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Conserved domains on  [gi|640530452|ref|WP_024964354|]
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ThiF family adenylyltransferase [Trueperella pyogenes]

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 ...
 31-237 4.46e-87

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: 258.86  E-value: 4.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  31 GGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVF 110
Cdd:COG1179   33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452 111 AQfpRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIRLVCMRRRI-RGLEV 189
Cdd:COG1179  113 SE--DYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIpKGVKV 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640530452 190 LYSTEVP-------ASLPRKGGGSKAETLGTMSYMPPIMGQMLAGKVIRRLVGLE 237
Cdd:COG1179  191 VYSTEQPrkpqadgTVCDTGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 31-237 4.46e-87

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: 258.86  E-value: 4.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  31 GGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVF 110
Cdd:COG1179   33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452 111 AQfpRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIRLVCMRRRI-RGLEV 189
Cdd:COG1179  113 SE--DYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIpKGVKV 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640530452 190 LYSTEVP-------ASLPRKGGGSKAETLGTMSYMPPIMGQMLAGKVIRRLVGLE 237
Cdd:COG1179  191 VYSTEQPrkpqadgTVCDTGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 18-230 8.32e-61

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: 191.28  E-value: 8.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  18 ARLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQ 97
Cdd:cd00755    7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  98 QVYINRDNLAEVFaqFPRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIRL 177
Cdd:cd00755   87 EEFLTPDNSEDLL--GGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLARKVRK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640530452 178 VCMRRRIR-GLEVLYSTEVP-------------ASLPRKGGGSKAETLGTMSYMPPIMGQMLAGKVI 230
Cdd:cd00755  165 RLRKRGIFfGVPVVYSTEPPdppkadelvcgdeVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 38-244 1.53e-28

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: 108.50  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452   38 AEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpD 117
Cdd:pfam00899  36 AKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELIKSF---D 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  118 YVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDpakltfskinkteycplakairlvcMRRRIRGLEVLYSTEVPA 197
Cdd:pfam00899 113 IVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQ-------------------------VTVVIPGKTPCYRCLFPE 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 640530452  198 SLPRKG--GGSKAETLGTmsyMPPIMGQMLAGKVIRRLVGLEPLPLAPR 244
Cdd:pfam00899 168 DPPPKLvpSCTVAGVLGP---TTAVVAGLQALEALKLLLGKGEPNLAGR 213
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 31-176 6.97e-26

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 102.19  E-value: 6.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  31 GGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVF 110
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640530452 111 AQfpRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIR 176
Cdd:PRK15116 119 SA--GFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLR 182
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 41-90 1.24e-03

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: 39.87  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 640530452    41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINP 90
Cdd:TIGR01408  443 VGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINP 492
 
Name Accession Description Interval E-value
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 31-237 4.46e-87

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: 258.86  E-value: 4.46e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  31 GGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVF 110
Cdd:COG1179   33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452 111 AQfpRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIRLVCMRRRI-RGLEV 189
Cdd:COG1179  113 SE--DYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIpKGVKV 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640530452 190 LYSTEVP-------ASLPRKGGGSKAETLGTMSYMPPIMGQMLAGKVIRRLVGLE 237
Cdd:COG1179  191 VYSTEQPrkpqadgTVCDTGGTGLKCAGPGSISFVPAVFGLIAAGEVIRDLLGKA 245
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 18-230 8.32e-61

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: 191.28  E-value: 8.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  18 ARLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQ 97
Cdd:cd00755    7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  98 QVYINRDNLAEVFaqFPRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIRL 177
Cdd:cd00755   87 EEFLTPDNSEDLL--GGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLARKVRK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 640530452 178 VCMRRRIR-GLEVLYSTEVP-------------ASLPRKGGGSKAETLGTMSYMPPIMGQMLAGKVI 230
Cdd:cd00755  165 RLRKRGIFfGVPVVYSTEPPdppkadelvcgdeVGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 35-154 4.54e-31

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: 115.23  E-value: 4.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFp 114
Cdd:COG0476   40 SPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGA- 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 640530452 115 rpDYVIDCIDVVASKIEIAQWCAQNGVHLISsmGGANKFD 154
Cdd:COG0476  119 --DLVLDCTDNFATRYLLNDACVKLGIPLVS--GAVIGFE 154
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 38-244 1.53e-28

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: 108.50  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452   38 AEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpD 117
Cdd:pfam00899  36 AKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLREINPDVEVEAYTERLTPENAEELIKSF---D 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  118 YVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDpakltfskinkteycplakairlvcMRRRIRGLEVLYSTEVPA 197
Cdd:pfam00899 113 IVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQ-------------------------VTVVIPGKTPCYRCLFPE 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 640530452  198 SLPRKG--GGSKAETLGTmsyMPPIMGQMLAGKVIRRLVGLEPLPLAPR 244
Cdd:pfam00899 168 DPPPKLvpSCTVAGVLGP---TTAVVAGLQALEALKLLLGKGEPNLAGR 213
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 31-176 6.97e-26

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 102.19  E-value: 6.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  31 GGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVF 110
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640530452 111 AQfpRPDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGGANKFDPAKLTFSKINKTEYCPLAKAIR 176
Cdd:PRK15116 119 SA--GFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLR 182
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 38-154 8.21e-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: 101.01  E-value: 8.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  38 AEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpD 117
Cdd:cd00757   37 AEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIAGY---D 113

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 640530452 118 YVIDCIDVVASKIEIAQWCAQNGVHLISsmGGANKFD 154
Cdd:cd00757  114 LVLDCTDNFATRYLINDACVKLGKPLVS--GAVLGFE 148
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 35-149 3.48e-25

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


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 96.95  E-value: 3.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFp 114
Cdd:cd01483   12 SEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFLDGV- 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 640530452 115 rpDYVIDCIDVVASKIEIAQWCAQNGVHLISSMGG 149
Cdd:cd01483   91 --DLVIDAIDNIAVRRALNRACKELGIPVIDAGGL 123
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
35-165 6.03e-23

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 93.00  E-value: 6.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQAIaFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFp 114
Cdd:PRK08644  41 SNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDC- 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640530452 115 rpDYVIDCIDVVASKIEIAQWCAQN-GVHLISSMGGANKFDPAKLTFSKINK 165
Cdd:PRK08644 119 --DIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMAGYGDSNSIKTRRIGK 168
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 35-168 1.19e-20

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 85.90  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQAIaFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFp 114
Cdd:cd01487   12 SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQY-FLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGDC- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640530452 115 rpDYVIDCIDVVASKIEIAQWCAQN-GVHLISSMGGANKFDPAKLTFSKINKTEY 168
Cdd:cd01487   90 --DIVVEAFDNAETKAMLAESLLGNkNKPVVCASGMAGFGDSNNIKTKKISDNFY 142
PRK08223 PRK08223
hypothetical protein; Validated
 40-160 2.83e-14

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 70.87  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  40 ALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpDYV 119
Cdd:PRK08223  45 TLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLDGV---DVY 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 640530452 120 IDCID--VVASKIEIAQWCAQNGVHLISS----MGGA-NKFDPAKLTF 160
Cdd:PRK08223 122 VDGLDffEFDARRLVFAACQQRGIPALTAaplgMGTAlLVFDPGGMSF 169
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 19-154 7.12e-13

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 66.41  E-value: 7.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  19 RLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQ 98
Cdd:PRK05690  29 KLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETIN 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 640530452  99 VYINRDNLAEVFAQFprpDYVIDCIDVVASKIEIAQWCAQNGVHLISsmGGANKFD 154
Cdd:PRK05690 109 ARLDDDELAALIAGH---DLVLDCTDNVATRNQLNRACFAAKKPLVS--GAAIRME 159
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
35-239 1.25e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 66.57  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFp 114
Cdd:PRK08762 148 SPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDV- 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452 115 rpDYVIDCIDVVASKIEIAQWCAQNGVHLISsmGGANKFDPAKLTFSKINKTEYCPlakairlvCMRrrirgleVLYSTE 194
Cdd:PRK08762 227 --DVVVDGADNFPTRYLLNDACVKLGKPLVY--GAVFRFEGQVSVFDAGRQRGQAP--------CYR-------CLFPEP 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 640530452 195 VPASL-PrkgggSKAETlGTMSYMPPIMGQMLAGKVIRRLVGL-EPL 239
Cdd:PRK08762 288 PPPELaP-----SCAEA-GVLGVLPGVIGLLQATEAIKLLLGIgDPL 328
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 41-129 6.24e-12

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 64.73  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpDYVI 120
Cdd:PRK07878  61 LAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQY---DLIL 137


                 ....*....
gi 640530452 121 DCIDVVASK 129
Cdd:PRK07878 138 DGTDNFATR 146
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
41-124 4.28e-09

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 56.28  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQVYINRDNLAEVFAQFprpDYVI 120
Cdd:PRK07411  57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPY---DVVV 133


                 ....
gi 640530452 121 DCID 124
Cdd:PRK07411 134 DGTD 137
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 19-137 4.68e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 56.03  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  19 RLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQq 98
Cdd:PRK05597  25 SLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPDVKVTVS- 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 640530452  99 vyINRDNLAEVFAQFPRPDYVIDCIDVVASKiEIAQWCA 137
Cdd:PRK05597 104 --VRRLTWSNALDELRDADVILDGSDNFDTR-HLASWAA 139
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 19-144 9.91e-09

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 55.27  E-value: 9.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  19 RLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDCVTYAQQ 98
Cdd:PRK05600  38 RLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNALR 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 640530452  99 VYINRDNLAEVFAQFprpDYVIDCIDVVASKIEIAQWCAQNGVHLI 144
Cdd:PRK05600 118 ERLTAENAVELLNGV---DLVLDGSDSFATKFLVADAAEITGTPLV 160
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 41-146 5.75e-07

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: 49.11  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDC--VTYAQQVYINRDNLAEVFAQFprpDY 118
Cdd:cd01484   18 LALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCkvVPYQNKVGPEQDFNDTFFEQF---HI 94

                         90       100
                 ....*....|....*....|....*...
gi 640530452 119 VIDCIDVVASKIEIAQWCAQNGVHLISS 146
Cdd:cd01484   95 IVNALDNIIARRYVNGMLIFLIVPLIES 122
PRK14851 PRK14851
hypothetical protein; Provisional
 41-161 6.21e-06

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 47.16  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINP--DCVTYAQQvyINRDNLaEVFaqFPRPDY 118
Cdd:PRK14851  62 MVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPflEITPFPAG--INADNM-DAF--LDGVDV 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 640530452 119 VIDCIDVVASKI--EIAQWCAQNGVHLISSmgGANKFDPAKLTFS 161
Cdd:PRK14851 137 VLDGLDFFQFEIrrTLFNMAREKGIPVITA--GPLGYSSAMLVFT 179
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 35-65 6.77e-06

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 46.26  E-value: 6.77e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 640530452  35 SSCAEALARGGVGRLILLDRDVVEESNINRQ 65
Cdd:PRK12475  37 AANAEALVRAGIGKLTIADRDYVEWSNLQRQ 67
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 38-65 1.02e-05

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 45.75  E-value: 1.02e-05
                         10        20
                 ....*....|....*....|....*...
gi 640530452  38 AEALARGGVGRLILLDRDVVEESNINRQ 65
Cdd:PRK07688  40 AEMLVRAGVGKVTIVDRDYVEWSNLQRQ 67
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 41-91 1.37e-05

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: 45.74  E-value: 1.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPD 91
Cdd:cd01490   23 VGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPD 73
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 41-146 1.86e-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: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDC--VTYAQQVYINRDNLaEVFAQFprpDY 118
Cdd:cd01489   18 LVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVkiVAYHANIKDPDFNV-EFFKQF---DL 93

                         90       100
                 ....*....|....*....|....*...
gi 640530452 119 VIDCIDVVASKIEIAQWCAQNGVHLISS 146
Cdd:cd01489   94 VFNALDNLAARRHVNKMCLAADVPLIES 121
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 41-92 1.20e-04

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: 42.34  E-value: 1.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640530452  41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINPDC 92
Cdd:cd01488   18 LALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGV 69
PRK08328 PRK08328
hypothetical protein; Provisional
 19-144 3.52e-04

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 40.93  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640530452  19 RLSASTVMVVGLGGVGSSCAEALARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAE-MVADINPDCVTYAQ 97
Cdd:PRK08328  24 KLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNPKPLSAKwKLERFNSDIKIETF 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 640530452  98 QVYINRDNLAEVFAQFprpDYVIDCIDVVASKIEIAQWCAQNGVHLI 144
Cdd:PRK08328 104 VGRLSEENIDEVLKGV---DVIVDCLDNFETRYLLDDYAHKKGIPLV 147
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 41-90 1.24e-03

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: 39.87  E-value: 1.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 640530452    41 LARGGVGRLILLDRDVVEESNINRQAIAFVSTVGKVKAQVMAEMVADINP 90
Cdd:TIGR01408  443 VGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATLKINP 492
 
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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