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Conserved domains on  [gi|1953020465|ref|XP_038426792|]
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ubiquitin-like modifier-activating enzyme 5 isoform X1 [Canis lupus familiaris]

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 ...
 75-320 1.99e-69

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: 219.27  E-value: 1.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  75 PYSRLMALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 153
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 154 AEYTLRNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 233
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 234 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 311
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 1953020465 312 QDFFPTMSM 320
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 ...
 75-320 1.99e-69

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: 219.27  E-value: 1.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  75 PYSRLMALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 153
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 154 AEYTLRNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 233
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 234 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 311
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 1953020465 312 QDFFPTMSM 320
Cdd:cd00757   220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 76-326 8.68e-52

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: 173.98  E-value: 8.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 154
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenA 234
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAM 311
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*.
gi 1953020465 312 QDFFPTMSMK-PNPQC 326
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 76-326 3.02e-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: 122.55  E-value: 3.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGIvSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 154
Cdd:COG0476     8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEna 234
Cdd:COG0476    87 AERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQ 312
Cdd:COG0476   153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALT 225

                         250
                  ....*....|....
gi 1953020465 313 DFFPTMSMKPNPQC 326
Cdd:COG0476   226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
112-222 4.55e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 85.29  E-value: 4.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 112 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 191
Cdd:PRK08644   44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1953020465 192 leegKPVDLVLSCVDNFEA-RMTINTACNELG 222
Cdd:PRK08644  116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 91-216 6.40e-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: 61.42  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  91 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVH 170
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953020465 171 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 216
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 ...
 75-320 1.99e-69

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: 219.27  E-value: 1.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  75 PYSRLMALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 153
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 154 AEYTLRNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEn 233
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 234 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAM 311
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 1953020465 312 QDFFPTMSM 320
Cdd:cd00757   220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 76-326 8.68e-52

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: 173.98  E-value: 8.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 154
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenA 234
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAM 311
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*.
gi 1953020465 312 QDFFPTMSMK-PNPQC 326
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 76-326 3.02e-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: 122.55  E-value: 3.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGIvSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 154
Cdd:COG0476     8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEna 234
Cdd:COG0476    87 AERLRALNPDVEVEAIPERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQ 312
Cdd:COG0476   153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALT 225

                         250
                  ....*....|....
gi 1953020465 313 DFFPTMSMKPNPQC 326
Cdd:COG0476   226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
112-222 4.55e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 85.29  E-value: 4.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 112 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 191
Cdd:PRK08644   44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1953020465 192 leegKPVDLVLSCVDNFEA-RMTINTACNELG 222
Cdd:PRK08644  116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 76-252 3.20e-18

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 85.04  E-value: 3.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQ 152
Cdd:PRK07688    5 YSRQELFSPIG-EEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 153 AAEYTLRNINPDVLFEVHNYNItTVENFQHFMDRisnggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGvse 232
Cdd:PRK07688   84 AAKKRLEEINSDVRVEAIVQDV-TAEELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA--- 148

                         170       180
                  ....*....|....*....|..
gi 1953020465 233 nAVS--GHIQLIIPGESACFAC 252
Cdd:PRK07688  149 -CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 99-249 1.41e-15

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: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  99 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVlfevhnyNITTV 177
Cdd:cd01483     2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953020465 178 EnfqhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 249
Cdd:cd01483    75 P------EGISEDNLDDfLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 76-252 2.44e-15

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 76.69  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQ 152
Cdd:PRK12475    5 YSRQILFSGIGEEGQ-RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 153 AAEYTLRNINPDVlfEVHNYNI-TTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESG-V 230
Cdd:PRK12475   84 AAKEHLRKINSEV--EIVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcV 150

                         170       180
                  ....*....|....*....|..
gi 1953020465 231 SENAVSghiQLIIPGESACFAC 252
Cdd:PRK12475  151 GSYGVT---YTIIPGKTPCLRC 169
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
99-326 1.39e-12

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 68.50  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  99 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQAAEYTLRNINPDVlfevhnynit 175
Cdd:PRK08762  138 VLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVDSAAQRLAALNPDV---------- 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 176 TVENFQhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESA----CF 250
Cdd:PRK08762  206 QVEAVQ---ERVTSDNVEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR--FEGQVSVFDAGRQRgqapCY 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 251 AC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNP 324
Cdd:PRK08762  281 RClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDP 351


                  ..
gi 1953020465 325 QC 326
Cdd:PRK08762  352 HC 353
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 105-254 3.47e-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: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 105 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITT----VEN 179
Cdd:cd01489     8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953020465 180 FQHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 254
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 ...
 119-255 4.54e-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: 65.29  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 119 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPdvlfevhNYNITTvenFQHFMDRISNGGLEEGKP 197
Cdd:cd01484    22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNP-------NCKVVP---YQNKVGPEQDFNDTFFEQ 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 198 VDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 255
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. ...
 99-217 2.66e-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: 62.01  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  99 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITTVE 178
Cdd:cd01487     2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953020465 179 NFQHFMDrisnggleegkpVDLVLSCVDNFEA-RMTINTA 217
Cdd:cd01487    82 LEGLFGD------------CDIVVEAFDNAETkAMLAESL 109
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 76-326 4.97e-11

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 62.55  E-value: 4.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 154
Cdd:PRK05690   13 YNRQIILRGFDFDGQ-EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITtvenfQHFMDRISNGgleegkpVDLVLSCVDNFEARMTINTACNELGQTWmesgVSENA 234
Cdd:PRK05690   92 RAALARINPHIAIETINARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL----VSGAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 V--SGHIQLIIPGESA-CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLNFGT--VSFYLGYN 309
Cdd:PRK05690  156 IrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLLLYD 228

                         250
                  ....*....|....*..
gi 1953020465 310 AMQDFFPTMSMKPNPQC 326
Cdd:PRK05690  229 AMTMQFREMKLKRDPGC 245
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 91-216 6.40e-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: 61.42  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  91 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEYTLRNINPDVLFEVH 170
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953020465 171 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 216
Cdd:TIGR02354  96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 92-210 7.21e-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: 61.85  E-value: 7.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  92 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEYTLRNINPDVLF 167
Cdd:cd00755     7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953020465 168 EVHNYNITTvENFQHFMdrisnggleeGKPVDLVLSCVDNFEA 210
Cdd:cd00755    84 DAVEEFLTP-DNSEDLL----------GGDPDFVVDAIDSIRA 115
PRK08328 PRK08328
hypothetical protein; Provisional
 92-300 7.73e-10

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 58.65  E-value: 7.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  92 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEYTLRNINPDVLFEV 169
Cdd:PRK08328   23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 170 hnynittvenfqhFMDRISNGGLEEG-KPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESA 248
Cdd:PRK08328  103 -------------FVGRLSEENIDEVlKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTK 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953020465 249 CFACAPPlvvaaNIDEKTLKREGVCAaslptTMGVVAGILVQNVLKFLLNFG 300
Cdd:PRK08328  168 RLREIFP-----KVKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 71-222 3.98e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 57.96  E-value: 3.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  71 VDSNPYSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLS 149
Cdd:PRK05597    4 LDIARYRRQIMLGEIG-QQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQP 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953020465 150 KVQAAEYTLRNINPDVLFEVHNYNITTvenfqhfmdrisNGGLEEGKPVDLVLSCVDNFEARMTINTACNELG 222
Cdd:PRK05597   83 KAESAREAMLALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLG 143
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 92-222 5.92e-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: 53.55  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  92 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEYTLRNINPDVl 166
Cdd:COG1179    20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDC- 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953020465 167 fevhnyNITTVENFqhfmdrISNGGLEE--GKPVDLVLSCVDNFEARMTINTACNELG 222
Cdd:COG1179    95 ------EVTAIDEF------VTPENADEllSEDYDYVIDAIDSVSAKAALIAWCRRRG 140
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 115-257 1.83e-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: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 115 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQ-AAEYTLRNInPDVLFEVHNYNITT--VENFQHFmdrisng 190
Cdd:cd01488    18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEvAAKFVNDRV-PGVNVTPHFGKIQDkdEEFYRQF------- 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953020465 191 gleegkpvDLVLSCVDNFEARMTIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 257
Cdd:cd01488    90 --------NIIICGLDSIEARRWINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 115-324 3.13e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 52.19  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 115 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLE 193
Cdd:PRK05600   60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 194 EGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAvsGHIQLIIPGESAC-------FACAPPLVVAANidekt 266
Cdd:PRK05600  128 LLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFH--GELAVFNSGPDHRgvglrdlFPEQPSGDSIPD----- 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953020465 267 lkregvCAAS--LPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNP 324
Cdd:PRK05600  201 ------CATAgvLGATTAVIGALMATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 121-244 5.74e-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: 51.81  E-value: 5.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  121 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPV 198
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKL 519

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953020465  199 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 244
Cdd:TIGR01408  520 DVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 121-244 4.99e-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: 48.44  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 121 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEYTLRNINPDVLFEVHNYNI-TTVENFqhFMDRISNGgleegkpV 198
Cdd:cd01490    29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgPETEHI--FNDEFWEK-------L 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953020465 199 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 244
Cdd:cd01490   100 DGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
PRK08223 PRK08223
hypothetical protein; Validated
 115-222 5.78e-06

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 47.76  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 115 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEYTLRNINPDVLFEVHNYNITTvENFQHFMDrisnggle 193
Cdd:PRK08223   46 LARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFLD-------- 116

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1953020465 194 egkPVDLVLSCVDNFE--ARMTINTACNELG 222
Cdd:PRK08223  117 ---GVDVYVDGLDFFEfdARRLVFAACQQRG 144
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 76-326 4.92e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 42.00  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 154
Cdd:PRK07878   23 YSRHLIIPDVG-VDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITT---VENFQHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQ--TW---- 225
Cdd:PRK07878  102 RDSIVEINPLVNVRLHEFRLDPsnaVELFSQY---------------DLILDGTDNFATRYLVNDAAVLAGKpyVWgsiy 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 226 -MESGVS---ENAVSGHiqliipgeSACFAC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKFL 296
Cdd:PRK07878  167 rFEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLI 228

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1953020465 297 LNFGT--VSFYLGYNAMQDFFPTMSMKPNPQC 326
Cdd:PRK07878  229 TGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
76-326 1.07e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 40.87  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465  76 YSRLMALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 154
Cdd:PRK07411   19 YSRHLILPEVG-LEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 155 EYTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTwmesgvsenA 234
Cdd:PRK07411   98 KNRILEINPYCQVDLYETRLS------------SENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKP---------N 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953020465 235 VSGHIqLIIPGESACF-------------ACAPPLVVAANidektlkREGVCAASLPttmGVVAGILVQNVLKFLLNFGT 301
Cdd:PRK07411  157 VYGSI-FRFEGQATVFnyeggpnyrdlypEPPPPGMVPSC-------AEGGVLGILP---GIIGVIQATETIKIILGAGN 225

                         250       260
                  ....*....|....*....|....*..
gi 1953020465 302 V--SFYLGYNAMQDFFPTMSMKPNPQC 326
Cdd:PRK07411  226 TlsGRLLLYNALDMKFRELKLRPNPER 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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