlpngVLCAVDEPFGIDDI 268
Cdd:pfam00814 159 EKLAKEGA--FEFPRPVKGMDFSFSGLKTA------------------------------------VLRLIEKKEPKEDI 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71402413   269 CYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYCIDNGCMIAY 340
Cdd:pfam00814 201 AASFQEAVFDHLAEKTERALKLPGAKELVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 272
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 12-354 8.20e-68

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: 216.80  E-value: 8.20e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEAGNVLSNERETYIT---PAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:COG0533   4 LGIETSCDETAAAVVDDGRGLLSNVVASQIDlhaRYG-GVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  89 G-MGApLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNP--VVLYVSGGNTQVIAYAEH-RYRIFGETIDIA 164
Cdd:COG0533  83 GlIGA-LLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFpfLALLVSGGHTQLVLVKGVgDYELLGETIDDA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 165 VGNCLDRAARFLGLPNdPApGYNIEQCAKRGRL-FIELPyvvKGM------DMSFSGLLSFmeALLQHPQFKDRdkcssa 237
Cdd:COG0533 162 AGEAFDKVAKLLGLGY-PG-GPAIDKLAKEGDPkAFRFP---RPMldrpglDFSFSGLKTA--VLNYIEKLKQK------ 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 238 lassvslstqrrtlpngvlcavDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMAT 317
Cdd:COG0533 229 ----------------------GEEQDKADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAE 286

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71402413 318 SRGGRCFDMDARYCIDNGCMIAYAGLLEYKAGGFTSL 354
Cdd:COG0533 287 KRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEFSDL 323
 
Name Accession Description Interval E-value
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 9-373 0e+00

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 699.87  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    9 ILALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:PTZ00340   1 FLALGIEGSANKLGVGIVTSDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   89 GMGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNC 168
Cdd:PTZ00340  81 GMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  169 LDRAARFLGLPNDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKDRDKCSSalassvslstqr 248
Cdd:PTZ00340 161 LDRFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDVVSEIV------------ 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  249 rtlpngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDA 328
Cdd:PTZ00340 229 ---------PPEEEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDE 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 71402413  329 RYCIDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSWR 373
Cdd:PTZ00340 300 RYCIDNGAMIAYAGLLEYLSGGFTPLKDATVTQRFRTDEVDVTWR 344
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 10-349 0e+00

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.


Pssm-ID: 466982  Cd Length: 309  Bit Score: 601.45  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  10 LALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24132   1 IALGIEGSANKLGVGIVRSDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCL 169
Cdd:cd24132  81 MGAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 170 DRAARFLGLPNDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKdrdkcssalassvslstqrr 249
Cdd:cd24132 161 DRFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKK-------------------- 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 250 tlpngvlcavdEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDAR 329
Cdd:cd24132 221 -----------GECTPEDLCFSLQETVFAMLVEITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATDER 289

                       330       340
                ....*....|....*....|
gi 71402413 330 YCIDNGCMIAYAGLLEYKAG 349
Cdd:cd24132 290 YCIDNGAMIAQAGLLMFRSG 309
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 10-370 4.01e-149

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: 423.99  E-value: 4.01e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  10 LALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24131   2 IVLGIEGTAHTFGVGIVDSEGEVLANVTDTYVPEKG-GIHPREAAEHHSEVAPELIKKALEEAGVSLNDIDLIAFSQGPG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCL 169
Cdd:cd24131  81 LGPCLRVVATAARALALKLDKPLVGVNHCIAHIEIGRLTTGAKDPVTLYVSGGNTQVIAYVNGRYRVFGETLDIGIGNAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 170 DRAARFLGLpndPAPGY-NIEQCAKRGRLFIELPYVVKGMDMSFSGLLSfmeALLQhpqfkdrdkcssalassvslstqr 248
Cdd:cd24131 161 DKFAREVGL---GHPGGpKIEKLAEKGKKYVELPYTVKGMDLSFSGLLT---AALR------------------------ 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 249 rtlpngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDA 328
Cdd:cd24131 211 ---------AYKSGARLEDVCYSLQETAFAMLVEVTERALAHTGKDEVLLVGGVAANNRLREMLREMCEERGAKFYVPPP 281

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 71402413 329 RYCIDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNV 370
Cdd:cd24131 282 ELCGDNGAMIAWTGLLMYKHGIRMSLEETIVRPRFRTDEVDV 323
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 12-372 1.66e-148

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: 422.44  E-value: 1.66e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    12 LGIEGSANKIGVGIVDEAGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMG 91
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVDEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    92 APLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDR 171
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   172 AARFLGLPndPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSfmeALLQhpqfkdrdkcssalassvslstqrrtl 251
Cdd:TIGR03722 160 FAREVGLG--HPGGPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT---AALR--------------------------- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   252 pngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYC 331
Cdd:TIGR03722 208 ------AYKKGARLEDVCYSLQETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYA 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 71402413   332 IDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSW 372
Cdd:TIGR03722 282 GDNGAMIAYTGLLMYKHGVTIPVEESRVRQRWRTDEVEVPW 322
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 10-349 4.82e-148

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: 420.30  E-value: 4.82e-148
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  10 LALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24096   1 ICLGIEGTAHTFGVGIVDSDGKVLANVRDMYTPPKG-GIHPREAADHHAEVFDKLLSEALEEAGVTINDIDLIAFSQGPG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCL 169
Cdd:cd24096  80 LGPSLRVTATVARTLAVLLNKPIIGVNHCIAHIEIGKLTTGAKDPVVLYVSGGNTQVIAYVGKRYRVFGETLDIGIGNCL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 170 DRAARFLGLPndPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEAllqhpqfkdrdkcssalassvslstqrr 249
Cdd:cd24096 160 DQFARELGLP--FPGGPKIEKLAEKGKKLIDLPYTVKGMDVSFSGLLTAAER---------------------------- 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 250 tlpngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDAR 329
Cdd:cd24096 210 --------AYKSGYRKEDLCYSLQETAFAMLVEITERALAHTGKDEVLLVGGVAANNRLREMLKAMCEDRGIKFFVPPKE 281

                       330       340
                ....*....|....*....|
gi 71402413 330 YCIDNGCMIAYAGLLEYKAG 349
Cdd:cd24096 282 YCGDNGAMIAWTGLLMYKAG 301
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
12-373 1.81e-146

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 425.07  E-value: 1.81e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   12 LGIEGSANKIGVGIVDEAGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMG 91
Cdd:PRK09605   4 LGIEGTAWKTSAGIVDSDGDVLFNESDPYKPPSG-GIHPREAAEHHAEAIPKVIKEALEEAGLKPEDIDLVAFSQGPGLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   92 APLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDR 171
Cdd:PRK09605  83 PCLRVVATAARALALSLDVPLIGVNHCVAHVEIGRLTTGAEDPVTLYVSGGNTQVLAYLNGRYRVFGETLDIGVGNALDK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  172 AARFLGLPNDPAPgyNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSfmeALLQhpqfkdrdkcssalassvslstqrrtl 251
Cdd:PRK09605 163 FARHVGLPHPGGP--KIEKLAKDGKKYIDLPYVVKGMDFSFSGLLT---AAKR--------------------------- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  252 pngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYC 331
Cdd:PRK09605 211 ------AYDAGEPLEDVCYSLQETAFAMLTEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEERGADFYVPEPRFC 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 71402413  332 IDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSWR 373
Cdd:PRK09605 285 GDNGAMIAWLGLLMYKAGDTLDIEDTRVNPNFRTDEVEVTWI 326
PRK14878 PRK14878
UGMP family protein; Provisional
 12-373 1.65e-142

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 407.00  E-value: 1.65e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   12 LGIEGSANKIGVGIVDEaGNVLSNERETYITPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMG 91
Cdd:PRK14878   1 LGIESTAHTLGVGIVKE-DKVLANVRDTYVPEKG-GIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPGLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   92 APLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDR 171
Cdd:PRK14878  79 PALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTTGAKDPVVLYVSGGNTQVLAFRGGRYRVFGETLDIAIGNALDT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  172 AARFLGLPndPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSfmeALLQhpqfkdrdkcssalassvslstqrrtl 251
Cdd:PRK14878 159 FAREVGLA--PPGGPAIEKCAEKGEKYIELPYVVKGQDLSFSGLLT---AALR--------------------------- 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  252 pngvlcAVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYC 331
Cdd:PRK14878 207 ------LYKGKERLEDVCYSLRETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREKLEIMAEDRGAKFYVVPPEYA 280

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 71402413  332 IDNGCMIAYAGLLEYKAGGFTSLPNATITQRFRTDEVNVSWR 373
Cdd:PRK14878 281 GDNGAMIAYTGLLAYKHGVTIPPEESFVRQRWRLDEVDVPWR 322
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 11-348 3.85e-136

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: 390.30  E-value: 3.85e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  11 ALGIEGSANKIGVGIVDEAGNVLSNERETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGM 90
Cdd:cd24031   1 VLGIEGSADKTGVGIVDDEGKVLANQLDTYVTPKAGGIVPEEAARHHARKIVPLIQEALKESGLTAKDIDLIAYTQGPGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  91 GAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLD 170
Cdd:cd24031  81 GGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKLNTPAFPPVALYVSGGNTQVIAYTGGRYRVFGETIDIAVGNALD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 171 RAARFLGLpnDPAPGYNIEQCAKRGRLFIELPYVVKGMDMSFSGLLSFMEALLQHPQFKDRDkcssalassvslstqrrt 250
Cdd:cd24031 161 KFARELGL--DYPGGPLIEKMAAQGKKLVELPYTVKGMDFSFSGLLTAAARTYRDGGTDEQT------------------ 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 251 lpngvlcavdepfgIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARY 330
Cdd:cd24031 221 --------------REDIAYSFQETVFDMLVEKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRGGEFFYPPPEF 286

                       330
                ....*....|....*...
gi 71402413 331 CIDNGCMIAYAGLLEYKA 348
Cdd:cd24031 287 CTDNGAMIAYAGLEMFKA 304
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 31-340 1.45e-100

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: 298.53  E-value: 1.45e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    31 NVLSNERETYIT--PAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGMGAPLAVCCTVAKTLSLLW 108
Cdd:pfam00814   1 EILANVILSQKDlhAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   109 SVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAYAEHRYRIFGETIDIAVGNCLDRAARFLGLPNDPAPgyNI 188
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--KI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   189 EQCAKRGRlfIELPYVVKGMDMSFSGLLSFmeallqhpqfkdrdkcssalassvslstqrrtlpngVLCAVDEPFGIDDI 268
Cdd:pfam00814 159 EKLAKEGA--FEFPRPVKGMDFSFSGLKTA------------------------------------VLRLIEKKEPKEDI 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71402413   269 CYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGRCFDMDARYCIDNGCMIAY 340
Cdd:pfam00814 201 AASFQEAVFDHLAEKTERALKLPGAKELVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 272
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 12-339 2.60e-97

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: 291.57  E-value: 2.60e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    12 LGIEGSANKIGVGIVDEAGNVLSNERETYITPAGT--GFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:TIGR00329   1 LGIETSCDDTGVAIVDEEGNVLANIKISQIPLHAKygGVVPEEASRHHAENIPPLLERALIESNVDKSEIDLIAVTRGPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNN--PVVLYVSGGNTQVIAYAE-HRYRIFGETIDIAVG 166
Cdd:TIGR00329  81 LGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLDTNIPQfpFVSLLVSGGHTQIILVKGiGDYEVLGETLDDAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   167 NCLDRAARFLGLPNdPApGYNIEQCAKRG---RLFIELPYVVKGM-DMSFSGLLSFMEALLQhpQFKDRDkcssalassv 242
Cdd:TIGR00329 161 EAFDKVARLLGLGY-PG-GPKIEELAKKGdalPFYFPLPYTVKPMlDFSFSGLKTAARRKIE--KLGKNL---------- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   243 slstQRRTlpngvlcavdepfgIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRGGR 322
Cdd:TIGR00329 227 ----NEAT--------------KEDIAYSFQETAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELNVE 288

                         330
                  ....*....|....*..
gi 71402413   323 CFDMDARYCIDNGCMIA 339
Cdd:TIGR00329 289 FYYPPLEFCSDNGAMIA 305
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 12-354 3.86e-70

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: 222.74  E-value: 3.86e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEAGNVLSNERETYI---TPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:cd24133   2 LGIETSCDETAVAVVDDGGKILSNVVSSQIdlhAKYG-GVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  89 G-MGApLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNP--VVLYVSGGNTQ-VIAYAEHRYRIFGETIDIA 164
Cdd:cd24133  81 GlIGA-LLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLEDPPPEFpfLALLVSGGHTQlVLVKDFGRYELLGETRDDA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 165 VGNCLDRAARFLGLPNdPApGYNIEQCAKRG-RLFIELPYV---VKGMDMSFSGL-LSFMEALLQHPQfkdrdkcssala 239
Cdd:cd24133 160 AGEAFDKVAKLLGLGY-PG-GPAIDKLAKEGdPTAFVFPRPmlkRDGYDFSFSGLkTAVLNYLEKNKQ------------ 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 240 ssvslstqrrtlpngvlcaVDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSR 319
Cdd:cd24133 226 -------------------DGIEQNKADIAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKR 286

                       330       340       350
                ....*....|....*....|....*....|....*
gi 71402413 320 GGRCFDMDARYCIDNGCMIAYAGLLEYKAGGFTSL 354
Cdd:cd24133 287 GLEVYIPPPELCTDNAAMIAAAGYYRYKRGKFADL 321
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 12-354 8.20e-68

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: 216.80  E-value: 8.20e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEAGNVLSNERETYIT---PAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:COG0533   4 LGIETSCDETAAAVVDDGRGLLSNVVASQIDlhaRYG-GVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAGP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  89 G-MGApLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNP--VVLYVSGGNTQVIAYAEH-RYRIFGETIDIA 164
Cdd:COG0533  83 GlIGA-LLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFpfLALLVSGGHTQLVLVKGVgDYELLGETIDDA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 165 VGNCLDRAARFLGLPNdPApGYNIEQCAKRGRL-FIELPyvvKGM------DMSFSGLLSFmeALLQHPQFKDRdkcssa 237
Cdd:COG0533 162 AGEAFDKVAKLLGLGY-PG-GPAIDKLAKEGDPkAFRFP---RPMldrpglDFSFSGLKTA--VLNYIEKLKQK------ 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 238 lassvslstqrrtlpngvlcavDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMAT 317
Cdd:COG0533 229 ----------------------GEEQDKADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAE 286

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 71402413 318 SRGGRCFDMDARYCIDNGCMIAYAGLLEYKAGGFTSL 354
Cdd:COG0533 287 KRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEFSDL 323
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 12-348 1.27e-67

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: 216.23  E-value: 1.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEAGNVLSNER--ETYITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24134   2 LGIETSCDDTGAAVVDSDGRILGEALasQKEIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGPG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVtgsNNPV-----VLYVSGGNTQvIAYAE--HRYRIFGETID 162
Cdd:cd24134  82 LALCLRVGLEFAKGLAAAHNKPLIPVHHMEAHALTARLT---EEPVefpflVLLVSGGHCL-LVLARgvGDYTILGTTLD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 163 IAVGNCLDRAARFLGLPNDP---APGYNIEQCAKRG--RLFIELP---YVVKGMDMSFSGLLSFMEALLQHPQFKDRdkc 234
Cdd:cd24134 158 DAPGEAFDKVARLLGLKPLCdglSGGAALEALAKEGdpAAFKPFPvpmSKRKDCDFSFSGLKTAVRRLIEKLEKEEG--- 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 235 ssalassvslstqrrtlpngvlCAVDEPFgIDDICYSLQETIFAVLAEVTERAMSQC----ESNEVLIV-GGVGCNLRLQ 309
Cdd:cd24134 235 ----------------------VGLSLPE-RADIAASFQHAAVRHLEDRLRRALKYCrelpPEPKTLVVsGGVASNQYLR 291

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 71402413 310 EMMRQMATSRGGRCFDMDARYCIDNGCMIAYAGLLEYKA 348
Cdd:cd24134 292 KRLETLAEEHGLQLVCPPPRLCTDNGVMIAWAGIERLRA 330
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 12-347 1.98e-64

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: 207.66  E-value: 1.98e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    12 LGIEGSANKIGVGIVDEAGNVLSNERETYI---TPAGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:TIGR03723   2 LGIETSCDETAVAIVDDGKGLLSNVVASQIdlhARYG-GVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413    89 G-MGApLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVvtgSNNP----VVLYVSGGNTQ-VIAYAEHRYRIFGETID 162
Cdd:TIGR03723  81 GlIGA-LLVGVSFAKALALALNKPLIGVNHLEGHLLAPFL---EKPLefpfLALLVSGGHTQlVLVKGVGDYELLGETLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   163 IAVGNCLDRAARFLGLPNdPApGYNIEQCAKRGRL-FIELPyvvKGM------DMSFSGLLSFmeALLQHPQFKDRdkcs 235
Cdd:TIGR03723 157 DAAGEAFDKVARLLGLGY-PG-GPAIDRLAKQGDPkAFKFP---RPMldrpglDFSFSGLKTA--VLNLIEKLKQK---- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   236 salassvslstqrrtlpngvlcavDEPFGIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQM 315
Cdd:TIGR03723 226 ------------------------GEELTKADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEEL 281

                         330       340       350
                  ....*....|....*....|....*....|..
gi 71402413   316 ATSRGGRCFDMDARYCIDNGCMIAYAGLLEYK 347
Cdd:TIGR03723 282 AEKRGLEVFFPPLELCTDNAAMIAAAGYERLK 313
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
12-354 7.57e-64

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 206.46  E-value: 7.57e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   12 LGIEGSANKIGVGIVDEAGNVLSN-------ERETYitpaGtGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICY 84
Cdd:PRK09604   4 LGIETSCDETSVAVVDDGRGLLSNvvasqidLHARY----G-GVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIAV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   85 TKGPG-MGApLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNP-VVLYVSGGNTQVIAYAEH-RYRIFGETI 161
Cdd:PRK09604  79 TAGPGlVGA-LLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPfLALLVSGGHTQLVLVKGIgDYELLGETL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  162 DIAVGNCLDRAARFLGLPNdPApGYNIEQCAKRGRL-FIELP--YVVKGMDMSFSGLLSfmeALLQHPQFKDRDKCssal 238
Cdd:PRK09604 158 DDAAGEAFDKVAKLLGLGY-PG-GPAIDKLAKQGDPdAFKFPrpMDRPGLDFSFSGLKT---AVLNTIEKSEQTKA---- 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  239 assvslstqrrtlpngvlcavdepfgidDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATS 318
Cdd:PRK09604 229 ----------------------------DIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKK 280

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 71402413  319 RGGRCFDMDARYCIDNGCMIAYAGLLEYKAGGFTSL 354
Cdd:PRK09604 281 RGIEVFIPPLKLCTDNAAMIAAAGYERLKAGEFSDL 316
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 12-348 1.27e-51

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: 174.40  E-value: 1.27e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEAGNVLSNERETY--ITPAGTGFLPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG 89
Cdd:cd24097   2 LGIETSCDETGIAIYDDEKGLLANQLYSQvkLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGPG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  90 MGAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVvtGSNNP----VVLYVSGGNTQVI-AYAEHRYRIFGETIDIA 164
Cdd:cd24097  82 LVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPML--EDNPPefpfVALLVSGGHTQLIsVTGIGQYELLGESIDDA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 165 VGNCLDRAARFLGLPNDPAPgyNIEQCAKRG---RLFIELPYVVK-GMDMSFSGLLSFMEALLQHPQFKDRDkcssalas 240
Cdd:cd24097 160 AGEAFDKTAKLLGLDYPGGP--LLSKMAAQGtagRFVFPRPMTDRpGLDFSFSGLKTFAANTIRDNGTDEQT-------- 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413 241 svslstqrrtlpngvlcavdepfgIDDICYSLQETIFAVLAEVTERAMSQCESNEVLIVGGVGCNLRLQEMMRQMATSRG 320
Cdd:cd24097 230 ------------------------RADIARAFEDAVVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRR 285

                       330       340
                ....*....|....*....|....*...
gi 71402413 321 GRCFDMDARYCIDNGCMIAYAGLLEYKA 348
Cdd:cd24097 286 GEVFYARPEFCTDNGAMIAYAGMVRFKA 313
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 11-149 3.39e-47

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: 158.77  E-value: 3.39e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  11 ALGIEGSANKIGVGIVDEaGNVLSNERETYITPAGTGFlPRETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPGM 90
Cdd:cd24001   1 VLGIEGSAEDTGVAIVDD-GGVLANHFETYVTEKTGGY-PPEAARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGPGL 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71402413  91 GAPLAVCCTVAKTLSLLWSVPLVGVNHCIGHIEMGRVVTGSNNPVVLYVSGGNTQVIAY 149
Cdd:cd24001  79 GGALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKLKTGATRPVALIVSGGNTQVIAY 137
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 8-116 9.83e-10

tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440827  Cd Length: 227  Bit Score: 57.94  E-value: 9.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413   8 RILAlgIEGSANKIGVGIVDEaGNVLSnERETyitpagtgflprETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKG 87
Cdd:COG1214   2 LILA--IDTSTEACSVALLDD-GEVLA-EREE------------NDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIG 65

                        90       100       110
                ....*....|....*....|....*....|.
gi 71402413  88 PG--MGapLAVCCTVAKTLSLLWSVPLVGVN 116
Cdd:COG1214  66 PGsfTG--LRIGVATAKGLALALGIPLVGVS 94
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 12-116 2.16e-09

nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ) and similar proteins; TsaB, also called t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, it can act as a protease that specifically degrades TsaD in vitro; therefore, TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. TsaB does not show sialoglycoprotease activity against glycophorin A.


Pssm-ID: 466882 [Multi-domain]  Cd Length: 205  Bit Score: 56.90  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413  12 LGIEGSANKIGVGIVDEaGNVLSnERETyitpagtgflprETAQHHTTHILRLAQAAFETAQVRPSDISVICYTKGPG-- 89
Cdd:cd24032   2 LAIDTSTSACSVALLKG-GKILA-EYEL------------DLGRRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGPGsf 67

                        90       100
                ....*....|....*....|....*..
gi 71402413  90 MGapLAVCCTVAKTLSLLWSVPLVGVN 116
Cdd:cd24032  68 TG--LRIGLATAKGLALALGIPLVGVS 92
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 9-116 3.78e-08

tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274750 [Multi-domain]  Cd Length: 204  Bit Score: 53.04  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71402413     9 ILAlgIEGSANKIGVGIVDEaGNVLSneRETYITPAGtgflpretaqhHTTHILRLAQAAFETAQVRPSDISVICYTKGP 88
Cdd:TIGR03725   1 ILA--IDTSTEALSVALLDD-GKVLA--ERTEPAGRN-----------HSERLLPMIEELLAEAGLSLQDLDAIAVGVGP 64

                          90       100       110
                  ....*....|....*....|....*....|
gi 71402413    89 G--MGapLAVCCTVAKTLSLLWSVPLVGVN 116
Cdd:TIGR03725  65 GsfTG--LRIGLATAKGLALALGIPLVGVS 92
 
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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