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Conserved domains on  [gi|1277140750|gb|PIR42122|]
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MAG: tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD [Candidatus Yanofskybacteria bacterium CG10_big_fil_rev_8_21_14_0_10_37_15]

Protein Classification

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD( domain architecture ID 11425234)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-333 0e+00

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: 512.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAIleIKNEKlKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:COG0533     1 MLILGIETSCDETAAAV--VDDGR-GLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTlkDIDAIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWL--PPVtgifnskfliskkEFPILNLIVSGGHTELVL 156
Cdd:COG0533    78 VTAGPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLedPPP-------------EFPFLALLVSGGHTQLVL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 157 MKDHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRD 236
Cdd:COG0533   145 VKGVGDYELLGETIDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 237 LKKQNVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTT 316
Cdd:COG0533   225 LKQKGEEQD---KADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCT 301

                         330
                  ....*....|....*..
gi 1277140750 317 DNAAMIAVAGYFSARGG 333
Cdd:COG0533   302 DNAAMIAAAGYERLKAG 318
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-333 0e+00

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: 512.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAIleIKNEKlKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:COG0533     1 MLILGIETSCDETAAAV--VDDGR-GLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTlkDIDAIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWL--PPVtgifnskfliskkEFPILNLIVSGGHTELVL 156
Cdd:COG0533    78 VTAGPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLedPPP-------------EFPFLALLVSGGHTQLVL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 157 MKDHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRD 236
Cdd:COG0533   145 VKGVGDYELLGETIDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 237 LKKQNVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTT 316
Cdd:COG0533   225 LKQKGEEQD---KADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCT 301

                         330
                  ....*....|....*..
gi 1277140750 317 DNAAMIAVAGYFSARGG 333
Cdd:COG0533   302 DNAAMIAAAGYERLKAG 318
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-328 1.35e-179

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: 500.47  E-value: 1.35e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEiknEKLKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24133     1 ILGIETSCDETAVAVVD---DGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTldDIDAIAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWL--PPVtgifnskfliskkEFPILNLIVSGGHTELVLMK 158
Cdd:cd24133    78 YGPGLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLedPPP-------------EFPFLALLVSGGHTQLVLVK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLK 238
Cdd:cd24133   145 DFGRYELLGETRDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKTAVLNYLEKNK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 KQNVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:cd24133   225 QDGIEQN---KADIAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDN 301

                         330
                  ....*....|
gi 1277140750 319 AAMIAVAGYF 328
Cdd:cd24133   302 AAMIAAAGYY 311
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-333 6.83e-174

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 486.11  E-value: 6.83e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAILEikNEKlKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:PRK09604    1 MLILGIETSCDETSVAVVD--DGR-GLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTleDIDAIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILNLIVSGGHTELVLMK 158
Cdd:PRK09604   78 VTAGPGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAP------------FLEEEPEFPFLALLVSGGHTQLVLVK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMlHSKNFNFSYSGLKTAVLYLLRDlk 238
Cdd:PRK09604  146 GIGDYELLGETLDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKQGDPDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEK-- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 kqnvqiNKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:PRK09604  223 ------SEQTKADIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDN 296

                         330
                  ....*....|....*
gi 1277140750 319 AAMIAVAGYFSARGG 333
Cdd:PRK09604  297 AAMIAAAGYERLKAG 311
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-328 3.66e-173

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: 483.47  E-value: 3.66e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEIKNEklkVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGI--SDIDLISVT 80
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKG---LLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLtlSDIDAIAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILNLIVSGGHTELVLMKDH 160
Cdd:TIGR03723  78 AGPGLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAP------------FLEKPLEFPFLALLVSGGHTQLVLVKGV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 161 GKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLKKQ 240
Cdd:TIGR03723 146 GDYELLGETLDDAAGEAFDKVARLLGLGYPGGPAIDRLAKQGDPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 241 NVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAA 320
Cdd:TIGR03723 226 GEELT---KADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAA 302


                  ....*...
gi 1277140750 321 MIAVAGYF 328
Cdd:TIGR03723 303 MIAAAGYE 310
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 26-323 1.73e-116

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: 338.59  E-value: 1.73e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  26 KVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVTRGPGLGPSLLTGITFAKTIAWLH 103
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSleDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 104 KKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILnLIVSGGHTELVLMKDhGKYQIIGETLDDAAGEAFDKVAR 183
Cdd:pfam00814  81 NKPLVGVNHLEAHALAA------------RLETGLEFPVV-LLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 184 LLELGYPGGPAIAKIAGKGdpqSFNLPRPMlhsKNFNFSYSGLKTAVLYLLRdlkkqnvqiNKKIKADIAASFQEAAIEV 263
Cdd:pfam00814 147 LLGLPYPGGPKIEKLAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLIE---------KKEPKEDIAASFQEAVFDH 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 264 LIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAAMIA 323
Cdd:pfam00814 212 LAEKTERALKLPGAKELVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-333 0e+00

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: 512.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAIleIKNEKlKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:COG0533     1 MLILGIETSCDETAAAV--VDDGR-GLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTlkDIDAIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWL--PPVtgifnskfliskkEFPILNLIVSGGHTELVL 156
Cdd:COG0533    78 VTAGPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLedPPP-------------EFPFLALLVSGGHTQLVL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 157 MKDHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRD 236
Cdd:COG0533   145 VKGVGDYELLGETIDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 237 LKKQNVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTT 316
Cdd:COG0533   225 LKQKGEEQD---KADIAASFQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCT 301

                         330
                  ....*....|....*..
gi 1277140750 317 DNAAMIAVAGYFSARGG 333
Cdd:COG0533   302 DNAAMIAAAGYERLKAG 318
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-328 1.35e-179

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: 500.47  E-value: 1.35e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEiknEKLKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24133     1 ILGIETSCDETAVAVVD---DGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTldDIDAIAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWL--PPVtgifnskfliskkEFPILNLIVSGGHTELVLMK 158
Cdd:cd24133    78 YGPGLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLedPPP-------------EFPFLALLVSGGHTQLVLVK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLK 238
Cdd:cd24133   145 DFGRYELLGETRDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKTAVLNYLEKNK 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 KQNVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:cd24133   225 QDGIEQN---KADIAASFQEAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDN 301

                         330
                  ....*....|
gi 1277140750 319 AAMIAVAGYF 328
Cdd:cd24133   302 AAMIAAAGYY 311
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-333 6.83e-174

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 486.11  E-value: 6.83e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAILEikNEKlKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:PRK09604    1 MLILGIETSCDETSVAVVD--DGR-GLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTleDIDAIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILNLIVSGGHTELVLMK 158
Cdd:PRK09604   78 VTAGPGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAP------------FLEEEPEFPFLALLVSGGHTQLVLVK 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMlHSKNFNFSYSGLKTAVLYLLRDlk 238
Cdd:PRK09604  146 GIGDYELLGETLDDAAGEAFDKVAKLLGLGYPGGPAIDKLAKQGDPDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEK-- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 kqnvqiNKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:PRK09604  223 ------SEQTKADIAASFQAAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDN 296

                         330
                  ....*....|....*
gi 1277140750 319 AAMIAVAGYFSARGG 333
Cdd:PRK09604  297 AAMIAAAGYERLKAG 311
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-328 3.66e-173

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: 483.47  E-value: 3.66e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEIKNEklkVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGI--SDIDLISVT 80
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKG---LLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLtlSDIDAIAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILNLIVSGGHTELVLMKDH 160
Cdd:TIGR03723  78 AGPGLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAP------------FLEKPLEFPFLALLVSGGHTQLVLVKGV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 161 GKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLKKQ 240
Cdd:TIGR03723 146 GDYELLGETLDDAAGEAFDKVARLLGLGYPGGPAIDRLAKQGDPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 241 NVQINkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAA 320
Cdd:TIGR03723 226 GEELT---KADIAASFQAAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAA 302


                  ....*...
gi 1277140750 321 MIAVAGYF 328
Cdd:TIGR03723 303 MIAAAGYE 310
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 4-323 5.27e-130

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: 374.00  E-value: 5.27e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   4 LGIETSCDDTAMAILeikNEKLKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTG--ISDIDLISVTR 81
Cdd:TIGR00329   1 LGIETSCDDTGVAIV---DEEGNVLANIKISQIPLHAKYGGVVPEEASRHHAENIPPLLERALIESNvdKSEIDLIAVTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  82 GPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSnwlppvtGIFNSKFLiskkEFPILNLIVSGGHTELVLMKDHG 161
Cdd:TIGR00329  78 GPGLGGSLRVGATFARSLALALNKPLIGVNHLLGHIYI-------PRLDTNIP----QFPFVSLLVSGGHTQIILVKGIG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 162 KYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLKKqn 241
Cdd:TIGR00329 147 DYEVLGETLDDAVGEAFDKVARLLGLGYPGGPKIEELAKKGDALPFYFPLPYTVKPMLDFSFSGLKTAARRKIEKLGK-- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 242 vQINKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAAM 321
Cdd:TIGR00329 225 -NLNEATKEDIAYSFQETAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELNVEFYYPPLEFCSDNGAM 303


                  ..
gi 1277140750 322 IA 323
Cdd:TIGR00329 304 IA 305
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 3-326 6.49e-129

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: 372.24  E-value: 6.49e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILeikNEKLKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24134     1 VLGIETSCDDTGAAVV---DSDGRILGEALASQKEIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSlsDLDAVAVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIysnwLPPVtgifnskfLISKK-EFPILNLIVSGGHTELVLMKD 159
Cdd:cd24134    78 VGPGLALCLRVGLEFAKGLAAAHNKPLIPVHHMEAHA----LTAR--------LTEEPvEFPFLVLLVSGGHCLLVLARG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 160 HGKYQIIGETLDDAAGEAFDKVARLLEL-----GYPGGPAIAKIAGKGDPQSFN-LPRPMLHSKNFNFSYSGLKTAVLYL 233
Cdd:cd24134   146 VGDYTILGTTLDDAPGEAFDKVARLLGLkplcdGLSGGAALEALAKEGDPAAFKpFPVPMSKRKDCDFSFSGLKTAVRRL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 234 LRDLKKQ-NVQINKKIKADIAASFQEAAIEVLIQKTKRAVEKYKT-----KHLFLSGGVSANKLLREKIEKEARGLGINF 307
Cdd:cd24134   226 IEKLEKEeGVGLSLPERADIAASFQHAAVRHLEDRLRRALKYCRElppepKTLVVSGGVASNQYLRKRLETLAEEHGLQL 305

                         330
                  ....*....|....*....
gi 1277140750 308 SCPPMEYTTDNAAMIAVAG 326
Cdd:cd24134   306 VCPPPRLCTDNGVMIAWAG 324
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 26-323 1.73e-116

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: 338.59  E-value: 1.73e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  26 KVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVTRGPGLGPSLLTGITFAKTIAWLH 103
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSleDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 104 KKPILGVNHLEGHIYSNwlppvtgifnskFLISKKEFPILnLIVSGGHTELVLMKDhGKYQIIGETLDDAAGEAFDKVAR 183
Cdd:pfam00814  81 NKPLVGVNHLEAHALAA------------RLETGLEFPVV-LLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 184 LLELGYPGGPAIAKIAGKGdpqSFNLPRPMlhsKNFNFSYSGLKTAVLYLLRdlkkqnvqiNKKIKADIAASFQEAAIEV 263
Cdd:pfam00814 147 LLGLPYPGGPKIEKLAKEG---AFEFPRPV---KGMDFSFSGLKTAVLRLIE---------KKEPKEDIAASFQEAVFDH 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 264 LIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAAMIA 323
Cdd:pfam00814 212 LAEKTERALKLPGAKELVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIA 271
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 3-326 9.34e-93

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: 279.56  E-value: 9.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEiknEKLKVLANVVSSQVKIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24097     1 VLGIETSCDETGIAIYD---DEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTakDIDAVAYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIysnwLPPVTGIfnskfliSKKEFPILNLIVSGGHTELVLMKDH 160
Cdd:cd24097    78 AGPGLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHL----LAPMLED-------NPPEFPFVALLVSGGHTQLISVTGI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 161 GKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDPQSFNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLKKQ 240
Cdd:cd24097   147 GQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 241 NVQInkkikADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAA 320
Cdd:cd24097   227 EQTR-----ADIARAFEDAVVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGA 301


                  ....*.
gi 1277140750 321 MIAVAG 326
Cdd:cd24097   302 MIAYAG 307
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 3-326 1.60e-92

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: 278.59  E-value: 1.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEIKNeklKVLANVVSSQVKIHKkfGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24031     1 VLGIEGSADKTGVGIVDDEG---KVLANQLDTYVTPKA--GGIVPEEAARHHARKIVPLIQEALKESGLTakDIDLIAYT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWLPPvtgifnskfliskKEFPILNLIVSGGHTELVLMKDH 160
Cdd:cd24031    76 QGPGLGGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKLNT-------------PAFPPVALYVSGGNTQVIAYTGG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 161 gKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDpqsfNLPRPMLHSKNFNFSYSGLKTAVLYLLRDLKKQ 240
Cdd:cd24031   143 -RYRVFGETIDIAVGNALDKFARELGLDYPGGPLIEKMAAQGK----KLVELPYTVKGMDFSFSGLLTAAARTYRDGGTD 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 241 NVQInkkikADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAA 320
Cdd:cd24031   218 EQTR-----EDIAYSFQETVFDMLVEKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRGGEFFYPPPEFCTDNGA 292


                  ....*.
gi 1277140750 321 MIAVAG 326
Cdd:cd24031   293 MIAYAG 298
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 1-333 1.18e-68

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: 218.29  E-value: 1.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAILEIKNEklkVLANVVSSQVKihkKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:cd24131     1 MIVLGIEGTAHTFGVGIVDSEGE---VLANVTDTYVP---EKGGIHPREAAEHHSEVAPELIKKALEEAGVSlnDIDLIA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYsnwlppvTGIFNSKFliskkEFPILnLIVSGGHTELVLMK 158
Cdd:cd24131    75 FSQGPGLGPCLRVVATAARALALKLDKPLVGVNHCIAHIE-------IGRLTTGA-----KDPVT-LYVSGGNTQVIAYV 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DhGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDpQSFNLPRPMlhsKNFNFSYSGLKTAVLYLLRdlk 238
Cdd:cd24131   142 N-GRYRVFGETLDIGIGNALDKFAREVGLGHPGGPKIEKLAEKGK-KYVELPYTV---KGMDLSFSGLLTAALRAYK--- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 kqnvqiNKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:cd24131   214 ------SGARLEDVCYSLQETAFAMLVEVTERALAHTGKDEVLLVGGVAANNRLREMLREMCEERGAKFYVPPPELCGDN 287

                         330
                  ....*....|....*
gi 1277140750 319 AAMIAVAGYFSARGG 333
Cdd:cd24131   288 GAMIAWTGLLMYKHG 302
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 4-334 4.09e-67

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: 214.04  E-value: 4.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   4 LGIETSCDDTAMAILeikNEKLKVLANVVSSQVKIHkkfGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVTR 81
Cdd:TIGR03722   1 LGIEGTAHTFGVGIV---DEDGEILANVSDTYVPEK---GGIHPREAAEHHAEVAPKLIKEALEEAGVSleDIDAVAFSQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  82 GPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHI-----YSNWLPPVTgifnskfliskkefpilnLIVSGGHTeLVL 156
Cdd:TIGR03722  75 GPGLGPCLRVGATAARALALKLNKPLVGVNHCVAHIeigrlTTGAKDPVV------------------LYVSGGNT-QVI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 157 MKDHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGdpqSFNLPRPMLhSKNFNFSYSGLKTAVLYLLRD 236
Cdd:TIGR03722 136 AYRNGRYRVFGETLDIGLGNALDKFAREVGLGHPGGPKIEELAEKG---KEYIELPYT-VKGMDLSFSGLLTAALRAYKK 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 237 lkkqnvqinKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTT 316
Cdd:TIGR03722 212 ---------GARLEDVCYSLQETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREMLELMAEDRGAKFYVPPPEYAG 282

                         330
                  ....*....|....*...
gi 1277140750 317 DNAAMIAVAGYFSARGGN 334
Cdd:TIGR03722 283 DNGAMIAYTGLLMYKHGV 300
PRK14878 PRK14878
UGMP family protein; Provisional
 4-333 2.38e-63

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 204.38  E-value: 2.38e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   4 LGIETscddTAMAI-LEIKNEKlKVLANVVSSQVKihkKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:PRK14878    1 LGIES----TAHTLgVGIVKED-KVLANVRDTYVP---EKGGIHPREAAQHHAEVAPELLRKALEKAGISieDIDAVAVS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHI-----YSNWLPPVTgifnskfliskkefpilnLIVSGGHTELV 155
Cdd:PRK14878   73 QGPGLGPALRVGATAARALALKYNKPLVPVNHCIAHIeigrlTTGAKDPVV------------------LYVSGGNTQVL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 156 LMKDhGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGdpqSFNLPRPMLhSKNFNFSYSGLKTAVLYLLR 235
Cdd:PRK14878  135 AFRG-GRYRVFGETLDIAIGNALDTFAREVGLAPPGGPAIEKCAEKG---EKYIELPYV-VKGQDLSFSGLLTAALRLYK 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 236 dlkkqnvqiNKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYT 315
Cdd:PRK14878  210 ---------GKERLEDVCYSLRETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREKLEIMAEDRGAKFYVVPPEYA 280

                         330
                  ....*....|....*...
gi 1277140750 316 TDNAAMIAVAGYFSARGG 333
Cdd:PRK14878  281 GDNGAMIAYTGLLAYKHG 298
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 4-333 1.89e-62

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: 201.51  E-value: 1.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   4 LGIETSCDDTAMAILEIKNeklKVLANVVSSQVKihkKFGGVVPFLAAREHTKNISRVFKLTLKKTG--ISDIDLISVTR 81
Cdd:cd24096     3 LGIEGTAHTFGVGIVDSDG---KVLANVRDMYTP---PKGGIHPREAADHHAEVFDKLLSEALEEAGvtINDIDLIAFSQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  82 GPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIysnwlppvtgifNSKFLISKKEFPILnLIVSGGHTElVLMKDHG 161
Cdd:cd24096    77 GPGLGPSLRVTATVARTLAVLLNKPIIGVNHCIAHI------------EIGKLTTGAKDPVV-LYVSGGNTQ-VIAYVGK 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 162 KYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDpQSFNLPRPMlhsKNFNFSYSGLKTAVLYLLRDLKKqn 241
Cdd:cd24096   143 RYRVFGETLDIGIGNCLDQFARELGLPFPGGPKIEKLAEKGK-KLIDLPYTV---KGMDVSFSGLLTAAERAYKSGYR-- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 242 vqinkkiKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDNAAM 321
Cdd:cd24096   217 -------KEDLCYSLQETAFAMLVEITERALAHTGKDEVLLVGGVAANNRLREMLKAMCEDRGIKFFVPPKEYCGDNGAM 289

                         330
                  ....*....|..
gi 1277140750 322 IAVAGYFSARGG 333
Cdd:cd24096   290 IAWTGLLMYKAG 301
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
1-326 2.24e-56

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 192.03  E-value: 2.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAILEiknEKLKVLANVvSSQVKihKKFGGVVPFLAAREHTKNISRVFKLTLKKTGIS--DIDLIS 78
Cdd:PRK09605    1 MIVLGIEGTAWKTSAGIVD---SDGDVLFNE-SDPYK--PPSGGIHPREAAEHHAEAIPKVIKEALEEAGLKpeDIDLVA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  79 VTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYsnwlppvTGIFNSKFliskkEFPILnLIVSGGHTElVLMK 158
Cdd:PRK09605   75 FSQGPGLGPCLRVVATAARALALSLDVPLIGVNHCVAHVE-------IGRLTTGA-----EDPVT-LYVSGGNTQ-VLAY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 159 DHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIAGKGDpQSFNLPRPMlhsKNFNFSYSGLKTAVlyllrdlk 238
Cdd:PRK09605  141 LNGRYRVFGETLDIGVGNALDKFARHVGLPHPGGPKIEKLAKDGK-KYIDLPYVV---KGMDFSFSGLLTAA-------- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 239 KQNVQINKKIkADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTDN 318
Cdd:PRK09605  209 KRAYDAGEPL-EDVCYSLQETAFAMLTEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEERGADFYVPEPRFCGDN 287


                  ....*...
gi 1277140750 319 AAMIAVAG 326
Cdd:PRK09605  288 GAMIAWLG 295
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 3-335 8.84e-51

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 172.53  E-value: 8.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEIKNEklkVLANVVSSQvkIHKKFGGVVPFLAAREHTKNISRVFKLTLKKTGI--SDIDLISVT 80
Cdd:PTZ00340    3 ALGIEGSANKLGVGIVTSDGE---ILSNVRETY--ITPPGTGFLPRETAQHHREHILSLVKEALEEAKItpSDISLICYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWLppVTGIFNskfliskkefPILnLIVSGGHTElVLMKDH 160
Cdd:PTZ00340   78 KGPGMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRL--VTGAEN----------PVV-LYVSGGNTQ-VIAYSE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 161 GKYQIIGETLDDAAGEAFDKVARLLELgyPGGPA----IAKIAGKGDpQSFNLPRPMlhsKNFNFSYSGLKTAVLYLLRd 236
Cdd:PTZ00340  144 HRYRIFGETIDIAVGNCLDRFARLLNL--SNDPApgynIEQLAKKGK-NLIELPYVV---KGMDMSFSGILTYIEDLVE- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 237 lKKQNVQINKKI--------KADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEA--RGlGIn 306
Cdd:PTZ00340  217 -HPQFKDVVSEIvppeeeffTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAkeRG-GK- 293

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1277140750 307 fsCPPME--YTTDNAAMIAVAGYFSARGGNY 335
Cdd:PTZ00340  294 --LFAMDerYCIDNGAMIAYAGLLEYLSGGF 322
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 3-333 3.96e-44

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: 154.24  E-value: 3.96e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILeikNEKLKVLANVvssqvkiHKKF----G-GVVPFLAAREHTKNISRVFKLTLKKTGIS--DID 75
Cdd:cd24132     2 ALGIEGSANKLGVGIV---RSDGEILSNP-------RHTYitppGqGFLPRDTAKHHRAHILDLVKEALKEAGITpsDID 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  76 LISVTRGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWLppVTGIFNskfliskkefPILnLIVSGGHTElV 155
Cdd:cd24132    72 CICYTKGPGMGAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRL--VTGAQN----------PVV-LYVSGGNTQ-V 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 156 LMKDHGKYQIIGETLDDAAGEAFDKVARLLELgyPGGPA----IAKIAGKGDpQSFNLPRPMlhsKNFNFSYSGLktavL 231
Cdd:cd24132   138 IAYSEKRYRIFGETIDIAVGNCLDRFARVLKL--SNDPSpgynIEQLAKKGK-KLIELPYTV---KGMDVSFSGI----L 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 232 YLLRDLKKQNVQINKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPP 311
Cdd:cd24132   208 SYIEKLAKKKLKKGECTPEDLCFSLQETVFAMLVEITERAMAHCGSKEVLIVGGVGCNLRLQEMMGIMAEERGGKLFATD 287

                         330       340
                  ....*....|....*....|..
gi 1277140750 312 MEYTTDNAAMIAVAGYFSARGG 333
Cdd:cd24132   288 ERYCIDNGAMIAQAGLLMFRSG 309
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 3-156 5.53e-30

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: 113.32  E-value: 5.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILeikNEKlKVLANVVSSQVKIHKKFGGVVPflaAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24001     1 VLGIEGSAEDTGVAIV---DDG-GVLANHFETYVTEKTGGYPPEA---ARHHARRIVPLIQEALAESGLTldDIDAIAFG 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLEGHIYSNWLPPvtgifnskfliskKEFPILNLIVSGGHTELVL 156
Cdd:cd24001    74 RGPGLGGALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKLKT-------------GATRPVALIVSGGNTQVIA 136
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 1-114 2.45e-10

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


Pssm-ID: 440827  Cd Length: 227  Bit Score: 59.86  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   1 MKILGIETSCDDTAMAILEikNEKlkVLANVVssqvkihkkfggvvpFLAAREHTKNISRVFKLTLKKTGI--SDIDLIS 78
Cdd:COG1214     1 MLILAIDTSTEACSVALLD--DGE--VLAERE---------------ENDGRGHSERLLPMIDELLAEAGLtlSDLDAIA 61

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1277140750  79 VTRGPGlgpS---LLTGITFAKTIAWLHKKPILGVNHLE 114
Cdd:COG1214    62 VGIGPG---SftgLRIGVATAKGLALALGIPLVGVSSLE 97
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 3-199 2.23e-09

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


Pssm-ID: 466882 [Multi-domain]  Cd Length: 205  Bit Score: 56.52  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEikneklkvlANVVSSQVKIHKKfggvvpflaaREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:cd24032     1 ILAIDTSTSACSVALLK---------GGKILAEYELDLG----------RRHSERLLPMIDELLKEAGLSlkDLDAIAVG 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750  81 RGPGLGPSLLTGITFAKTIAWLHKKPILGVNHLE---------------------GHIYsnwlppvTGIFNSKFLISKKE 139
Cdd:cd24032    62 IGPGSFTGLRIGLATAKGLALALGIPLVGVSTLEalaqnapradgrvlpaidarrGEVY-------WALYERDKGGLILE 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 140 FPilnLIVSGGHTELVLMKDHGKYQIIGETLDDAAGEAFDKVARLLELGYPGGPAIAKIA 199
Cdd:cd24032   135 EE---EAVLPPEELEEILLLKKPAILVGDGWDKYPDLIKENPVLPIELLLPSAADLAPLA 191
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 3-114 2.10e-08

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


Pssm-ID: 274750 [Multi-domain]  Cd Length: 204  Bit Score: 53.81  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750   3 ILGIETSCDDTAMAILEikNEKlkvlanVVSSQVkihkkfggvvpFLAAREHTKNISRVFKLTLKKTGIS--DIDLISVT 80
Cdd:TIGR03725   1 ILAIDTSTEALSVALLD--DGK------VLAERT-----------EPAGRNHSERLLPMIEELLAEAGLSlqDLDAIAVG 61

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277140750  81 RGPGlgpS---LLTGITFAKTIAWLHKKPILGVNHLE 114
Cdd:TIGR03725  62 VGPG---SftgLRIGLATAKGLALALGIPLVGVSSLE 95
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 174-307 4.84e-08

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 54.73  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277140750 174 AGEAFDKVARLL----ELGYPGGPAI-----AKIAGKGDPQSFNLPRpmlHSKNFNFSYSGLktaVLYLLRDLKKqnvqi 244
Cdd:COG0068   600 AGRLFDAVAALLgicdEISYEGQAAMelealADRAEEAEPYPFPLRE---IDGLLVLDWAPL---LRALLEDLQA----- 668

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277140750 245 nKKIKADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINF 307
Cdd:COG0068   669 -GVPPAEIAARFHNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLLLELLRARLEAAGFKV 730
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 250-311 1.20e-07

N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; 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), also called 3'-hydroxymethylcephem-O-CASE (CCT), is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12), also called decarbamoylnovobiocin carbamoyltransferase, 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.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members in this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466883 [Multi-domain]  Cd Length: 268  Bit Score: 52.30  E-value: 1.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277140750 250 ADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEarGLGINFSCPP 311
Cdd:cd24033   191 ADLAATVQKVFEEALLELIKKLLERTGSDNLCLSGGCALNCVANSKLAEE--GLFKNVFVPP 250
COG2192 COG2192
Predicted carbamoyl transferase, NodU family [General function prediction only];
250-294 1.24e-05

Predicted carbamoyl transferase, NodU family [General function prediction only];


Pssm-ID: 441795 [Multi-domain]  Cd Length: 568  Bit Score: 47.08  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277140750 250 ADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGV----SAN-KLLRE 294
Cdd:COG2192   268 ADLAASVQAVLEEVVLHLARHLHERTGSRNLCLAGGValncVANgRILRE 317
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 250-299 4.34e-05

N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466950 [Multi-domain]  Cd Length: 238  Bit Score: 44.39  E-value: 4.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277140750 250 ADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGVSAN----KLLREKIEKE 299
Cdd:cd24100   161 EDIAAAVQRVLEEVVVEWVKNALKKTGIKNLALAGGVFANvklnQRIAELPEVE 214
ASKHA_NBD_TobZ_N cd24098
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
 250-299 4.66e-05

N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.


Pssm-ID: 466948 [Multi-domain]  Cd Length: 243  Bit Score: 44.37  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277140750 250 ADIAASFQEAAIEVLIQKTKRAVEKYKTKHLFLSGGV----SAN-KLLREKIEKE 299
Cdd:cd24098   165 KDLAASVQAVLEEAVLHLARYLRKKTGERNLCLAGGValncVANgKLLREGPFDN 219
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 249-325 1.61e-03

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 39.78  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277140750 249 KADIAASFQEA--AIEVLIQKTKRAVEKYKTKHLFLSGGVSANKLLREKIEKEARGLGINFSCPPMEYTTdnaamiAVA 325
Cdd:cd10170   252 EEEIRDLFDPVidKILELIEEQLEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGIIIVLRSDDPDT------AVA 324
 
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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