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Conserved domains on  [gi|517479003|ref|WP_018649586|]
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MULTISPECIES: ThiF family adenylyltransferase [Thioalkalivibrio]

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 ...
 14-248 3.76e-123

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: 349.77  E-value: 3.76e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  14 ERTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRI 93
Cdd:COG1179    8 SRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  94 RDIDPDIEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETR 173
Cdd:COG1179   88 RDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTS 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517479003 174 VCPLARQMRKRLRRLGAHLDYPVVFSIEQPRKGTEHRPV---GDGGRPRSVNGTISYLPAIFGLTAAGHVIQTLITRA 248
Cdd:COG1179  168 NCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVcdtGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 14-248 3.76e-123

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: 349.77  E-value: 3.76e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  14 ERTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRI 93
Cdd:COG1179    8 SRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  94 RDIDPDIEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETR 173
Cdd:COG1179   88 RDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTS 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517479003 174 VCPLARQMRKRLRRLGAHLDYPVVFSIEQPRKGTEHRPV---GDGGRPRSVNGTISYLPAIFGLTAAGHVIQTLITRA 248
Cdd:COG1179  168 NCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVcdtGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 20-241 1.78e-91

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: 269.09  E-value: 1.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPD 99
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003 100 IEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETRVCPLAR 179
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517479003 180 QMRKRLRRLGAHLDYPVVFSIEQPRK------GTEHRPVGDG---GRPRSVNGTISYLPAIFGLTAAGHVI 241
Cdd:cd00755  161 KVRKRLRKRGIFFGVPVVYSTEPPDPpkadelVCGDEVGADAalqGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 19-248 3.09e-49

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 162.67  E-value: 3.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  19 LLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDP 98
Cdd:PRK15116  19 LYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  99 DIEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETRVCPLA 178
Cdd:PRK15116  99 ECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003 179 RQMRKRLRRlgahlDYPV------------VFSIEQ---PR-KGT--EHRPVGDGgrPRSVN-----GTISYLPAIFGLT 235
Cdd:PRK15116 179 AKLRERLKS-----DFGVvknskgklgvdcVFSTEAlvyPQaDGSvcAMKSTAEG--PKRMDcasgfGAATMVTATFGFV 251

                        250
                 ....*....|...
gi 517479003 236 AAGHVIQTLITRA 248
Cdd:PRK15116 252 AVSHALKKMMAKA 264
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-244 4.35e-38

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: 133.15  E-value: 4.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003   19 LLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDP 98
Cdd:pfam00899   9 LIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003   99 DIEVIIRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVrVGPLTETRVCPLA 178
Cdd:pfam00899  89 DVEVEAYTERLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV-IPGKTPCYRCLFP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517479003  179 RQMRKRLRRLGAhldypvvfsieqprkgtehrpvgdggrprsVNGTISYLPAIFGLTAAGHVIQTL 244
Cdd:pfam00899 167 EDPPPKLVPSCT------------------------------VAGVLGPTTAVVAGLQALEALKLL 202
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 20-132 1.23e-07

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: 52.20  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003    20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGV-----GRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIR 94
Cdd:TIGR01408  409 FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATL 488

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 517479003    95 DIDPDIEVIIRQDFLQPDT---IGDLVPEDADFVLDAIDSI 132
Cdd:TIGR01408  489 KINPQIKIDAHQNRVGPETetiFNDEFYEKLDVVINALDNV 529
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 14-248 3.76e-123

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: 349.77  E-value: 3.76e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  14 ERTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRI 93
Cdd:COG1179    8 SRTERLYGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  94 RDIDPDIEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETR 173
Cdd:COG1179   88 RDINPDCEVTAIDEFVTPENADELLSEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTS 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517479003 174 VCPLARQMRKRLRRLGAHLDYPVVFSIEQPRKGTEHRPV---GDGGRPRSVNGTISYLPAIFGLTAAGHVIQTLITRA 248
Cdd:COG1179  168 NCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRKPQADGTVcdtGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 20-241 1.78e-91

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: 269.09  E-value: 1.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPD 99
Cdd:cd00755    1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003 100 IEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETRVCPLAR 179
Cdd:cd00755   81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517479003 180 QMRKRLRRLGAHLDYPVVFSIEQPRK------GTEHRPVGDG---GRPRSVNGTISYLPAIFGLTAAGHVI 241
Cdd:cd00755  161 KVRKRLRKRGIFFGVPVVYSTEPPDPpkadelVCGDEVGADAalqGLRRAGLGSASTVPAVFGLAIASEVI 231
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 19-248 3.09e-49

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 162.67  E-value: 3.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  19 LLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDP 98
Cdd:PRK15116  19 LYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  99 DIEVIIRQDFLQPDTIGDLVPEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPLTETRVCPLA 178
Cdd:PRK15116  99 ECRVTVVDDFITPDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003 179 RQMRKRLRRlgahlDYPV------------VFSIEQ---PR-KGT--EHRPVGDGgrPRSVN-----GTISYLPAIFGLT 235
Cdd:PRK15116 179 AKLRERLKS-----DFGVvknskgklgvdcVFSTEAlvyPQaDGSvcAMKSTAEG--PKRMDcasgfGAATMVTATFGFV 251

                        250
                 ....*....|...
gi 517479003 236 AAGHVIQTLITRA 248
Cdd:PRK15116 252 AVSHALKKMMAKA 264
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 19-244 4.35e-38

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: 133.15  E-value: 4.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003   19 LLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDP 98
Cdd:pfam00899   9 LIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003   99 DIEVIIRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVrVGPLTETRVCPLA 178
Cdd:pfam00899  89 DVEVEAYTERLTPENAEELI-KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVV-IPGKTPCYRCLFP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517479003  179 RQMRKRLRRLGAhldypvvfsieqprkgtehrpvgdggrprsVNGTISYLPAIFGLTAAGHVIQTL 244
Cdd:pfam00899 167 EDPPPKLVPSCT------------------------------VAGVLGPTTAVVAGLQALEALKLL 202
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 26-151 6.87e-36

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: 127.55  E-value: 6.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  26 ARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIR 105
Cdd:COG0476   23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 517479003 106 QDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVIS 151
Cdd:COG0476  103 PERLTEENALELL-AGADLVLDCTDNFATRYLLNDACVKLGIPLVS 147
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 32-169 2.96e-32

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: 115.06  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  32 HVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQDFLQP 111
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 517479003 112 DTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRIDPTAVRVGPL 169
Cdd:cd01483   81 DNLDDFL-DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSL 137
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 26-152 4.63e-30

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: 111.80  E-value: 4.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  26 ARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLvaLRSTVD--RPKTEIMANRIRDIDPDIEVI 103
Cdd:cd00757   17 EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQI--LHTEADvgQPKAEAAAERLRAINPDVEIE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 517479003 104 IRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVISS 152
Cdd:cd00757   95 AYNERLDAENAEELI-AGYDLVLDCTDNFATRYLINDACVKLGKPLVSG 142
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 32-165 5.72e-30

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: 110.16  E-value: 5.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  32 HVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALrSTVDRPKTEIMANRIRDIDPDIEVIIRQDFLQP 111
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFL-SQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517479003 112 DTIGDLVPeDADFVLDAIDSIVCKAALVATAQ-ARGQAVISSMGAGGRIDPTAVR 165
Cdd:cd01487   80 NNLEGLFG-DCDIVVEAFDNAETKAMLAESLLgNKNKPVVCASGMAGFGDSNNIK 133
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
20-157 4.42e-29

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 108.79  E-value: 4.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALrSTVDRPKTEIMANRIRDIDPD 99
Cdd:PRK08644  18 HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFI-SQIGMPKVEALKENLLEINPF 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517479003 100 IEVIIRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATA-QARGQAVISSMGAGG 157
Cdd:PRK08644  97 VEIEAHNEKIDEDNIEELF-KDCDIVVEAFDNAETKAMLVETVlEHPGKKLVAASGMAG 154
PRK08223 PRK08223
hypothetical protein; Validated
 9-146 1.04e-22

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 93.59  E-value: 1.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003   9 HNPFTeRTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEI 88
Cdd:PRK08223   7 DEAFC-RNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEV 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  89 MANRIRDIDPDIEVIIRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKA--ALVATAQARG 146
Cdd:PRK08223  86 LAEMVRDINPELEIRAFPEGIGKENADAFL-DGVDVYVDGLDFFEFDArrLVFAACQQRG 144
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 27-160 4.70e-20

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 85.67  E-value: 4.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:PRK05690  29 KLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETIN 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517479003 107 DFLQPDTIGDLVPeDADFVLDAIDSIVCKAALVATAQARGQAVISsmGAGGRID 160
Cdd:PRK05690 109 ARLDDDELAALIA-GHDLVLDCTDNVATRNQLNRACFAAKKPLVS--GAAIRME 159
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
26-130 3.62e-19

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 85.45  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  26 ARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIR 105
Cdd:PRK08762 131 RRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAV 210

                         90       100
                 ....*....|....*....|....*
gi 517479003 106 QDFLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK08762 211 QERVTSDNVEALL-QDVDVVVDGAD 234
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 27-142 2.20e-18

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 83.01  E-value: 2.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:PRK05600  38 RLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALR 117

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517479003 107 DFLQPDTIGDLVpEDADFVLDAIDSIVCKaALVATA 142
Cdd:PRK05600 118 ERLTAENAVELL-NGVDLVLDGSDSFATK-FLVADA 151
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 27-130 3.02e-18

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 82.47  E-value: 3.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQlvALRSTVD----RPKTEIMANRIRDIDPDIEV 102
Cdd:PRK12475  21 KIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQ--QLYTEEDakqkKPKAIAAKEHLRKINSEVEI 98

                         90       100
                 ....*....|....*....|....*...
gi 517479003 103 IIRQDFLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK12475  99 VPVVTDVTVEELEELV-KEVDLIIDATD 125
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 27-130 2.30e-17

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 79.92  E-value: 2.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:PRK05597  25 SLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVSV 104

                         90       100
                 ....*....|....*....|....
gi 517479003 107 DFLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK05597 105 RRLTWSNALDEL-RDADVILDGSD 127
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 27-130 2.04e-15

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 74.26  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDR--PKTEIMANRIRDIDPDIEV-I 103
Cdd:PRK07688  21 KLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlPKAVAAKKRLEEINSDVRVeA 100

                         90       100
                 ....*....|....*....|....*..
gi 517479003 104 IRQDfLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK07688 101 IVQD-VTAEELEELV-TGVDLIIDATD 125
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 20-130 2.36e-15

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 74.36  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPD 99
Cdd:PRK07878  32 VGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPL 111

                         90       100       110
                 ....*....|....*....|....*....|.
gi 517479003 100 IEVIIRQDFLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK07878 112 VNVRLHEFRLDPSNAVELF-SQYDLILDGTD 141
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
20-130 1.29e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 66.68  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPD 99
Cdd:PRK07411  28 VGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPY 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 517479003 100 IEVIIRQDFLQPDTIGDLVpEDADFVLDAID 130
Cdd:PRK07411 108 CQVDLYETRLSSENALDIL-APYDVVVDGTD 137
PRK07877 PRK07877
Rv1355c family protein;
26-160 4.64e-12

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 65.40  E-value: 4.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  26 ARLRDRHVFIAGLGgVGSYAAEAIARAGV-GRMTLADHDVVGASNLNRqlvaLRSTV---DRPKTEIMANRIRDIDPDIE 101
Cdd:PRK07877 103 ERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR----VPAGVfdlGVNKAVVAARRIAELDPYLP 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 517479003 102 VIIRQDFLQPDTIGDLVpEDADFVLDAIDSIVCKAALVATAQARGQAVISSMGAGGRID 160
Cdd:PRK07877 178 VEVFTDGLTEDNVDAFL-DGLDVVVEECDSLDVKVLLREAARARRIPVLMATSDRGLLD 235
PRK14851 PRK14851
hypothetical protein; Provisional
 27-130 3.37e-11

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 62.57  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:PRK14851  40 RLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFP 119

                         90       100
                 ....*....|....*....|....
gi 517479003 107 DFLQPDTIgDLVPEDADFVLDAID 130
Cdd:PRK14851 120 AGINADNM-DAFLDGVDVVLDGLD 142
PRK14852 PRK14852
hypothetical protein; Provisional
 27-130 1.00e-10

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 61.25  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  27 RLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:PRK14852 329 RLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFP 408

                         90       100
                 ....*....|....*....|....
gi 517479003 107 DFLQPDTIgDLVPEDADFVLDAID 130
Cdd:PRK14852 409 EGVAAETI-DAFLKDVDLLVDGID 431
PRK08328 PRK08328
hypothetical protein; Provisional
 14-146 7.13e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 57.50  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  14 ERTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDR-PKTEIMANR 92
Cdd:PRK08328  11 DRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWK 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517479003  93 IRDIDPDIEVIIRQDFLQPDTIgDLVPEDADFVLDAIDSIVCKAALVATAQARG 146
Cdd:PRK08328  91 LERFNSDIKIETFVGRLSEENI-DEVLKGVDVIVDCLDNFETRYLLDDYAHKKG 143
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 33-135 9.98e-10

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: 57.20  E-value: 9.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  33 VFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQDFLQPD 112
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                         90       100
                 ....*....|....*....|....
gi 517479003 113 -TIGDLVPEDADFVLDAIDSIVCK 135
Cdd:cd01484   82 qDFNDTFFEQFHIIVNALDNIIAR 105
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 32-132 5.45e-09

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: 55.76  E-value: 5.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  32 HVFIAGLGGVGSYAAEAIARAGV-----GRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQ 106
Cdd:cd01490    1 KVFLVGAGAIGCELLKNFALMGVgtgesGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100
                 ....*....|....*....|....*....
gi 517479003 107 DFLQPDT---IGDLVPEDADFVLDAIDSI 132
Cdd:cd01490   81 NRVGPETehiFNDEFWEKLDGVANALDNV 109
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 14-139 9.22e-09

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: 53.58  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  14 ERTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVD--RPKTEIMAN 91
Cdd:cd01485    3 DRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVSNsgMNRAAASYE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 517479003  92 RIRDIDPDIEVIIrqdflqpdtigdlVPEDADFVLDAIDSIVCKAALV 139
Cdd:cd01485   83 FLQELNPNVKLSI-------------VEEDSLSNDSNIEEYLQKFTLV 117
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 19-110 1.18e-08

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 53.45  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  19 LLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDP 98
Cdd:cd01492   10 LWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNP 89

                         90
                 ....*....|..
gi 517479003  99 DIEVIIRQDFLQ 110
Cdd:cd01492   90 RVKVSVDTDDIS 101
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 20-132 1.23e-07

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: 52.20  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003    20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGV-----GRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIR 94
Cdd:TIGR01408  409 FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATL 488

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 517479003    95 DIDPDIEVIIRQDFLQPDT---IGDLVPEDADFVLDAIDSI 132
Cdd:TIGR01408  489 KINPQIKIDAHQNRVGPETetiFNDEFYEKLDVVINALDNV 529
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 20-138 4.80e-07

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 49.57  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  20 LGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPD 99
Cdd:cd01491    9 LGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARLAELNPY 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517479003 100 IEVIIRQDflqpdtigdlvPEDADFVLDAIDSIVCKAAL 138
Cdd:cd01491   89 VPVTVSTG-----------PLTTDELLKFQVVVLTDASL 116
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 15-102 5.32e-07

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: 50.27  E-value: 5.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003    15 RTDLLLGHDVTARLRDRHVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIR 94
Cdd:TIGR01408    9 RQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKLA 88


                   ....*...
gi 517479003    95 DIDPDIEV 102
Cdd:TIGR01408   89 ELNPYVHV 96
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 32-102 6.54e-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: 46.19  E-value: 6.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517479003  32 HVFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEV 102
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNV 71
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 33-147 1.50e-05

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: 45.06  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517479003  33 VFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQLVALRSTVDRPKTEIMANRIRDIDPDIEVIIRQDFLQPD 112
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 517479003 113 TIGDLVPEDADFVLDAIDSI--------VCKAALVA-----TAQARGQ 147
Cdd:cd01489   82 DFNVEFFKQFDLVFNALDNLaarrhvnkMCLAADVPliesgTTGFLGQ 129
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 33-102 3.41e-03

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 38.12  E-value: 3.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517479003  33 VFIAGLGGVGSYAAEAIARAGVGRMTLADHDVVGASNLNRQlvALRSTVD----RPKTEIMANRIRDIDPDIEV 102
Cdd:cd01486    2 CLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQ--SLFTFEDckggKPKAEAAAERLKEIFPSIDA 73
 
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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