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Conserved domains on  [gi|155371865|ref|NP_001094537|]
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ubiquitin-like modifier-activating enzyme 5 [Bos taurus]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 10091534)

HesA/MoeB/ThiF family protein similar to eukaryotic ubiquitin-activating enzyme 5 (UBA5), a UFM1 (ubiquitin-fold modifier 1) E1-activating enzyme, and to bacterial protein HesA that may be required for efficient nitrogen fixation

CATH:  3.40.50.720
Gene Ontology:  GO:0008641
PubMed:  12660720

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 52-297 5.00e-72

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: 225.05  E-value: 5.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  52 PYSRLMALKRMGIVSDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 130
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 131 AEHTLRNINPDVLFEVHNYNItTVENFEHFMNRisnggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 210
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG-----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 211 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 288
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                 ....*....
gi 155371865 289 QDFFPTMSM 297
Cdd:cd00757  220 SMSFRTLKL 228
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 52-297 5.00e-72

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: 225.05  E-value: 5.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  52 PYSRLMALKRMGIVSDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 130
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 131 AEHTLRNINPDVLFEVHNYNItTVENFEHFMNRisnggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 210
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG-----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 211 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 288
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                 ....*....
gi 155371865 289 QDFFPTMSM 297
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 53-303 5.20e-54

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: 178.99  E-value: 5.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865   53 YSRLMALKRMGiVSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 131
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  132 EHTLRNINPDVLFEVHNYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenA 211
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  212 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAM 288
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*.
gi 155371865  289 QDFFPTMSMK-PNPQC 303
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 53-303 7.80e-35

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: 128.71  E-value: 7.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGIvSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 131
Cdd:COG0476    8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 132 EHTLRNINPDVLFEVHNYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEna 211
Cdd:COG0476   87 AERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 212 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQ 289
Cdd:COG0476  153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALT 225

                        250
                 ....*....|....
gi 155371865 290 DFFPTMSMKPNPQC 303
Cdd:COG0476  226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
89-199 4.40e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.91  E-value: 4.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  89 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFEHFMnrisngg 168
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 155371865 169 leegKPVDLVLSCVDNFEA-RMTINTACNELG 199
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 68-193 8.52e-12

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 63.73  E-value: 8.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865   68 YEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 147
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 155371865  148 NYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEAR-MTINT 193
Cdd:TIGR02354  96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 52-297 5.00e-72

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: 225.05  E-value: 5.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  52 PYSRLMALKRMGIVSDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 130
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 131 AEHTLRNINPDVLFEVHNYNItTVENFEHFMNRisnggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 210
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELIAG-----------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 211 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 288
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                 ....*....
gi 155371865 289 QDFFPTMSM 297
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 53-303 5.20e-54

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: 178.99  E-value: 5.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865   53 YSRLMALKRMGiVSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 131
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  132 EHTLRNINPDVLFEVHNYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenA 211
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  212 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAM 288
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*.
gi 155371865  289 QDFFPTMSMK-PNPQC 303
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 53-303 7.80e-35

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: 128.71  E-value: 7.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGIvSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 131
Cdd:COG0476    8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 132 EHTLRNINPDVLFEVHNYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEna 211
Cdd:COG0476   87 AERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 212 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQ 289
Cdd:COG0476  153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALT 225

                        250
                 ....*....|....
gi 155371865 290 DFFPTMSMKPNPQC 303
Cdd:COG0476  226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
89-199 4.40e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.91  E-value: 4.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  89 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFEHFMnrisngg 168
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 155371865 169 leegKPVDLVLSCVDNFEA-RMTINTACNELG 199
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 89-229 2.29e-18

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 85.43  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  89 AEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNItTVENFEHFMNRis 165
Cdd:PRK07688  40 AEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAVAAKKRLEEINSDVRVEAIVQDV-TAEELEELVTG-- 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 155371865 166 nggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGvsenAVS--GHIQLIIPGESACFAC 229
Cdd:PRK07688 117 ---------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 75-226 5.39e-16

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: 74.23  E-value: 5.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  75 TVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVlfevhnyNITT 153
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 155371865 154 VENFEHFMNRisnggLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 226
Cdd:cd01483   74 VPEGISEDNL-----DDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 53-229 5.64e-16

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 78.23  E-value: 5.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGIVSDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQ 129
Cdd:PRK12475   5 YSRQILFSGIGEEGQ-RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 130 AAEHTLRNINPDVlfEVHNYNI-TTVENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESG-V 207
Cdd:PRK12475  84 AAKEHLRKINSEV--EIVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcV 150

                        170       180
                 ....*....|....*....|..
gi 155371865 208 SENAVSghiQLIIPGESACFAC 229
Cdd:PRK12475 151 GSYGVT---YTIIPGKTPCLRC 169
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
76-303 1.96e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 71.20  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  76 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQAAEHTLRNINPDVLFEVHNYNIT 152
Cdd:PRK08762 138 VLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVDSAAQRLAALNPDVQVEAVQERVT 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 153 TvENFEhfmnrisngGLEEGkpVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESA----CFA 228
Cdd:PRK08762 216 S-DNVE---------ALLQD--VDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR--FEGQVSVFDAGRQRgqapCYR 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 229 C----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQ 302
Cdd:PRK08762 282 ClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDPH 352


                 .
gi 155371865 303 C 303
Cdd:PRK08762 353 C 353
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 82-231 2.18e-12

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: 67.40  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  82 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT----VEN 156
Cdd:cd01489    8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 155371865 157 FEHFmnrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 231
Cdd:cd01489   88 FKQF---------------DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 69-187 3.13e-12

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: 65.70  E-value: 3.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  69 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEHTLRNINPDVLF 144
Cdd:cd00755    7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 155371865 145 EVHNYNITTvENFEHFMnrisnggleeGKPVDLVLSCVDNFEA 187
Cdd:cd00755   84 DAVEEFLTP-DNSEDLL----------GGDPDFVVDAIDSIRA 115
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 96-232 3.55e-12

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: 65.68  E-value: 3.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  96 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFehfmnrisngGLEEGKP 174
Cdd:cd01484   22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDF----------NDTFFEQ 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 175 VDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 232
Cdd:cd01484   92 FHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 68-193 8.52e-12

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 63.73  E-value: 8.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865   68 YEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 147
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 155371865  148 NYNITTvENFEHFMnrisnggleegKPVDLVLSCVDNFEAR-MTINT 193
Cdd:TIGR02354  96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 75-194 1.93e-11

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: 62.40  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  75 TVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTV 154
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 155371865 155 ENFEHFmnrisnggleegKPVDLVLSCVDNFEA-RMTINTA 194
Cdd:cd01487   81 NLEGLF------------GDCDIVVEAFDNAETkAMLAESL 109
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 53-303 2.97e-11

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 62.94  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGIVSDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 131
Cdd:PRK05690  13 YNRQIILRGFDFDGQ-EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 132 EHTLRNINPDVLFEVHNYNITtvenfEHFMNRISNGgleegkpVDLVLSCVDNFEARMTINTACNELGQTWmesgVSENA 211
Cdd:PRK05690  92 RAALARINPHIAIETINARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL----VSGAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 212 V--SGHIQLIIPGESA-CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLNFGT--VSFYLGYN 286
Cdd:PRK05690 156 IrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLLLYD 228

                        250
                 ....*....|....*..
gi 155371865 287 AMQDFFPTMSMKPNPQC 303
Cdd:PRK05690 229 AMTMQFREMKLKRDPGC 245
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 48-199 8.97e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 59.89  E-value: 8.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  48 VDSNPYSRLMALKRMGiVSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLS 126
Cdd:PRK05597   4 LDIARYRRQIMLGEIG-QQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQP 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 155371865 127 KVQAAEHTLRNINPDVLFEVHNYNITTvenfehfmnrisNGGLEEGKPVDLVLSCVDNFEARMTINTACNELG 199
Cdd:PRK05597  83 KAESAREAMLALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLG 143
PRK08328 PRK08328
hypothetical protein; Provisional
 69-277 2.50e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 57.11  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  69 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEHTLRNINPDVLFEV 146
Cdd:PRK08328  23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 147 HnYNITTVENFEHFMnrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 226
Cdd:PRK08328 103 F-VGRLSEENIDEVL-----------KGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTKR 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 155371865 227 FACAPPlvvaaNIDEKTLKREGVCAaslptTMGVVAGILVQNVLKFLLNFG 277
Cdd:PRK08328 169 LREIFP-----KVKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 69-199 4.80e-09

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: 56.63  E-value: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  69 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEHTLRNINPDVl 143
Cdd:COG1179   20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDC- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 155371865 144 fevhnyNITTVENFehfmnrISNGGLEE--GKPVDLVLSCVDNFEARMTINTACNELG 199
Cdd:COG1179   95 ------EVTAIDEF------VTPENADEllSEDYDYVIDAIDSVSAKAALIAWCRRRG 140
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 92-234 1.46e-07

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: 52.36  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  92 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVEnfEHFMNRISnggle 170
Cdd:cd01488   18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKD--EEFYRQFN----- 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 155371865 171 egkpvdLVLSCVDNFEARMTIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 234
Cdd:cd01488   91 ------IIICGLDSIEARRWINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 92-301 1.56e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 52.96  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  92 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfehfmnriSNGGLE 170
Cdd:PRK05600  60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 171 EGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAvsGHIQLIIPGESAC-------FACAPPLVVAANidekt 243
Cdd:PRK05600 128 LLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFH--GELAVFNSGPDHRgvglrdlFPEQPSGDSIPD----- 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 155371865 244 lkregvCAAS--LPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNP 301
Cdd:PRK05600 201 ------CATAgvLGATTAVIGALMATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 98-221 3.86e-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: 3.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865    98 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI----TTVENFEHFMNrisnggleeg 172
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpetETIFNDEFYEK---------- 518

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 155371865   173 kpVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 221
Cdd:TIGR01408  519 --LDVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 98-221 6.93e-07

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: 51.14  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  98 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVlfevhnyNITTVEN-----FEHFMNRISNGGLee 171
Cdd:cd01490   29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDL-------KITALQNrvgpeTEHIFNDEFWEKL-- 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 155371865 172 gkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 221
Cdd:cd01490  100 ----DGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
PRK08223 PRK08223
hypothetical protein; Validated
 65-199 1.43e-05

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 46.21  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  65 VSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLRNINPDVL 143
Cdd:PRK08223  19 PTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELE 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 155371865 144 FEVHNYNITTvENFEHFMnrisnggleEGkpVDLVLSCVDNFE--ARMTINTACNELG 199
Cdd:PRK08223  99 IRAFPEGIGK-ENADAFL---------DG--VDVYVDGLDFFEfdARRLVFAACQQRG 144
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 53-303 1.15e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 43.93  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGiVSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 131
Cdd:PRK07878  23 YSRHLIIPDVG-VDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 132 EHTLRNINPDVLFEVHNYNITT---VENFEHFmnrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQ--TW---- 202
Cdd:PRK07878 102 RDSIVEINPLVNVRLHEFRLDPsnaVELFSQY---------------DLILDGTDNFATRYLVNDAAVLAGKpyVWgsiy 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 203 -MESGVS---ENAVSGHiqliipgeSACFAC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKFL 273
Cdd:PRK07878 167 rFEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLI 228

                        250       260       270
                 ....*....|....*....|....*....|..
gi 155371865 274 LNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 303
Cdd:PRK07878 229 TGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
53-367 1.47e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 43.57  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865  53 YSRLMALKRMGiVSDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 131
Cdd:PRK07411  19 YSRHLILPEVG-LEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 132 EHTLRNINPDVLFEVHNYNITtvenfehfmnriSNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTwmesgvsenA 211
Cdd:PRK07411  98 KNRILEINPYCQVDLYETRLS------------SENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKP---------N 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 212 VSGHIqLIIPGESACF-------------ACAPPLVVAANidektlkREGVCAASLPttmGVVAGILVQNVLKFLLNFGT 278
Cdd:PRK07411 157 VYGSI-FRFEGQATVFnyeggpnyrdlypEPPPPGMVPSC-------AEGGVLGILP---GIIGVIQATETIKIILGAGN 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 155371865 279 V--SFYLGYNAMQDFFPTMSMKPNPQCD--------DRNC--RKQQKEYKKKVAALPKQEVIQEEGEIIHEDNEWGIELV 346
Cdd:PRK07411 226 TlsGRLLLYNALDMKFRELKLRPNPERPvieklidyEQFCgiPQAKAAEAAQKAEIPEMTVTELKALLDSGADDFVLIDV 305

                        330       340
                 ....*....|....*....|....*
gi 155371865 347 SEISEEELKKSSG----PIPDLPEG 367
Cdd:PRK07411 306 RNPNEYEIARIPGsvlvPLPDIENG 330
 
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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