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Conserved domains on  [gi|489322444|ref|WP_003229763|]
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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 8.13e-127

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: 359.40  E-value: 8.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179    3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  81 MKARIADINPECEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179  163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                 ....
gi 489322444 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 8.13e-127

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: 359.40  E-value: 8.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179    3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  81 MKARIADINPECEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179  163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                 ....
gi 489322444 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 9.27e-104

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: 300.29  E-value: 9.27e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPE 91
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  92 CEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAK 171
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489322444 172 VVRTKLRKEGIKKGVQVIFSDESPIVIRED---VRKEVGNDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVV 239
Cdd:cd00755  161 KVRKRLRKRGIFFGVPVVYSTEPPDPPKADelvCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 35-193 1.09e-50

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 166.52  E-value: 1.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDYDL 114
Cdd:PRK15116  43 SWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444 115 DYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAKVVRTKLRKE-GIKK------GVQ 187
Cdd:PRK15116 123 SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVD 202


                 ....*.
gi 489322444 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 1.42e-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: 116.20  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    5 FSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMK 82
Cdd:pfam00899   1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489322444   83 ARIADINPECEVIALKMFYTEETYEQFFdYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRF 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 1.42e-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: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    13 GKEGLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPEC 92
Cdd:TIGR01408  428 GAIGCEMLKN-------------FALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQI 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    93 EVIALKMFY---TEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISS--MGAANKTDPTRFQIADISKTHTD 167
Cdd:TIGR01408  495 KIDAHQNRVgpeTETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESgtLGTKGNTQVVVPHLTESYGSSRD 574


                   .
gi 489322444   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 8.13e-127

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: 359.40  E-value: 8.13e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNELAIGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDL 80
Cdd:COG1179    3 MERRFSRTERLYGEEGLERLANAHvavvglggvgSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  81 MKARIADINPECEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIAD 160
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVAD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444 161 ISKTHTDPIAKVVRTKLRKEGIKKGVQVIFSDESPIVIREDVRKEvgnDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVVM 240
Cdd:COG1179  163 LSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVC---DTGGTGLKCAGPGSISFVPAVFGLIAAGEVIR 239


                 ....
gi 489322444 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 9.27e-104

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: 300.29  E-value: 9.27e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPE 91
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  92 CEVIALKMFYTEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAK 171
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489322444 172 VVRTKLRKEGIKKGVQVIFSDESPIVIRED---VRKEVGNDEAKIRKAKMPPSSNAFVPSVAGLIMGGHVV 239
Cdd:cd00755  161 KVRKRLRKRGIFFGVPVVYSTEPPDPPKADelvCGDEVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 35-193 1.09e-50

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 166.52  E-value: 1.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDYDL 114
Cdd:PRK15116  43 SWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444 115 DYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRFQIADISKTHTDPIAKVVRTKLRKE-GIKK------GVQ 187
Cdd:PRK15116 123 SYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDfGVVKnskgklGVD 202


                 ....*.
gi 489322444 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 1.42e-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: 116.20  E-value: 1.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    5 FSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMK 82
Cdd:pfam00899   1 YSRQLAlpLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489322444   83 ARIADINPECEVIALKMFYTEETYEQFFdYDLDYVIDASDTICYKIHLMKECLKRDIPLISSMGAANKTDPTRF 156
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV 153
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 1-148 1.18e-29

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: 111.37  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNELA--IGKEGLETLKNSTvavlgvggvgSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPK 77
Cdd:COG0476    4 ELERYSRQILLpeIGEEGQEKLKAARvlvvgagglgSPVALYLAAAGVGTLTLVDDDVVELSNLQRQiLYT-EADVGRPK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489322444  78 VDLMKARIADINPECEVIALKMFYTEETYEQFF-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 2.63e-26

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: 102.17  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFF-DY 112
Cdd:cd00757   34 SPAAEYLAAAGVGKLGLVDDDVVELSNLQRQiLHT-EADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIaGY 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489322444 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 1.85e-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: 97.72  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  31 GGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFF 110
Cdd:cd01483    8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489322444 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 9.26e-21

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: 86.28  E-value: 9.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQlHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDL 114
Cdd:cd01487   12 SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFG-DC 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489322444 115 DYVIDASDTICYKIHLMKECLK-RDIPLISSMGAANKTDPTRFQIADISK 163
Cdd:cd01487   90 DIVVEAFDNAETKAMLAESLLGnKNKPVVCASGMAGFGDSNNIKTKKISD 139
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
35-148 1.97e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 83.37  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  35 SFAAEALARSGVGRILLVDKDDVDITNVNRQlHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDL 114
Cdd:PRK08644  41 SNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFK-DC 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489322444 115 DYVIDASDTICYKIHLMKECLKR-DIPLISSMGAA 148
Cdd:PRK08644 119 DIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMA 153
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 11-148 3.97e-17

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 77.96  E-value: 3.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  11 AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADIN 89
Cdd:PRK05690  21 GFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQvLHD-DATIGQPKVESARAALARIN 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  90 PECEVIAL-KMFYTEETYEQFFDYDLdyVIDASDTICYKIHLMKECLKRDIPLISsmGAA 148
Cdd:PRK05690 100 PHIAIETInARLDDDELAALIAGHDL--VLDCTDNVATRNQLNRACFAAKKPLVS--GAA 155
PRK08223 PRK08223
hypothetical protein; Validated
 40-148 1.29e-15

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 74.33  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  40 ALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDLDYVID 119
Cdd:PRK08223  45 TLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLD-GVDVYVD 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489322444 120 ASDTICYKIH--LMKECLKRDIPLISS----MGAA 148
Cdd:PRK08223 124 GLDFFEFDARrlVFAACQQRGIPALTAaplgMGTA 158
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
12-144 3.90e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.89  E-value: 3.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHAlLSTVGQPKVDLMKARIADINP 90
Cdd:PRK08762 125 VGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQiLHT-EDRVGQPKVDSAAQRLAALNP 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489322444  91 ECEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLISS 144
Cdd:PRK08762 204 DVQVEAVQERVTSDNVEALLQ-DVDVVVDGADNFPTRYLLNDACVKLGKPLVYG 256
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 1-122 1.10e-13

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 69.52  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKV 78
Cdd:PRK05597   5 DIARYRRQIMlgEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489322444  79 DLMKARIADINPECEV-IALKMFYTEETYEQFFDYDLdyVIDASD 122
Cdd:PRK05597  85 ESAREAMLALNPDVKVtVSVRRLTWSNALDELRDADV--ILDGSD 127
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 37-127 5.63e-13

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 67.60  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  37 AAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDLDY 116
Cdd:PRK05600  56 AMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLN-GVDL 134

                         90
                 ....*....|.
gi 489322444 117 VIDASDTICYK 127
Cdd:PRK05600 135 VLDGSDSFATK 145
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-142 4.44e-12

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 64.63  E-value: 4.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQ--P 76
Cdd:PRK07688   1 MNERYSRQELfsPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489322444  77 KVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLI 142
Cdd:PRK07688  81 KAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVT-GVDLIIDATDNFETRFIVNDAAQKYGIPWI 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 489322444  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEV----IALKmfyTEETYEQFFDYDLdy 116
Cdd:PRK07411  57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVdlyeTRLS---SENALDILAPYDV-- 131


                 ....*.
gi 489322444 117 VIDASD 122
Cdd:PRK07411 132 VVDGTD 137
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 1-122 4.36e-11

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 62.06  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   1 MLHQFSRNEL--AIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQ--P 76
Cdd:PRK12475   1 MQERYSRQILfsGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkkP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489322444  77 KVDLMKARIADINPECEVIALKMFYTEETYEQFFDyDLDYVIDASD 122
Cdd:PRK12475  81 KAIAAKEHLRKINSEVEIVPVVTDVTVEELEELVK-EVDLIIDATD 125
PRK14851 PRK14851
hypothetical protein; Provisional
 5-144 8.45e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 58.72  E-value: 8.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKAR 84
Cdd:PRK14851  26 FSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQ 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489322444  85 IADINPECEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIH--LMKECLKRDIPLISS 144
Cdd:PRK14851 106 ALSINPFLEITPFPAGINADNMDAFLD-GVDVVLDGLDFFQFEIRrtLFNMAREKGIPVITA 166
PRK14852 PRK14852
hypothetical protein; Provisional
 5-144 2.23e-09

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 57.40  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKAR 84
Cdd:PRK14852 315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489322444  85 IADINPECEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKI--HLMKECLKRDIPLISS 144
Cdd:PRK14852 395 ALSVNPFLDIRSFPEGVAAETIDAFLK-DVDLLVDGIDFFALDIrrRLFNRALELGIPVITA 455
PRK08328 PRK08328
hypothetical protein; Provisional
 2-142 1.61e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 53.65  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   2 LHQFSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ-LHALLSTVGQPKVDL 80
Cdd:PRK08328   7 LERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQiLHWEEDLGKNPKPLS 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489322444  81 MKARIADINPECEVIALKMFYTEETYEQFFDyDLDYVIDASDTICYKIHLMKECLKRDIPLI 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 3.53e-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: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEV------IALKMFYTEETYEQFfdydl 114
Cdd:cd01484   18 LALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVvpyqnkVGPEQDFNDTFFEQF----- 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 489322444 115 DYVIDASDTICYKIHLMKECLKRDIPLISS 144
Cdd:cd01484   93 HIIVNALDNIIARRYVNGMLIFLIVPLIES 122
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 41-144 4.14e-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: 53.15  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  41 LARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVIALKMFYTEETYEQFFDYDLDYVIDA 120
Cdd:cd01489   18 LVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDPDFNVEFFKQFDLVFNA 97

                         90       100
                 ....*....|....*....|....
gi 489322444 121 SDTICYKIHLMKECLKRDIPLISS 144
Cdd:cd01489   98 LDNLAARRHVNKMCLAADVPLIES 121
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 12-122 1.43e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 51.63  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  12 IGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPE 91
Cdd:PRK07878  32 VGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489322444  92 CEVIaLKMFY--TEETYEQFFDYDLdyVIDASD 122
Cdd:PRK07878 112 VNVR-LHEFRldPSNAVELFSQYDL--ILDGTD 141
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 10-109 3.05e-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: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  10 LAIGKEGL--ETLKNstvavlgvggvgsfaaeaLARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIAD 87
Cdd:cd01488    3 LVIGAGGLgcELLKN------------------LALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVND 64

                         90       100
                 ....*....|....*....|....*.
gi 489322444  88 INPECEVIA----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 4.13e-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: 47.28  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444  16 GLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPECEVI 95
Cdd:cd01490   11 GCELLKN-------------FALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKIT 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489322444  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 1.42e-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: 1.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    13 GKEGLETLKNstvavlgvggvgsFAAEALARSGVGRILLVDKDDVDITNVNRQLHALLSTVGQPKVDLMKARIADINPEC 92
Cdd:TIGR01408  428 GAIGCEMLKN-------------FALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINPQI 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444    93 EVIALKMFY---TEETYEQFFDYDLDYVIDASDTICYKIHLMKECLKRDIPLISS--MGAANKTDPTRFQIADISKTHTD 167
Cdd:TIGR01408  495 KIDAHQNRVgpeTETIFNDEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESgtLGTKGNTQVVVPHLTESYGSSRD 574


                   .
gi 489322444   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 8.78e-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: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489322444   5 FSRNELAIGKEGLETLKNSTVAVLGVGGVGSFAAEALARSGVGRILLVDKDDVDITNVNRQ--LHALLSTVGQPKVDLMK 82
Cdd:cd01485    2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAASY 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489322444  83 ARIADINPECEV-----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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