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Conserved domains on  [gi|995970191|ref|NP_001307139|]
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ubiquitin-like modifier-activating enzyme 5 isoform 2 [Homo sapiens]

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 ...
 1-241 2.28e-68

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: 213.88  E-value: 2.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   1 MALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTL 79
Cdd:cd00757    6 ILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  80 RNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGH 159
Cdd:cd00757   85 RAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 160 IQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFP 237
Cdd:cd00757  151 VTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFR 224


                 ....
gi 995970191 238 TMSM 241
Cdd:cd00757  225 TLKL 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 ...
 1-241 2.28e-68

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: 213.88  E-value: 2.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   1 MALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTL 79
Cdd:cd00757    6 ILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  80 RNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGH 159
Cdd:cd00757   85 RAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 160 IQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFP 237
Cdd:cd00757  151 VTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFR 224


                 ....
gi 995970191 238 TMSM 241
Cdd:cd00757  225 TLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-247 1.66e-50

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: 168.20  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191    1 MALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTL 79
Cdd:pfam00899   5 LALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   80 RNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGH 159
Cdd:pfam00899  84 REINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  160 IQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFF 236
Cdd:pfam00899 150 VTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTF 224

                         250
                  ....*....|..
gi 995970191  237 PTMSMK-PNPQC 247
Cdd:pfam00899 225 RELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-247 2.91e-32

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: 120.62  E-value: 2.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:COG0476   23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACF 171
Cdd:COG0476  103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995970191 172 ACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 247
Cdd:COG0476  169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
33-143 3.79e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.52  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  33 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 112
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 995970191 113 leegKPVDLVLSCVDNFEA-RMTINTACNELG 143
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 12-137 2.18e-11

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: 62.19  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   12 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 995970191   92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 137
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 ...
 1-241 2.28e-68

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: 213.88  E-value: 2.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   1 MALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTL 79
Cdd:cd00757    6 ILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  80 RNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGH 159
Cdd:cd00757   85 RAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 160 IQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFP 237
Cdd:cd00757  151 VTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFR 224


                 ....
gi 995970191 238 TMSM 241
Cdd:cd00757  225 TLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 1-247 1.66e-50

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: 168.20  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191    1 MALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTL 79
Cdd:pfam00899   5 LALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   80 RNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGH 159
Cdd:pfam00899  84 REINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  160 IQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFF 236
Cdd:pfam00899 150 VTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTF 224

                         250
                  ....*....|..
gi 995970191  237 PTMSMK-PNPQC 247
Cdd:pfam00899 225 RELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 13-247 2.91e-32

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: 120.62  E-value: 2.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:COG0476   23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACF 171
Cdd:COG0476  103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995970191 172 ACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 247
Cdd:COG0476  169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
33-143 3.79e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 84.52  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  33 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 112
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|..
gi 995970191 113 leegKPVDLVLSCVDNFEA-RMTINTACNELG 143
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 33-173 1.53e-18

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 85.04  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  33 AEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNItTVENFQHFMDRis 109
Cdd:PRK07688  40 AEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAVAAKKRLEEINSDVRVEAIVQDV-TAEELEELVTG-- 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995970191 110 nggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGvsenAVS--GHIQLIIPGESACFAC 173
Cdd:PRK07688 117 ---------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 20-170 7.75e-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: 73.46  E-value: 7.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVlfevhnyNITTV 98
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995970191  99 EnfqhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 170
Cdd:cd01483   75 P------EGISEDNLDDfLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 13-173 9.00e-15

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 74.38  E-value: 9.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEHTLRNINPDVlfE 89
Cdd:PRK12475  20 RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAIAAKEHLRKINSEV--E 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  90 VHNYNI-TTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESG-VSENAVSghiQLIIPGE 167
Cdd:PRK12475  98 IVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVGSYGVT---YTIIPGK 163


                 ....*.
gi 995970191 168 SACFAC 173
Cdd:PRK12475 164 TPCLRC 169
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
20-247 1.37e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 70.81  E-value: 1.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQAAEHTLRNINPDVlfevhnynit 96
Cdd:PRK08762 138 VLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVDSAAQRLAALNPDV---------- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  97 TVENFQhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESA----CF 171
Cdd:PRK08762 206 QVEAVQ---ERVTSDNVEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR--FEGQVSVFDAGRQRgqapCY 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 172 AC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNP 245
Cdd:PRK08762 281 RClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDP 351


                 ..
gi 995970191 246 QC 247
Cdd:PRK08762 352 HC 353
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 26-175 2.13e-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: 67.02  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT----VEN 100
Cdd:cd01489    8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995970191 101 FQHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 175
Cdd:cd01489   88 FKQF---------------DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 40-176 4.18e-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: 64.91  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  40 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPdvlfevhNYNITTvenFQHFMDRISNGGLEEGKP 118
Cdd:cd01484   22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNP-------NCKVVP---YQNKVGPEQDFNDTFFEQ 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 119 VDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 176
Cdd:cd01484   92 FHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 20-138 1.46e-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: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVE 99
Cdd:cd01487    2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 995970191 100 NFQHFMDrisnggleegkpVDLVLSCVDNFEA-RMTINTA 138
Cdd:cd01487   82 LEGLFGD------------CDIVVEAFDNAETkAMLAESL 109
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 13-131 1.83e-11

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: 63.01  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEHTLRNINPDVLF 88
Cdd:cd00755    7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 995970191  89 EVHNYNITTvENFQHFMdrisnggleeGKPVDLVLSCVDNFEA 131
Cdd:cd00755   84 DAVEEFLTP-DNSEDLL----------GGDPDFVVDAIDSIRA 115
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 12-137 2.18e-11

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: 62.19  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   12 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 995970191   92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 137
Cdd:TIGR02354  96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 13-247 3.26e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 59.47  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:PRK05690  28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESARAALARINPHIAIETI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  92 NYNITtvenfQHFMDRISNGgleegkpVDLVLSCVDNFEARMTINTACNELGQTWmesgVSENAV--SGHIQLIIPGESA 169
Cdd:PRK05690 108 NARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL----VSGAAIrmEGQVTVFTYQDDE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 170 -CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQ 246
Cdd:PRK05690 172 pCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLLLYDAMTMQFREMKLKRDPG 244


                 .
gi 995970191 247 C 247
Cdd:PRK05690 245 C 245
PRK08328 PRK08328
hypothetical protein; Provisional
 13-221 1.52e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 57.50  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEHTLRNINPDVLFEV 90
Cdd:PRK08328  23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  91 hnynittvenfqhFMDRISNGGLEEG-KPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESA 169
Cdd:PRK08328 103 -------------FVGRLSEENIDEVlKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTK 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 995970191 170 CFACAPPlvvaaNIDEKTLKREGVCAaslptTMGVVAGILVQNVLKFLLNFG 221
Cdd:PRK08328 168 RLREIFP-----KVKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 13-143 1.78e-08

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: 54.32  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEHTLRNINPDVl 87
Cdd:COG1179   20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDC- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 995970191  88 fevhnyNITTVENFqhfmdrISNGGLEE--GKPVDLVLSCVDNFEARMTINTACNELG 143
Cdd:COG1179   95 ------EVTAIDEF------VTPENADEllSEDYDYVIDAIDSVSAKAALIAWCRRRG 140
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 36-245 1.16e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 52.96  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  36 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLE 114
Cdd:PRK05600  60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 115 EGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAvsGHIQLIIPGESAC-------FACAPPLVVAANidekt 187
Cdd:PRK05600 128 LLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFH--GELAVFNSGPDHRgvglrdlFPEQPSGDSIPD----- 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 995970191 188 lkregvCAAS--LPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNP 245
Cdd:PRK05600 201 ------CATAgvLGATTAVIGALMATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 36-178 2.00e-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: 51.59  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  36 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT--VENFQHFmdrisngg 112
Cdd:cd01488   18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDkdEEFYRQF-------- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 995970191 113 leegkpvDLVLSCVDNFEARMTIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 178
Cdd:cd01488   90 -------NIIICGLDSIEARRWINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 42-165 2.88e-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: 2.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191    42 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPV 119
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKL 519

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 995970191   120 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 165
Cdd:TIGR01408  520 DVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 2-143 3.29e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 51.41  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191   2 ALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLR 80
Cdd:PRK05597  14 MLGEIG-QQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQPKAESAREAML 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995970191  81 NINPDVLFEVHNYNITTvenfqhfmdrisNGGLEEGKPVDLVLSCVDNFEARMTINTACNELG 143
Cdd:PRK05597  93 ALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLG 143
PRK08223 PRK08223
hypothetical protein; Validated
 36-143 1.69e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 48.91  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  36 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMDrisnggle 114
Cdd:PRK08223  46 LARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFLD-------- 116

                         90       100       110
                 ....*....|....*....|....*....|.
gi 995970191 115 egkPVDLVLSCVDNFE--ARMTINTACNELG 143
Cdd:PRK08223 117 ---GVDVYVDGLDFFEfdARRLVFAACQQRG 144
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 42-165 2.60e-06

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 48.82  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  42 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDRISNGgleegkpV 119
Cdd:cd01490   29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgPETEHI--FNDEFWEK-------L 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 995970191 120 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 165
Cdd:cd01490  100 DGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 26-247 2.45e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 42.77  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT---VENF 101
Cdd:PRK07878  51 GGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPsnaVELF 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 102 QHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQ--TW-----MESGVS---ENAVSGHiqliipgeSACF 171
Cdd:PRK07878 131 SQY---------------DLILDGTDNFATRYLVNDAAVLAGKpyVWgsiyrFEGQASvfwEDAPDGL--------GLNY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 172 AC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPN 244
Cdd:PRK07878 188 RDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKD 257


                 ...
gi 995970191 245 PQC 247
Cdd:PRK07878 258 PST 260
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
26-247 2.04e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 39.72  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191  26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfqhf 104
Cdd:PRK07411  47 GGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLS-------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995970191 105 mdriSNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTwmesgvsenAVSGHIqLIIPGESACF------------- 171
Cdd:PRK07411 119 ----SENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKP---------NVYGSI-FRFEGQATVFnyeggpnyrdlyp 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995970191 172 ACAPPLVVAANidektlkREGVCAASLPttmGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSMKPNPQC 247
Cdd:PRK07411 185 EPPPPGMVPSC-------AEGGVLGILP---GIIGVIQATETIKIILGAGNTlsGRLLLYNALDMKFRELKLRPNPER 252
 
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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