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Conserved domains on  [gi|149033627|gb|EDL88425|]
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O-sialoglycoprotein endopeptidase, isoform CRA_b [Rattus norvegicus]

Protein Classification

tRNA N6-adenosine threonylcarbamoyltransferase( domain architecture ID 19235180)

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
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
4-310 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: 705.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:cd24132    2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132   82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132  162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149033627 243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAG 310
Cdd:cd24132  242 EITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATDERYCIDNGAMIAQAGLLMFRSG 309
 
Name Accession Description Interval E-value
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
4-310 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: 705.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:cd24132    2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132   82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132  162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149033627 243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAG 310
Cdd:cd24132  242 EITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATDERYCIDNGAMIAQAGLLMFRSG 309
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
4-335 0e+00

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 653.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:PTZ00340   3 ALGIEGSANKLGVGIVTsDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGPGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PTZ00340  83 GAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLATG----------ECTPEDLCFS 232
Cdd:PTZ00340 163 RFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDvvseivppeeEFFTDDLCFS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 233 LQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHR 312
Cdd:PTZ00340 243 LQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSGGF 322
                        330       340
                 ....*....|....*....|...
gi 149033627 313 TPLQDSGITQRYRTDEVEVTWRD 335
Cdd:PTZ00340 323 TPLKDATVTQRFRTDEVDVTWRD 345
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
5-333 1.02e-155

universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274747  Cd Length: 322  Bit Score: 439.00  E-value: 1.02e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627    5 LGFEGSANKIGVGVV-RDGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMG 83
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVdEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   84 APLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLDR 163
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  164 FARVLKIsndPSPG-YNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedAAQRMLATGEcTPEDLCFSLQETVFAMLV 242
Cdd:TIGR03722 160 FAREVGL---GHPGgPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT----AALRAYKKGA-RLEDVCYSLQETAFAMLV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLQDSGITQ 322
Cdd:TIGR03722 232 EVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYAGDNGAMIAYTGLLMYKHGVTIPVEESRVRQ 311
                         330
                  ....*....|.
gi 149033627  323 RYRTDEVEVTW 333
Cdd:TIGR03722 312 RWRTDEVEVPW 322
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
23-300 1.00e-113

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: 330.50  E-value: 1.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   23 TVLAN---PRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMGAPLASVAVVARTVAQL 99
Cdd:pfam00814   1 EILANvilSQKDLHAPYG-GVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  100 WNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPgyN 179
Cdd:pfam00814  80 LNKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--K 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  180 IEQMAKRGKklVELPYTVKGMDVSFSGILSFIEDAAQRmlatgECTPEDLCFSLQETVFAMLVEITERAMAHCGSKEALI 259
Cdd:pfam00814 158 IEKLAKEGA--FEFPRPVKGMDFSFSGLKTAVLRLIEK-----KEPKEDIAASFQEAVFDHLAEKTERALKLPGAKELVI 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 149033627  260 VGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIA 300
Cdd:pfam00814 231 LGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
4-315 1.83e-75

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: 235.29  E-value: 1.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDG-TVLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:COG0533    3 ILGIETSCDETAAAVVDDGrGLLSNVVASQIDlhARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  81 G-MGAPLASVAVvARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVN-PTV-LYVSGGNTQVISYSEH-RYRIFGETIDIA 156
Cdd:COG0533   83 GlIGALLVGVSF-AKALALALGKPLIGVNHLEGHLLAPFLEDPPPEfPFLaLLVSGGHTQLVLVKGVgDYELLGETIDDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 157 VGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELP---YTVKGMDVSFSGI----LSFIEDAAQRMLATgecTPE 227
Cdd:COG0533  162 AGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpKAFRFPrpmLDRPGLDFSFSGLktavLNYIEKLKQKGEEQ---DKA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 228 DLCFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMF 307
Cdd:COG0533  236 DIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERL 315

                 ....*...
gi 149033627 308 QAGHRTPL 315
Cdd:COG0533  316 KAGEFSDL 323
 
Name Accession Description Interval E-value
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
4-310 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: 705.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:cd24132    2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132   82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132  162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149033627 243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAG 310
Cdd:cd24132  242 EITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATDERYCIDNGAMIAQAGLLMFRSG 309
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
4-335 0e+00

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 653.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:PTZ00340   3 ALGIEGSANKLGVGIVTsDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGPGM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PTZ00340  83 GAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLATG----------ECTPEDLCFS 232
Cdd:PTZ00340 163 RFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDvvseivppeeEFFTDDLCFS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 233 LQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHR 312
Cdd:PTZ00340 243 LQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSGGF 322
                        330       340
                 ....*....|....*....|...
gi 149033627 313 TPLQDSGITQRYRTDEVEVTWRD 335
Cdd:PTZ00340 323 TPLKDATVTQRFRTDEVDVTWRD 345
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
3-310 0e+00

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: 516.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   3 AVLGFEGSANKIGVGVVR-DGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPG 81
Cdd:cd24096    1 ICLGIEGTAHTFGVGIVDsDGKVLANVRDMYTPPKG-GIHPREAADHHAEVFDKLLSEALEEAGVTINDIDLIAFSQGPG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  82 MGAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCL 161
Cdd:cd24096   80 LGPSLRVTATVARTLAVLLNKPIIGVNHCIAHIEIGKLTTGAKDPVVLYVSGGNTQVIAYVGKRYRVFGETLDIGIGNCL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 162 DRFARVLKISndPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMlatgeCTPEDLCFSLQETVFAML 241
Cdd:cd24096  160 DQFARELGLP--FPGGPKIEKLAEKGKKLIDLPYTVKGMDVSFSGLLTAAERAYKSG-----YRKEDLCYSLQETAFAML 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149033627 242 VEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAG 310
Cdd:cd24096  233 VEITERALAHTGKDEVLLVGGVAANNRLREMLKAMCEDRGIKFFVPPKEYCGDNGAMIAWTGLLMYKAG 301
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
4-309 3.24e-179

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: 497.77  E-value: 3.24e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVV-RDGTVLANPRRTYVTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:cd24031    1 VLGIEGSADKTGVGIVdDEGKVLANQLDTYVTPKAGGIVPEEAARHHARKIVPLIQEALKESGLTAKDIDLIAYTQGPGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24031   81 GGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKLNTPAFPPVALYVSGGNTQVIAYTGGRYRVFGETIDIAVGNALD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKIsnDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDAAQRMLaTGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24031  161 KFARELGL--DYPGGPLIEKMAAQGKKLVELPYTVKGMDFSFSGLLTAAARTYRDGG-TDEQTREDIAYSFQETVFDMLV 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149033627 243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQA 309
Cdd:cd24031  238 EKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRGGEFFYPPPEFCTDNGAMIAYAGLEMFKA 304
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
4-331 3.36e-157

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: 442.86  E-value: 3.36e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVV-RDGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:cd24131    3 VLGIEGTAHTFGVGIVdSEGEVLANVTDTYVPEKG-GIHPREAAEHHSEVAPELIKKALEEAGVSLNDIDLIAFSQGPGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24131   82 GPCLRVVATAARALALKLDKPLVGVNHCIAHIEIGRLTTGAKDPVTLYVSGGNTQVIAYVNGRYRVFGETLDIGIGNALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKIsndPSPGY-NIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedAAQRMLATGEcTPEDLCFSLQETVFAML 241
Cdd:cd24131  162 KFAREVGL---GHPGGpKIEKLAEKGKKYVELPYTVKGMDLSFSGLLT----AALRAYKSGA-RLEDVCYSLQETAFAML 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 242 VEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLQDSGIT 321
Cdd:cd24131  234 VEVTERALAHTGKDEVLLVGGVAANNRLREMLREMCEERGAKFYVPPPELCGDNGAMIAWTGLLMYKHGIRMSLEETIVR 313
                        330
                 ....*....|
gi 149033627 322 QRYRTDEVEV 331
Cdd:cd24131  314 PRFRTDEVDV 323
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
4-335 3.61e-157

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 450.88  E-value: 3.61e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVV-RDGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGM 82
Cdd:PRK09605   3 VLGIEGTAWKTSAGIVdSDGDVLFNESDPYKPPSG-GIHPREAAEHHAEAIPKVIKEALEEAGLKPEDIDLVAFSQGPGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  83 GAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PRK09605  82 GPCLRVVATAARALALSLDVPLIGVNHCVAHVEIGRLTTGAEDPVTLYVSGGNTQVLAYLNGRYRVFGETLDIGVGNALD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 163 RFARVLKIsndPSP-GYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedAAQRMLATGEcTPEDLCFSLQETVFAML 241
Cdd:PRK09605 162 KFARHVGL---PHPgGPKIEKLAKDGKKYIDLPYVVKGMDFSFSGLLT----AAKRAYDAGE-PLEDVCYSLQETAFAML 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 242 VEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLQDSGIT 321
Cdd:PRK09605 234 TEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEERGADFYVPEPRFCGDNGAMIAWLGLLMYKAGDTLDIEDTRVN 313
                        330
                 ....*....|....
gi 149033627 322 QRYRTDEVEVTWRD 335
Cdd:PRK09605 314 PNFRTDEVEVTWIK 327
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
5-333 1.02e-155

universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274747  Cd Length: 322  Bit Score: 439.00  E-value: 1.02e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627    5 LGFEGSANKIGVGVV-RDGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMG 83
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVdEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   84 APLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLDR 163
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  164 FARVLKIsndPSPG-YNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedAAQRMLATGEcTPEDLCFSLQETVFAMLV 242
Cdd:TIGR03722 160 FAREVGL---GHPGgPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT----AALRAYKKGA-RLEDVCYSLQETAFAMLV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  243 EITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLQDSGITQ 322
Cdd:TIGR03722 232 EVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYAGDNGAMIAYTGLLMYKHGVTIPVEESRVRQ 311
                         330
                  ....*....|.
gi 149033627  323 RYRTDEVEVTW 333
Cdd:TIGR03722 312 RWRTDEVEVPW 322
PRK14878 PRK14878
UGMP family protein; Provisional
5-335 4.95e-152

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 429.73  E-value: 4.95e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   5 LGFEGSANKIGVGVVRDGTVLANPRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMGA 84
Cdd:PRK14878   1 LGIESTAHTLGVGIVKEDKVLANVRDTYVPEKG-GIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPGLGP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  85 PLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLDRF 164
Cdd:PRK14878  80 ALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTTGAKDPVVLYVSGGNTQVLAFRGGRYRVFGETLDIAIGNALDTF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 165 ARVLKISndPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedAAQRmLATGECTPEDLCFSLQETVFAMLVEI 244
Cdd:PRK14878 160 AREVGLA--PPGGPAIEKCAEKGEKYIELPYVVKGQDLSFSGLLT----AALR-LYKGKERLEDVCYSLRETAFAMLVEV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 245 TERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLQDSGITQRY 324
Cdd:PRK14878 233 TERALAHTGKKEVLLVGGVAANRRLREKLEIMAEDRGAKFYVVPPEYAGDNGAMIAYTGLLAYKHGVTIPPEESFVRQRW 312
                        330
                 ....*....|.
gi 149033627 325 RTDEVEVTWRD 335
Cdd:PRK14878 313 RLDEVDVPWRN 323
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
23-300 1.00e-113

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: 330.50  E-value: 1.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   23 TVLAN---PRRTYVTAPGtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMGAPLASVAVVARTVAQL 99
Cdd:pfam00814   1 EILANvilSQKDLHAPYG-GVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  100 WNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPgyN 179
Cdd:pfam00814  80 LNKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--K 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  180 IEQMAKRGKklVELPYTVKGMDVSFSGILSFIEDAAQRmlatgECTPEDLCFSLQETVFAMLVEITERAMAHCGSKEALI 259
Cdd:pfam00814 158 IEKLAKEGA--FEFPRPVKGMDFSFSGLKTAVLRLIEK-----KEPKEDIAASFQEAVFDHLAEKTERALKLPGAKELVI 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 149033627  260 VGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIA 300
Cdd:pfam00814 231 LGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
5-300 3.69e-98

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: 292.34  E-value: 3.69e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627    5 LGFEGSANKIGVGVVRD-GTVLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPG 81
Cdd:TIGR00329   1 LGIETSCDDTGVAIVDEeGNVLANIKISQIPlhAKYGGVVPEEASRHHAENIPPLLERALIESNVDKSEIDLIAVTRGPG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   82 MGAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITG--AVNPTVLYVSGGNTQVISY-SEHRYRIFGETIDIAVG 158
Cdd:TIGR00329  81 LGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLDTNipQFPFVSLLVSGGHTQIILVkGIGDYEVLGETLDDAVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  159 NCLDRFARVLKIsndPSP-GYNIEQMAKRGKKL---VELPYTVKGM-DVSFSGILSF----IEDAAQRMlatGECTPEDL 229
Cdd:TIGR00329 161 EAFDKVARLLGL---GYPgGPKIEELAKKGDALpfyFPLPYTVKPMlDFSFSGLKTAarrkIEKLGKNL---NEATKEDI 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149033627  230 CFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIA 300
Cdd:TIGR00329 235 AYSFQETAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELNVEFYYPPLEFCSDNGAMIA 305
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
4-315 2.38e-77

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: 240.08  E-value: 2.38e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDGT-VLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:cd24133    1 ILGIETSCDETAVAVVDDGGkILSNVVSSQIDlhAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  81 G-MGAPLASVAVvARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNP--TVLYVSGGNTQVISYSEH-RYRIFGETIDIA 156
Cdd:cd24133   81 GlIGALLVGVSF-AKALAFALNKPLIGVNHLEGHILAPFLEDPPPEFpfLALLVSGGHTQLVLVKDFgRYELLGETRDDA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 157 VGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELPYT---VKGMDVSFSGI----LSFIEDAAQRMLatgECTPE 227
Cdd:cd24133  160 AGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpTAFVFPRPmlkRDGYDFSFSGLktavLNYLEKNKQDGI---EQNKA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 228 DLCFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMF 307
Cdd:cd24133  234 DIAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDNAAMIAAAGYYRY 313

                 ....*...
gi 149033627 308 QAGHRTPL 315
Cdd:cd24133  314 KRGKFADL 321
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
4-315 1.83e-75

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: 235.29  E-value: 1.83e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDG-TVLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:COG0533    3 ILGIETSCDETAAAVVDDGrGLLSNVVASQIDlhARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAGP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  81 G-MGAPLASVAVvARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVN-PTV-LYVSGGNTQVISYSEH-RYRIFGETIDIA 156
Cdd:COG0533   83 GlIGALLVGVSF-AKALALALGKPLIGVNHLEGHLLAPFLEDPPPEfPFLaLLVSGGHTQLVLVKGVgDYELLGETIDDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 157 VGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELP---YTVKGMDVSFSGI----LSFIEDAAQRMLATgecTPE 227
Cdd:COG0533  162 AGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpKAFRFPrpmLDRPGLDFSFSGLktavLNYIEKLKQKGEEQ---DKA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 228 DLCFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMF 307
Cdd:COG0533  236 DIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERL 315

                 ....*...
gi 149033627 308 QAGHRTPL 315
Cdd:COG0533  316 KAGEFSDL 323
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
4-308 9.52e-73

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: 227.69  E-value: 9.52e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627    4 VLGFEGSANKIGVGVVRDGT-VLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKgLLSNVVASQIDlhARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   81 G-MGApLASVAVVARTVAQLWNKPLLGVNHCIGHIeMGRLITGAVNP--TVLYVSGGNTQVISYSEH-RYRIFGETIDIA 156
Cdd:TIGR03723  81 GlIGA-LLVGVSFAKALALALNKPLIGVNHLEGHL-LAPFLEKPLEFpfLALLVSGGHTQLVLVKGVgDYELLGETLDDA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  157 VGNCLDRFARVLKIsndPSP-GYNIEQMAKRG-KKLVELPytvKGM------DVSFSGI----LSFIEDAAQRMlatGEC 224
Cdd:TIGR03723 159 AGEAFDKVARLLGL---GYPgGPAIDRLAKQGdPKAFKFP---RPMldrpglDFSFSGLktavLNLIEKLKQKG---EEL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  225 TPEDLCFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGW 304
Cdd:TIGR03723 230 TKADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGY 309

                  ....
gi 149033627  305 EMFQ 308
Cdd:TIGR03723 310 ERLK 313
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
4-331 1.26e-71

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 225.33  E-value: 1.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDG-TVLANprrtyVTAP--------GtGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCI 74
Cdd:PRK09604   3 ILGIETSCDETSVAVVDDGrGLLSN-----VVASqidlharyG-GVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  75 AYTKGPG-MGApLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTV-LYVSGGNTQVISYSEH-RYRIFGE 151
Cdd:PRK09604  77 AVTAGPGlVGA-LLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPFLaLLVSGGHTQLVLVKGIgDYELLGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 152 TIDIAVGNCLDRFARVLKIsndpspGY----NIEQMAKRG-KKLVELP--YTVKGMDVSFSGILSfiedAAQRMLATGEC 224
Cdd:PRK09604 156 TLDDAAGEAFDKVAKLLGL------GYpggpAIDKLAKQGdPDAFKFPrpMDRPGLDFSFSGLKT----AVLNTIEKSEQ 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 225 TPEDLCFSLQETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGW 304
Cdd:PRK09604 226 TKADIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGY 305
                        330       340
                 ....*....|....*....|....*..
gi 149033627 305 EMFQAGHRTPLqDSGITQRYRTDEVEV 331
Cdd:PRK09604 306 ERLKAGEFSDL-DLNARPRWPLDELSA 331
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
4-304 9.80e-69

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: 213.08  E-value: 9.80e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDGTVLANPRRTYVTAPGTGFLPGDtARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMG 83
Cdd:cd24001    1 VLGIEGSAEDTGVAIVDDGGVLANHFETYVTEKTGGYPPEA-ARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGPGLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  84 APLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLYVSGGNTQVISYsehryrifgetidiavgncldr 163
Cdd:cd24001   80 GALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKLKTGATRPVALIVSGGNTQVIAY---------------------- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 164 farvlkisndpspgynieqmakrgkklvelpytvkgmdvsfsgilsfiedaaqrmlatgectpedlcfslqetvfamlve 243
Cdd:cd24001      --------------------------------------------------------------------------------
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149033627 244 iteramahcgskEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGW 304
Cdd:cd24001  138 ------------ELVLVGGVSANNRLREKLATMCEKRGDKFFVPPGEFCIDNGAMIAYAGL 186
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
4-309 4.13e-68

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: 4.13e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVR-DGTVLANPRRTY--VTAPGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:cd24134    1 VLGIETSCDDTGAAVVDsDGRILGEALASQkeIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  81 GMGAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVN-P-TVLYVSGGNTQ-VISYSEHRYRIFGETIDIAV 157
Cdd:cd24134   81 GLALCLRVGLEFAKGLAAAHNKPLIPVHHMEAHALTARLTEEPVEfPfLVLLVSGGHCLlVLARGVGDYTILGTTLDDAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 158 GNCLDRFARVLKISNDP---SPGYNIEQMAKRGKKLVELPYTV-----KGMDVSFSGILSFIEDAAQRMLATGECTPE-- 227
Cdd:cd24134  161 GEAFDKVARLLGLKPLCdglSGGAALEALAKEGDPAAFKPFPVpmskrKDCDFSFSGLKTAVRRLIEKLEKEEGVGLSlp 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 228 ---DLCFSLQETVFAMLVEITERAMAHCGSKE----ALIV-GGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMI 299
Cdd:cd24134  241 eraDIAASFQHAAVRHLEDRLRRALKYCRELPpepkTLVVsGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNGVMI 320
                        330
                 ....*....|
gi 149033627 300 AQAGWEMFQA 309
Cdd:cd24134  321 AWAGIERLRA 330
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
4-309 2.65e-56

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: 185.57  E-value: 2.65e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVV-RDGTVLANPRRTYVT--APGTGFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGP 80
Cdd:cd24097    1 VLGIETSCDETGIAIYdDEKGLLANQLYSQVKlhADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  81 GMGAPLASVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVN-PTV-LYVSGGNTQVISYSE-HRYRIFGETIDIAV 157
Cdd:cd24097   81 GLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPMLEDNPPEfPFVaLLVSGGHTQLISVTGiGQYELLGESIDDAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627 158 GNCLDRFARVLKIsnDPSPGYNIEQMAKR---GKKLVELPYTVK-GMDVSFSGILSFIEDAAqRMLATGECTPEDLCFSL 233
Cdd:cd24097  161 GEAFDKTAKLLGL--DYPGGPLLSKMAAQgtaGRFVFPRPMTDRpGLDFSFSGLKTFAANTI-RDNGTDEQTRADIARAF 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149033627 234 QETVFAMLVEITERAMAHCGSKEALIVGGVGCNVRLQEMMATMCQERGAQLFATDERFCIDNGAMIAQAGWEMFQA 309
Cdd:cd24097  238 EDAVVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKA 313
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
4-108 5.26e-14

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: 69.60  E-value: 5.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627    4 VLGFEGSANKIGVGVVRDGTVLAnpRRTYvtapgtgflpgDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGmg 83
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDGKVLA--ERTE-----------PAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGPG-- 65
                          90       100       110
                  ....*....|....*....|....*....|.
gi 149033627   84 aplaS-----VAV-VARTVAQLWNKPLLGVN 108
Cdd:TIGR03725  66 ----SftglrIGLaTAKGLALALGIPLVGVS 92
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
4-108 6.86e-14

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: 69.61  E-value: 6.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDGTVLAnprrtyvtapgtgFLPGDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPG-- 81
Cdd:cd24032    1 ILAIDTSTSACSVALLKGGKILA-------------EYELDLGRRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGPGsf 67
                         90       100       110
                 ....*....|....*....|....*....|.
gi 149033627  82 ----MGapLAsvavVARTVAQLWNKPLLGVN 108
Cdd:cd24032   68 tglrIG--LA----TAKGLALALGIPLVGVS 92
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
4-108 7.30e-14

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: 69.88  E-value: 7.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627   4 VLGFEGSANKIGVGVVRDGTVLAnpRRTYvtapgtgflpgDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGmg 83
Cdd:COG1214    3 ILAIDTSTEACSVALLDDGEVLA--EREE-----------NDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPG-- 67
                         90       100       110
                 ....*....|....*....|....*....|.
gi 149033627  84 aplaS-----VAV-VARTVAQLWNKPLLGVN 108
Cdd:COG1214   68 ----SftglrIGVaTAKGLALALGIPLVGVS 94
Peptidase_S74_CIMCD cd10144
Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F ...
43-100 1.93e-03

Peptidase S74 family, C-terminal intramolecular chaperone domain of Escherichia coli phage K1F endosialidase and related proteins; This peptidase S74 family includes C-terminal intramolecular chaperone domain (CIMCD) of Escherichia coli phage K1F endosialidase, Bacillus phage GA-1 neck appendage protein, and Bacteriophage T5 L-shaped tail fibre. This domain acts as a molecular chaperone; during virus particle assembly, the CIMCD of phage tailspike proteins induces the homo-trimerization of phage tailspike proteins by chaperoning the formation of a triple beta-helix. Homo-trimeric phage tailspike proteins are then auto-cleaved by the CIMCD domain. This family also includes the peptidase S74 Intramolecular Chaperone Auto-processing (ICA) domain of mammalian Myrf. The ICA domain drives the homo-oligomerization of Myrf in the endoplasmic reticulum (ER) membrane. The homo-oligomeric Myrf is proteolyzed by the ICA domain, releasing its N-terminal fragments from the ER membrane.


Pssm-ID: 381748 [Multi-domain]  Cd Length: 113  Bit Score: 37.30  E-value: 1.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149033627  43 GDTARHHRAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMGAPLASVAVVARTVAQLW 100
Cdd:cd10144   38 GDDARLHFGVIAQEVIAAFEDAGLDAGKYGILCYDEWDAVTDEVITMENVGIEAGERY 95
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
17-94 8.05e-03

Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.


Pssm-ID: 238427 [Multi-domain]  Cd Length: 361  Bit Score: 37.59  E-value: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149033627  17 GVVRDGTVLANPRRTYvtAPGTGFLPGDTARHH------RAVILDLLQEALTEAGLTPKDIDCIAYTKGPGMGAPLASVA 90
Cdd:cd00831   49 GIETRYLVLPGGEETY--APRPEMSPSLDERNDialeeaRELAEEAARGALDEAGLRPSDIDHLVVNTSTGNPTPSLDAM 126

                 ....
gi 149033627  91 VVAR 94
Cdd:cd00831  127 LINR 130
 
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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