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Conserved domains on  [gi|13358864|dbj|BAB33172|]
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O-sialoglycoprotein endopeptidase [Homo sapiens]

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: 709.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:cd24132   2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132  82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132 162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13358864 243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAG 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: 709.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:cd24132   2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132  82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132 162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13358864 243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAG 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: 655.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    4 VLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:PTZ00340   3 ALGIEGSANKLGVGIVTsDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGPGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PTZ00340  83 GAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLATG----------ECTPEDLCFS 232
Cdd:PTZ00340 163 RFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDvvseivppeeEFFTDDLCFS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  233 LQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHR 312
Cdd:PTZ00340 243 LQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSGGF 322

                        330       340
                 ....*....|....*....|...
gi 13358864  313 TPLSDSGVTQRYRTDEVEVTWRD 335
Cdd:PTZ00340 323 TPLKDATVTQRFRTDEVDVTWRD 345
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 5-333 5.79e-153

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: 432.07  E-value: 5.79e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864     5 LGFEGSANKIGVGVV-RDGKVLANPRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMG 83
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVdEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    84 APLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDR 163
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   164 FARVLKIsndPSPG-YNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedVAHRMLATGEcTPEDLCFSLQETVFAMLV 242
Cdd:TIGR03722 160 FAREVGL---GHPGgPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT----AALRAYKKGA-RLEDVCYSLQETAFAMLV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHRTPLSDSGVTQ 322
Cdd:TIGR03722 232 EVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYAGDNGAMIAYTGLLMYKHGVTIPVEESRVRQ 311

                         330
                  ....*....|.
gi 13358864   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 1.06e-112

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: 328.19  E-value: 1.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    23 KVLAN---PRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMGAPLVSVAVVARTVAQL 99
Cdd:pfam00814   1 EILANvilSQKDLHAPYG-GVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   100 WNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPgyN 179
Cdd:pfam00814  80 LNKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--K 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   180 IEQMAKRGKklVELPYTVKGMDVSFSGILSFIEDVAHRmlatgECTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALI 259
Cdd:pfam00814 158 IEKLAKEGA--FEFPRPVKGMDFSFSGLKTAVLRLIEK-----KEPKEDIAASFQEAVFDHLAEKTERALKLPGAKELVI 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 13358864   260 VGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIA 300
Cdd:pfam00814 231 LGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 4-316 2.13e-73

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: 229.90  E-value: 2.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDG-KVLANPRRT-------YvtppGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIA 75
Cdd:COG0533   3 ILGIETSCDETAAAVVDDGrGLLSNVVASqidlharY----G-GVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  76 YTKGPG-MGAPLVSVAVvARTVAQLWNKPLVGVNHCIGHIEMGRLITGATS-PTV-LYVSGGNTQVIAYSEH-RYRIFGE 151
Cdd:COG0533  78 VTAGPGlIGALLVGVSF-AKALALALGKPLIGVNHLEGHLLAPFLEDPPPEfPFLaLLVSGGHTQLVLVKGVgDYELLGE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 152 TIDIAVGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELP---YTVKGMDVSFSGI----LSFIEDvaHRMLATG 222
Cdd:COG0533 157 TIDDAAGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpKAFRFPrpmLDRPGLDFSFSGLktavLNYIEK--LKQKGEE 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 223 EcTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQA 302
Cdd:COG0533 232 Q-DKADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAA 310

                       330
                ....*....|....
gi 13358864 303 GWEMFRAGHRTPLS 316
Cdd:COG0533 311 GYERLKAGEFSDLD 324
 
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: 709.70  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:cd24132   2 ALGIEGSANKLGVGIVRsDGEILSNPRHTYITPPGQGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKGPGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24132  82 GAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVVLYVSGGNTQVIAYSEKRYRIFGETIDIAVGNCLD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLATGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24132 162 RFARVLKLSNDPSPGYNIEQLAKKGKKLIELPYTVKGMDVSFSGILSYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLV 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13358864 243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAG 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: 655.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    4 VLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:PTZ00340   3 ALGIEGSANKLGVGIVTsDGEILSNVRETYITPPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKGPGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PTZ00340  83 GAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  163 RFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLATG----------ECTPEDLCFS 232
Cdd:PTZ00340 163 RFARLLNLSNDPAPGYNIEQLAKKGKNLIELPYVVKGMDMSFSGILTYIEDLVEHPQFKDvvseivppeeEFFTDDLCFS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  233 LQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHR 312
Cdd:PTZ00340 243 LQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAMIAYAGLLEYLSGGF 322

                        330       340
                 ....*....|....*....|...
gi 13358864  313 TPLSDSGVTQRYRTDEVEVTWRD 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: 532.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   3 AVLGFEGSANKIGVGVVR-DGKVLANPRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPG 81
Cdd:cd24096   1 ICLGIEGTAHTFGVGIVDsDGKVLANVRDMYTPPKG-GIHPREAADHHAEVFDKLLSEALEEAGVTINDIDLIAFSQGPG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  82 MGAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCL 161
Cdd:cd24096  80 LGPSLRVTATVARTLAVLLNKPIIGVNHCIAHIEIGKLTTGAKDPVVLYVSGGNTQVIAYVGKRYRVFGETLDIGIGNCL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 162 DRFARVLKISndPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMlatgeCTPEDLCFSLQETVFAML 241
Cdd:cd24096 160 DQFARELGLP--FPGGPKIEKLAEKGKKLIDLPYTVKGMDVSFSGLLTAAERAYKSG-----YRKEDLCYSLQETAFAML 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13358864 242 VEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAG 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 0e+00

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: 515.11  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVV-RDGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:cd24031   1 VLGIEGSADKTGVGIVdDEGKVLANQLDTYVTPKAGGIVPEEAARHHARKIVPLIQEALKESGLTAKDIDLIAYTQGPGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24031  81 GGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKLNTPAFPPVALYVSGGNTQVIAYTGGRYRVFGETIDIAVGNALD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 163 RFARVLKIsnDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAHRMLaTGECTPEDLCFSLQETVFAMLV 242
Cdd:cd24031 161 KFARELGL--DYPGGPLIEKMAAQGKKLVELPYTVKGMDFSFSGLLTAAARTYRDGG-TDEQTREDIAYSFQETVFDMLV 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13358864 243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRA 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 8.20e-156

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: 439.40  E-value: 8.20e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVV-RDGKVLANPRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:cd24131   3 VLGIEGTAHTFGVGIVdSEGEVLANVTDTYVPEKG-GIHPREAAEHHSEVAPELIKKALEEAGVSLNDIDLIAFSQGPGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:cd24131  82 GPCLRVVATAARALALKLDKPLVGVNHCIAHIEIGRLTTGAKDPVTLYVSGGNTQVIAYVNGRYRVFGETLDIGIGNALD 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 163 RFARVLKIsndPSPGY-NIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedVAHRMLATGEcTPEDLCFSLQETVFAML 241
Cdd:cd24131 162 KFAREVGL---GHPGGpKIEKLAEKGKKYVELPYTVKGMDLSFSGLLT----AALRAYKSGA-RLEDVCYSLQETAFAML 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 242 VEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHRTPLSDSGVT 321
Cdd:cd24131 234 VEVTERALAHTGKDEVLLVGGVAANNRLREMLREMCEERGAKFYVPPPELCGDNGAMIAWTGLLMYKHGIRMSLEETIVR 313

                       330
                ....*....|
gi 13358864 322 QRYRTDEVEV 331
Cdd:cd24131 314 PRFRTDEVDV 323
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
4-335 3.96e-155

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 445.49  E-value: 3.96e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    4 VLGFEGSANKIGVGVV-RDGKVLANPRRTYVtPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGM 82
Cdd:PRK09605   3 VLGIEGTAWKTSAGIVdSDGDVLFNESDPYK-PPSGGIHPREAAEHHAEAIPKVIKEALEEAGLKPEDIDLVAFSQGPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   83 GAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLD 162
Cdd:PRK09605  82 GPCLRVVATAARALALSLDVPLIGVNHCVAHVEIGRLTTGAEDPVTLYVSGGNTQVLAYLNGRYRVFGETLDIGVGNALD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  163 RFARVLKIsndPSP-GYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedVAHRMLATGEcTPEDLCFSLQETVFAML 241
Cdd:PRK09605 162 KFARHVGL---PHPgGPKIEKLAKDGKKYIDLPYVVKGMDFSFSGLLT----AAKRAYDAGE-PLEDVCYSLQETAFAML 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  242 VEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHRTPLSDSGVT 321
Cdd:PRK09605 234 TEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEERGADFYVPEPRFCGDNGAMIAWLGLLMYKAGDTLDIEDTRVN 313

                        330
                 ....*....|....
gi 13358864  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 5.79e-153

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: 432.07  E-value: 5.79e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864     5 LGFEGSANKIGVGVV-RDGKVLANPRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMG 83
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVdEDGEILANVSDTYVPEKG-GIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPGLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    84 APLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDR 163
Cdd:TIGR03722  80 PCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDPVVLYVSGGNTQVIAYRNGRYRVFGETLDIGLGNALDK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   164 FARVLKIsndPSPG-YNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedVAHRMLATGEcTPEDLCFSLQETVFAMLV 242
Cdd:TIGR03722 160 FAREVGL---GHPGgPKIEELAEKGKEYIELPYTVKGMDLSFSGLLT----AALRAYKKGA-RLEDVCYSLQETAFAMLV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   243 EITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHRTPLSDSGVTQ 322
Cdd:TIGR03722 232 EVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYAGDNGAMIAYTGLLMYKHGVTIPVEESRVRQ 311

                         330
                  ....*....|.
gi 13358864   323 RYRTDEVEVTW 333
Cdd:TIGR03722 312 RWRTDEVEVPW 322
PRK14878 PRK14878
UGMP family protein; Provisional
 5-335 1.33e-150

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 426.26  E-value: 1.33e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    5 LGFEGSANKIGVGVVRDGKVLANPRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMGA 84
Cdd:PRK14878   1 LGIESTAHTLGVGIVKEDKVLANVRDTYVPEKG-GIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPGLGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   85 PLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDRF 164
Cdd:PRK14878  80 ALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTTGAKDPVVLYVSGGNTQVLAFRGGRYRVFGETLDIAIGNALDTF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  165 ARVLKISndPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSfiedvAHRMLATGECTPEDLCFSLQETVFAMLVEI 244
Cdd:PRK14878 160 AREVGLA--PPGGPAIEKCAEKGEKYIELPYVVKGQDLSFSGLLT-----AALRLYKGKERLEDVCYSLRETAFAMLVEV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  245 TERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRAGHRTPLSDSGVTQRY 324
Cdd:PRK14878 233 TERALAHTGKKEVLLVGGVAANRRLREKLEIMAEDRGAKFYVVPPEYAGDNGAMIAYTGLLAYKHGVTIPPEESFVRQRW 312

                        330
                 ....*....|.
gi 13358864  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 1.06e-112

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: 328.19  E-value: 1.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    23 KVLAN---PRRTYVTPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMGAPLVSVAVVARTVAQL 99
Cdd:pfam00814   1 EILANvilSQKDLHAPYG-GVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   100 WNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPgyN 179
Cdd:pfam00814  80 LNKPLVGVNHLEAHALAARLETGLEFPVVLLVSGGHTQVYAAKDGRYEILGETLDDAAGEAFDKVARLLGLPYPGGP--K 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   180 IEQMAKRGKklVELPYTVKGMDVSFSGILSFIEDVAHRmlatgECTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALI 259
Cdd:pfam00814 158 IEKLAKEGA--FEFPRPVKGMDFSFSGLKTAVLRLIEK-----KEPKEDIAASFQEAVFDHLAEKTERALKLPGAKELVI 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 13358864   260 VGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIA 300
Cdd:pfam00814 231 LGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 5-300 3.77e-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: 3.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864     5 LGFEGSANKIGVGVVRD-GKVLANPRRTYVTPPGT--GFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPG 81
Cdd:TIGR00329   1 LGIETSCDDTGVAIVDEeGNVLANIKISQIPLHAKygGVVPEEASRHHAENIPPLLERALIESNVDKSEIDLIAVTRGPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    82 MGAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATS--PTVLYVSGGNTQVIAY-SEHRYRIFGETIDIAVG 158
Cdd:TIGR00329  81 LGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLDTNIPQfpFVSLLVSGGHTQIILVkGIGDYEVLGETLDDAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   159 NCLDRFARVLKIsndPSP-GYNIEQMAKRGKKL---VELPYTVKGM-DVSFSGILSFiedVAHRMLATGECTPE----DL 229
Cdd:TIGR00329 161 EAFDKVARLLGL---GYPgGPKIEELAKKGDALpfyFPLPYTVKPMlDFSFSGLKTA---ARRKIEKLGKNLNEatkeDI 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13358864   230 CFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIA 300
Cdd:TIGR00329 235 AYSFQETAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELNVEFYYPPLEFCSDNGAMIA 305
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 4-316 4.86e-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: 238.92  E-value: 4.86e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDG-KVLANPRRTYV---TPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKG 79
Cdd:cd24133   1 ILGIETSCDETAVAVVDDGgKILSNVVSSQIdlhAKYG-GVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  80 PG-MGAPLVSVAVvARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSP--TVLYVSGGNTQ-VIAYSEHRYRIFGETIDI 155
Cdd:cd24133  80 PGlIGALLVGVSF-AKALAFALNKPLIGVNHLEGHILAPFLEDPPPEFpfLALLVSGGHTQlVLVKDFGRYELLGETRDD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 156 AVGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELPYT---VKGMDVSFSGI----LSFIEDvahRMLATGECTP 226
Cdd:cd24133 159 AAGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpTAFVFPRPmlkRDGYDFSFSGLktavLNYLEK---NKQDGIEQNK 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 227 EDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEM 306
Cdd:cd24133 233 ADIAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDNAAMIAAAGYYR 312

                       330
                ....*....|
gi 13358864 307 FRAGHRTPLS 316
Cdd:cd24133 313 YKRGKFADLD 322
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 4-304 5.84e-74

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: 226.18  E-value: 5.84e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDGKVLANPRRTYVTPPGTGFLPGDtARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGMG 83
Cdd:cd24001   1 VLGIEGSAEDTGVAIVDDGGVLANHFETYVTEKTGGYPPEA-ARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGPGLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  84 APLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLYVSGGNTQVIAYsehryrifgetidiavgncldr 163
Cdd:cd24001  80 GALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKLKTGATRPVALIVSGGNTQVIAY---------------------- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 164 farvlkisndpspgynieqmakrgkklvelpytvkgmdvsfsgilsfiedvahrmlatgectpedlcfslqetvfamlve 243
Cdd:cd24001     --------------------------------------------------------------------------------

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13358864 244 iteramahcgsqEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGW 304
Cdd:cd24001 138 ------------ELVLVGGVSANNRLREKLATMCEKRGDKFFVPPGEFCIDNGAMIAYAGL 186
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 4-316 2.13e-73

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: 229.90  E-value: 2.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDG-KVLANPRRT-------YvtppGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIA 75
Cdd:COG0533   3 ILGIETSCDETAAAVVDDGrGLLSNVVASqidlharY----G-GVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  76 YTKGPG-MGAPLVSVAVvARTVAQLWNKPLVGVNHCIGHIEMGRLITGATS-PTV-LYVSGGNTQVIAYSEH-RYRIFGE 151
Cdd:COG0533  78 VTAGPGlIGALLVGVSF-AKALALALGKPLIGVNHLEGHLLAPFLEDPPPEfPFLaLLVSGGHTQLVLVKGVgDYELLGE 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 152 TIDIAVGNCLDRFARVLKIsndPSP-GYNIEQMAKRGK-KLVELP---YTVKGMDVSFSGI----LSFIEDvaHRMLATG 222
Cdd:COG0533 157 TIDDAAGEAFDKVAKLLGL---GYPgGPAIDKLAKEGDpKAFRFPrpmLDRPGLDFSFSGLktavLNYIEK--LKQKGEE 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 223 EcTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQA 302
Cdd:COG0533 232 Q-DKADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAA 310

                       330
                ....*....|....
gi 13358864 303 GWEMFRAGHRTPLS 316
Cdd:COG0533 311 GYERLKAGEFSDLD 324
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
4-331 1.39e-71

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 225.33  E-value: 1.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    4 VLGFEGSANKIGVGVVRDG-KVLAN-------PRRTYvtppGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIA 75
Cdd:PRK09604   3 ILGIETSCDETSVAVVDDGrGLLSNvvasqidLHARY----G-GVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   76 YTKGPG-MGAPLVSVAVvARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTV-LYVSGGNTQVIAYSEH-RYRIFGET 152
Cdd:PRK09604  78 VTAGPGlVGALLVGVSF-AKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPFLaLLVSGGHTQLVLVKGIgDYELLGET 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  153 IDIAVGNCLDRFARVLKIsndpspGY----NIEQMAKRG-KKLVELP--YTVKGMDVSFSGILSFiedVAhRMLATGECT 225
Cdd:PRK09604 157 LDDAAGEAFDKVAKLLGL------GYpggpAIDKLAKQGdPDAFKFPrpMDRPGLDFSFSGLKTA---VL-NTIEKSEQT 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  226 PEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWE 305
Cdd:PRK09604 227 KADIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGYE 306

                        330       340
                 ....*....|....*....|....*.
gi 13358864  306 MFRAGHRTPLsDSGVTQRYRTDEVEV 331
Cdd:PRK09604 307 RLKAGEFSDL-DLNARPRWPLDELSA 331
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 4-308 2.31e-71

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: 224.23  E-value: 2.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864     4 VLGFEGSANKIGVGVVRDGK-VLANPRRTYV---TPPGtGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKG 79
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKgLLSNVVASQIdlhARYG-GVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864    80 PG-MGAPLVSVaVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTV-LYVSGGNTQ-VIAYSEHRYRIFGETIDIA 156
Cdd:TIGR03723  80 PGlIGALLVGV-SFAKALALALNKPLIGVNHLEGHLLAPFLEKPLEFPFLaLLVSGGHTQlVLVKGVGDYELLGETLDDA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   157 VGNCLDRFARVLKIsndPSP-GYNIEQMAKRG-KKLVELPytvKGM------DVSFSGI----LSFIEDVAHRMlatGEC 224
Cdd:TIGR03723 159 AGEAFDKVARLLGL---GYPgGPAIDRLAKQGdPKAFKFP---RPMldrpglDFSFSGLktavLNLIEKLKQKG---EEL 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   225 TPEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGW 304
Cdd:TIGR03723 230 TKADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGY 309


                  ....
gi 13358864   305 EMFR 308
Cdd:TIGR03723 310 ERLK 313
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 4-309 5.99e-66

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: 210.84  E-value: 5.99e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVR-DGKVLANPRRTY--VTPPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGP 80
Cdd:cd24134   1 VLGIETSCDDTGAAVVDsDGRILGEALASQkeIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  81 GMGAPLvSVAVV-ARTVAQLWNKPLVGVNHCIGHIEMGRLITgaTSPT----VLYVSGGNTQ-VIAYSEHRYRIFGETID 154
Cdd:cd24134  81 GLALCL-RVGLEfAKGLAAAHNKPLIPVHHMEAHALTARLTE--EPVEfpflVLLVSGGHCLlVLARGVGDYTILGTTLD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 155 IAVGNCLDRFARVLKISNDP---SPGYNIEQMAKRGKKLVELPYTV-----KGMDVSFSGILSFIEDVAHRMLATGECTP 226
Cdd:cd24134 158 DAPGEAFDKVARLLGLKPLCdglSGGAALEALAKEGDPAAFKPFPVpmskrKDCDFSFSGLKTAVRRLIEKLEKEEGVGL 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 227 E-----DLCFSLQETVFAMLVEITERAMAHCGSQE----ALIV-GGVGCNVRLQEMMATMCQERGARLFATDERFCIDNG 296
Cdd:cd24134 238 SlperaDIAASFQHAAVRHLEDRLRRALKYCRELPpepkTLVVsGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNG 317

                       330
                ....*....|...
gi 13358864 297 AMIAQAGWEMFRA 309
Cdd:cd24134 318 VMIAWAGIERLRA 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 8.24e-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: 184.03  E-value: 8.24e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDGK-VLANPRRTYVT--PPGTGFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGP 80
Cdd:cd24097   1 VLGIETSCDETGIAIYDDEKgLLANQLYSQVKlhADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864  81 GMGAPLVSVAVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATS-PTV-LYVSGGNTQVIAYSE-HRYRIFGETIDIAV 157
Cdd:cd24097  81 GLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPMLEDNPPEfPFVaLLVSGGHTQLISVTGiGQYELLGESIDDAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864 158 GNCLDRFARVLKIsnDPSPGYNIEQMAKR---GKKLVELPYTVK-GMDVSFSGILSFIEDVAhRMLATGECTPEDLCFSL 233
Cdd:cd24097 161 GEAFDKTAKLLGL--DYPGGPLLSKMAAQgtaGRFVFPRPMTDRpGLDFSFSGLKTFAANTI-RDNGTDEQTRADIARAF 237

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13358864 234 QETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMATMCQERGARLFATDERFCIDNGAMIAQAGWEMFRA 309
Cdd:cd24097 238 EDAVVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKA 313
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 4-108 2.62e-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: 70.76  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864     4 VLGFEGSANKIGVGVVRDGKVLAnpRRTYVTPpgtgflpgdtaRHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGmg 83
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDGKVLA--ERTEPAG-----------RNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGPG-- 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 13358864    84 aplvS-----VAV-VARTVAQLWNKPLVGVN 108
Cdd:TIGR03725  66 ----SftglrIGLaTAKGLALALGIPLVGVS 92
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 4-108 1.36e-13

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: 69.11  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDGKVLAnpRRTYVTPpgtgflpgdtaRHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPGmg 83
Cdd:COG1214   3 ILAIDTSTEACSVALLDDGEVLA--EREENDG-----------RGHSERLLPMIDELLAEAGLTLSDLDAIAVGIGPG-- 67

                        90       100       110
                ....*....|....*....|....*....|.
gi 13358864  84 aplvS-----VAV-VARTVAQLWNKPLVGVN 108
Cdd:COG1214  68 ----SftglrIGVaTAKGLALALGIPLVGVS 94
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 4-108 9.81e-13

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: 66.15  E-value: 9.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13358864   4 VLGFEGSANKIGVGVVRDGKVLAnprrtyvtppgtgFLPGDTARHHRAVILDLLQEALTESGLTSQDIDCIAYTKGPG-- 81
Cdd:cd24032   1 ILAIDTSTSACSVALLKGGKILA-------------EYELDLGRRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGPGsf 67

                        90       100       110
                ....*....|....*....|....*....|.
gi 13358864  82 ----MGaplVSvavVARTVAQLWNKPLVGVN 108
Cdd:cd24032  68 tglrIG---LA---TAKGLALALGIPLVGVS 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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