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Conserved domains on  [gi|1092598020|ref|WP_070547595|]
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MULTISPECIES: ThiF family adenylyltransferase [Bacillus]

Protein Classification

tRNA threonylcarbamoyladenosine dehydratase( domain architecture ID 11439562)

tRNA threonylcarbamoyladenosine dehydratase catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine to form cyclic t(6)A in tRNA

EC:  2.3.2.-

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 1-244 4.07e-126

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


:

Pssm-ID: 440792  Cd Length: 247  Bit Score: 357.47  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179     3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  81 MKARIADINPKCEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179    83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179   163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                  ....
gi 1092598020 241 DLLK 244
Cdd:COG1179   240 DLLG 243
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 1-244 4.07e-126

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


Pssm-ID: 440792  Cd Length: 247  Bit Score: 357.47  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179     3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  81 MKARIADINPKCEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179    83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179   163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                  ....
gi 1092598020 241 DLLK 244
Cdd:COG1179   240 DLLG 243
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 12-239 5.95e-103

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 298.36  E-value: 5.95e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPK 91
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  92 CEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAK 171
Cdd:cd00755    81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092598020 172 VVRTKLRKEGIKKGVQVIFSDESPIVIRED---VRKEVGNDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVV 239
Cdd:cd00755   161 KVRKRLRKRGIFFGVPVVYSTEPPDPPKADelvCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 35-193 1.05e-49

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 164.21  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDYDL 114
Cdd:PRK15116   43 SWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020 115 DYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAKVVRTKLRKE-GIKK------GVQ 187
Cdd:PRK15116  123 SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVD 202


                  ....*.
gi 1092598020 188 VIFSDE 193
Cdd:PRK15116  203 CVFSTE 208
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 5-156 2.26e-31

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 115.82  E-value: 2.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   5 FSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMK 82
Cdd:pfam00899   1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092598020  83 ARIADINPKCEVIALKMFYTEETYEQFFdYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRF 156
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV 153
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 13-168 1.22e-05

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 46.04  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   13 GKEGLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKC 92
Cdd:TIGR01408  428 GAIGCEMLKN-------------FALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQI 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   93 EVIALKMFY---TEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISS--MGAANKTDPTRFQIADISKTHTD 167
Cdd:TIGR01408  495 KIDAHQNRVgpeTETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESgtLGTKGNTQVVVPHLTESYGSSRD 574


                   .
gi 1092598020  168 P 168
Cdd:TIGR01408  575 P 575
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 1-244 4.07e-126

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


Pssm-ID: 440792  Cd Length: 247  Bit Score: 357.47  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179     3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  81 MKARIADINPKCEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179    83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179   163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                  ....
gi 1092598020 241 DLLK 244
Cdd:COG1179   240 DLLG 243
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 12-239 5.95e-103

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 298.36  E-value: 5.95e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPK 91
Cdd:cd00755     1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  92 CEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAK 171
Cdd:cd00755    81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092598020 172 VVRTKLRKEGIKKGVQVIFSDESPIVIRED---VRKEVGNDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVV 239
Cdd:cd00755   161 KVRKRLRKRGIFFGVPVVYSTEPPDPPKADelvCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 35-193 1.05e-49

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 164.21  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDYDL 114
Cdd:PRK15116   43 SWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020 115 DYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAKVVRTKLRKE-GIKK------GVQ 187
Cdd:PRK15116  123 SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVD 202


                  ....*.
gi 1092598020 188 VIFSDE 193
Cdd:PRK15116  203 CVFSTE 208
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 5-156 2.26e-31

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 115.82  E-value: 2.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   5 FSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMK 82
Cdd:pfam00899   1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092598020  83 ARIADINPKCEVIALKMFYTEETYEQFFdYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRF 156
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV 153
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-148 1.24e-28

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 108.68  E-value: 1.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNELA--IGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPK 77
Cdd:COG0476     4 ELERYSRQILLpeIGEEGQEKLKAARvlvvgagglgSPVALYLAAAGVGTLTLVDDDVVELSNLQRQiLYT-EADVGRPK 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092598020  78 VDLMKARIADINPKCEVIALKMFYTEETYEQFF-DYDLdyVIDASDTICYKIHLMKECLKRDIPLISsmGAA 148
Cdd:COG0476    83 VEAAAERLRALNPDVEVEAIPERLTEENALELLaGADL--VLDCTDNFATRYLLNDACVKLGIPLVS--GAV 150
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 35-152 1.49e-25

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 100.24  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFF-DY 112
Cdd:cd00757    34 SPAAEYLAAAGVGKLGLVDDDVVELSNLQRQiLHT-EADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIaGY 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1092598020 113 DLdyVIDASDTICYKIHLMKECLKRDIPLISsmGAANKTD 152
Cdd:cd00757   113 DL--VLDCTDNFATRYLINDACVKLGKPLVS--GAVLGFE 148
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 31-159 6.12e-25

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 96.18  E-value: 6.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  31 GGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFF 110
Cdd:cd01483     8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1092598020 111 DyDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIA 159
Cdd:cd01483    88 D-GVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIG 135
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 35-163 1.15e-20

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 85.90  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQlHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDL 114
Cdd:cd01487    12 SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFG-DC 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1092598020 115 DYVIDASDTICYKIHLMKECLK-RDIPLISSMGAANKTDPTRFQIADISK 163
Cdd:cd01487    90 DIVVEAFDNAETKAMLAESLLGnKNKPVVCASGMAGFGDSNNIKTKKISD 139
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
35-148 3.78e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 82.60  E-value: 3.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQlHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDL 114
Cdd:PRK08644   41 SNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFK-DC 118

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1092598020 115 DYVIDASDTICYKIHLMKECLKR-DIPLISSMGAA 148
Cdd:PRK08644  119 DIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMA 153
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 11-148 1.01e-16

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.81  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  11 AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADIN 89
Cdd:PRK05690   21 GFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQvLHD-DATIGQPKVESARAALARIN 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  90 PKCEVIAL-KMFYTEETYEQFFDYDLdyVIDASDTICYKIHLMKECLKRDIPLISsmGAA 148
Cdd:PRK05690  100 PHIAIETInARLDDDELAALIAGHDL--VLDCTDNVATRNQLNRACFAAKKPLVS--GAA 155
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-144 9.05e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 72.74  E-value: 9.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADINP 90
Cdd:PRK08762  125 VGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQiLHT-EDRVGQPKVDSAAQRLAALNP 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1092598020  91 KCEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLISS 144
Cdd:PRK08762  204 DVQVEAVQERVTSDNVEALLQ-DVDVVVDGADNFPTRYLLNDACVKLGKPLVYG 256
PRK08223 PRK08223
hypothetical protein; Validated
 40-148 1.04e-14

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 72.02  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  40 ALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDLDYVID 119
Cdd:PRK08223   45 TLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLD-GVDVYVD 123

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1092598020 120 ASDTICYKIH--LMKECLKRDIPLISS----MGAA 148
Cdd:PRK08223  124 GLDFFEFDARrlVFAACQQRGIPALTAaplgMGTA 158
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 1-122 3.48e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 67.98  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKV 78
Cdd:PRK05597    5 DIARYRRQIMlgEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1092598020  79 DLMKARIADINPKCEV-IALKMFYTEETYEQFFDYDLdyVIDASD 122
Cdd:PRK05597   85 ESAREAMLALNPDVKVtVSVRRLTWSNALDELRDADV--ILDGSD 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 37-127 1.03e-12

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 66.83  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  37 AAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDLDY 116
Cdd:PRK05600   56 AMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLN-GVDL 134

                          90
                  ....*....|.
gi 1092598020 117 VIDASDTICYK 127
Cdd:PRK05600  135 VLDGSDSFATK 145
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
41-122 8.25e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 64.37  E-value: 8.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEV----IALKmfyTEETYEQFFDYDLdy 116
Cdd:PRK07411   57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVdlyeTRLS---SENALDILAPYDV-- 131


                  ....*.
gi 1092598020 117 VIDASD 122
Cdd:PRK07411  132 VVDGTD 137
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-142 2.16e-11

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 62.70  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQ--P 76
Cdd:PRK07688    1 MNERYSRQELfsPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092598020  77 KVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLI 142
Cdd:PRK07688   81 KAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVT-GVDLIIDATDNFETRFIVNDAAQKYGIPWI 145
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 1-122 2.93e-10

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 59.36  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQ--P 76
Cdd:PRK12475    1 MQERYSRQILfsGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1092598020  77 KVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDLDYVIDASD 122
Cdd:PRK12475   81 KAIAAKEHLRKINSEVEIVPVVTDVTVEELEELVK-EVDLIIDATD 125
PRK14851 PRK14851
hypothetical protein; Provisional
 5-144 8.14e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 58.72  E-value: 8.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKAR 84
Cdd:PRK14851   26 FSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQ 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092598020  85 IADINPKCEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIH--LMKECLKRDIPLISS 144
Cdd:PRK14851  106 ALSINPFLEITPFPAGINADNMDAFLD-GVDVVLDGLDFFQFEIRrtLFNMAREKGIPVITA 166
PRK14852 PRK14852
hypothetical protein; Provisional
 5-144 2.15e-09

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 57.40  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKAR 84
Cdd:PRK14852  315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092598020  85 IADINPKCEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKI--HLMKECLKRDIPLISS 144
Cdd:PRK14852  395 ALSVNPFLDIRSFPEGVAAETIDAFLK-DVDLLVDGIDFFALDIrrRLFNRALELGIPVITA 455
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 41-144 2.78e-08

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 53.54  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDYDLDYVIDA 120
Cdd:cd01489    18 LVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDPDFNVEFFKQFDLVFNA 97

                          90       100
                  ....*....|....*....|....
gi 1092598020 121 SDTICYKIHLMKECLKRDIPLISS 144
Cdd:cd01489    98 LDNLAARRHVNKMCLAADVPLIES 121
PRK08328 PRK08328
hypothetical protein; Provisional
 2-142 2.92e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 52.88  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   2 LHQFSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHALLSTVGQPKVDL 80
Cdd:PRK08328    7 LERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQiLHWEEDLGKNPKPLS 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092598020  81 MKARIADINPKCEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLI 142
Cdd:PRK08328   87 AKWKLERFNSDIKIETFVGRLSEENIDEVLK-GVDVIVDCLDNFETRYLLDDYAHKKGIPLV 147
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 41-144 3.40e-08

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 52.58  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEV------IALKMFYTEETYEQFfdydl 114
Cdd:cd01484    18 LALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVvpyqnkVGPEQDFNDTFFEQF----- 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1092598020 115 DYVIDASDTICYKIHLMKECLKRDIPLISS 144
Cdd:cd01484    93 HIIVNALDNIIARRYVNGMLIFLIVPLIES 122
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-122 1.25e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 51.63  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPK 91
Cdd:PRK07878   32 VGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1092598020  92 CEVIaLKMFY--TEETYEQFFDYDLdyVIDASD 122
Cdd:PRK07878  112 VNVR-LHEFRldPSNAVELFSQYDL--ILDGTD 141
PRK07877 PRK07877
Rv1355c family protein;
38-142 1.06e-06

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 49.22  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  38 AEALARSGV-GRILLVDKDDVDITNVNRqLHALLSTVGQPKVDLMKARIADINPKCEVIALKMFYTEETYEQFFDyDLDY 116
Cdd:PRK07877  122 AHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFLD-GLDV 199

                          90       100
                  ....*....|....*....|....*.
gi 1092598020 117 VIDASDTICYKIHLMKECLKRDIPLI 142
Cdd:PRK07877  200 VVEECDSLDVKVLLREAARARRIPVL 225
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 10-109 2.97e-06

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 47.35  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  10 LAIGKEGL--ETLKNstvavlgvggvgsfaaeaLARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIAD 87
Cdd:cd01488     3 LVIGAGGLgcELLKN------------------LALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVND 64

                          90       100
                  ....*....|....*....|....*.
gi 1092598020  88 INPKCEVIA----LKMFyTEETYEQF 109
Cdd:cd01488    65 RVPGVNVTPhfgkIQDK-DEEFYRQF 89
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 16-144 6.63e-06

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 46.51  E-value: 6.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020  16 GLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKCEVI 95
Cdd:cd01490    11 GCELLKN-------------FALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKIT 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1092598020  96 ALKMFYTEETyEQFFDYD----LDYVIDASDTICYKIHLMKECLKRDIPLISS 144
Cdd:cd01490    78 ALQNRVGPET-EHIFNDEfwekLDGVANALDNVDARMYVDRRCVYYRKPLLES 129
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 13-168 1.22e-05

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 46.04  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   13 GKEGLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPKC 92
Cdd:TIGR01408  428 GAIGCEMLKN-------------FALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQI 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   93 EVIALKMFY---TEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISS--MGAANKTDPTRFQIADISKTHTD 167
Cdd:TIGR01408  495 KIDAHQNRVgpeTETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESgtLGTKGNTQVVVPHLTESYGSSRD 574


                   .
gi 1092598020  168 P 168
Cdd:TIGR01408  575 P 575
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 5-143 8.38e-03

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 36.25  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092598020   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ--LHALLSTVGQPKVDLMK 82
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAASY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092598020  83 ARIADINPKCEV-----IALKMFYTEETYEQFFDYDLDYVIDASDTicykIHLMKECLKRDIPLIS 143
Cdd:cd01485    82 EFLQELNPNVKLsiveeDSLSNDSNIEEYLQKFTLVIATEENYERT----AKVNDVCRKHHIPFIS 143
 
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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