NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2129192916|ref|NP_001001765|]
View 

ubiquitin-like modifier-activating enzyme 5 [Gallus gallus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 47-292 1.49e-72

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


:

Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 226.20  E-value: 1.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  47 PYSRLMALKRMGIVKDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 125
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 126 AEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSEn 205
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 206 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTV--SYYLGYNAM 283
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 2129192916 284 QDFFPTMAM 292
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 ...
 47-292 1.49e-72

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 226.20  E-value: 1.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  47 PYSRLMALKRMGIVKDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 125
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 126 AEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSEn 205
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 206 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTV--SYYLGYNAM 283
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 2129192916 284 QDFFPTMAM 292
Cdd:cd00757   220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 48-299 4.22e-55

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: 181.69  E-value: 4.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 126
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNYNITTLDNFEHFmdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSenA 206
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 207 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTVSY---YLGYNAM 283
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*..
gi 2129192916 284 QDFFPTMAMK-PNPQCS 299
Cdd:pfam00899 221 TMTFRELRLAlKNPNCP 237
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 48-298 4.90e-38

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: 137.18  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGIvKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 126
Cdd:COG0476     8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNYNITTlDNfehfmdrisngALEEGKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSEna 206
Cdd:COG0476    87 AERLRALNPDVEVEAIPERLTE-EN-----------ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 207 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKYLLNFGT--VSYYLGYNAMQ 284
Cdd:COG0476   153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEplAGRLLLFDALT 225

                         250
                  ....*....|....
gi 2129192916 285 DFFPTMAMKPNPQC 298
Cdd:COG0476   226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
84-202 1.93e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 86.06  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  84 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisnga 163
Cdd:PRK08644   44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2129192916 164 leegKPVDLVLSCVDNFEA-RMAINTACNELGQ-IWMESGV 202
Cdd:PRK08644  116 ----KDCDIVVEAFDNAETkAMLVETVLEHPGKkLVAASGM 152
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 61-188 1.55e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 66.05  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  61 KDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFE 140
Cdd:TIGR02354  14 KIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2129192916 141 VHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEAR-MAINT 188
Cdd:TIGR02354  94 AYDEKITE-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 ...
 47-292 1.49e-72

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 226.20  E-value: 1.49e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  47 PYSRLMALKRMGIVKDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQA 125
Cdd:cd00757     1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 126 AEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSEn 205
Cdd:cd00757    80 AAERLRAINPDVEIEAYNERLDA-ENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 206 aVSGHIQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTV--SYYLGYNAM 283
Cdd:cd00757   147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDAL 219


                  ....*....
gi 2129192916 284 QDFFPTMAM 292
Cdd:cd00757   220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 48-299 4.22e-55

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: 181.69  E-value: 4.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAA 126
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNYNITTLDNFEHFmdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSenA 206
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTPENAEELI------------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 207 VSGHIQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKYLLNFGTVSY---YLGYNAM 283
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDAL 220

                         250
                  ....*....|....*..
gi 2129192916 284 QDFFPTMAMK-PNPQCS 299
Cdd:pfam00899 221 TMTFRELRLAlKNPNCP 237
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 48-298 4.90e-38

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: 137.18  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGIvKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 126
Cdd:COG0476     8 YSRQILLPEIGE-EGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNYNITTlDNfehfmdrisngALEEGKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSEna 206
Cdd:COG0476    87 AERLRALNPDVEVEAIPERLTE-EN-----------ALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 207 VSGHIQLIIPGESACFACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKYLLNFGT--VSYYLGYNAMQ 284
Cdd:COG0476   153 FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEplAGRLLLFDALT 225

                         250
                  ....*....|....
gi 2129192916 285 DFFPTMAMKPNPQC 298
Cdd:COG0476   226 MEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
84-202 1.93e-19

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 86.06  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  84 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNFEHFMdrisnga 163
Cdd:PRK08644   44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2129192916 164 leegKPVDLVLSCVDNFEA-RMAINTACNELGQ-IWMESGV 202
Cdd:PRK08644  116 ----KDCDIVVEAFDNAETkAMLVETVLEHPGKkLVAASGM 152
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 48-224 1.97e-18

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 85.43  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQ 124
Cdd:PRK07688    5 YSRQELFSPIG-EEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 125 AAEHTLRNINPDVQFEVHNYNITTlDNFEHFMDRisngaleegkpVDLVLSCVDNFEARMAINTACNELGQIWMESGvse 204
Cdd:PRK07688   84 AAKKRLEEINSDVRVEAIVQDVTA-EELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA--- 148

                         170       180
                  ....*....|....*....|..
gi 2129192916 205 nAVS--GHIQLIIPGESACFAC 224
Cdd:PRK07688  149 -CVGsyGLSYTIIPGKTPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 70-221 5.82e-17

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: 76.92  E-value: 5.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  70 TVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVqfevhnyNITT 148
Cdd:cd01483     1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129192916 149 ldnfeHFMDRISNGALEEGKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSenAVSGHIQLIIPGESAC 221
Cdd:cd01483    74 -----VPEGISEDNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 48-224 1.11e-15

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 77.46  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQ 124
Cdd:PRK12475    5 YSRQILFSGIG-EEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 125 AAEHTLRNINPDVQFEVHNYNItTLDNFEHFMdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESG-VS 203
Cdd:PRK12475   84 AAKEHLRKINSEVEIVPVVTDV-TVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVG 151

                         170       180
                  ....*....|....*....|.
gi 2129192916 204 ENAVSghiQLIIPGESACFAC 224
Cdd:PRK12475  152 SYGVT---YTIIPGKTPCLRC 169
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 38-298 4.30e-15

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 74.11  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  38 MSPEVTDSN--PYSRLMALKRMGIVKDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQ 114
Cdd:PRK05690    1 MMAELSDEEmlRYNRQIILRGFDFDGQ-EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 115 PHQAGLSKVQAAEHTLRNINPDVQFEVHNyniTTLDnfEHFMDRISNGaleegkpVDLVLSCVDNFEARMAINTACNELG 194
Cdd:PRK05690   80 DATIGQPKVESARAALARINPHIAIETIN---ARLD--DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 195 Q-------IWMEsgvsenavsGHIQLIIPGESA-CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLK 266
Cdd:PRK05690  148 KplvsgaaIRME---------GQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIK 211

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2129192916 267 YLLNFGT--VSYYLGYNAMQDFFPTMAMKPNPQC 298
Cdd:PRK05690  212 LLTGYGEplSGRLLLYDAMTMQFREMKLKRDPGC 245
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
48-299 5.12e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 75.82  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGIvKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQ 124
Cdd:PRK08762  116 YSRHLRLPEVGE-EGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVD 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 125 AAEHTLRNINPDVQFEVHNYNITTlDNFEhfmdrisngALEEGkpVDLVLSCVDNFEARMAINTACNELGqIWMESGvse 204
Cdd:PRK08762  193 SAAQRLAALNPDVQVEAVQERVTS-DNVE---------ALLQD--VDVVVDGADNFPTRYLLNDACVKLG-KPLVYG--- 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 205 nAV---SGHIQLIIPGESA----CFAC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKYLLNFGT 273
Cdd:PRK08762  257 -AVfrfEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGD 326

                         250       260
                  ....*....|....*....|....*...
gi 2129192916 274 --VSYYLGYNAMQDFFPTMAMKPNPQCS 299
Cdd:PRK08762  327 plTGRLLTFDALAMRFRELRLPPDPHCP 354
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 64-186 9.18e-14

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: 70.33  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  64 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEHTLRNINPDVQF 139
Cdd:cd00755     7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2129192916 140 EVHNYNItTLDNFEHFMdrisngaleeGKPVDLVLSCVDNFEARMAI 186
Cdd:cd00755    84 DAVEEFL-TPDNSEDLL----------GGDPDFVVDAIDSIRAKVAL 119
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 70-189 1.37e-12

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: 65.48  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  70 TVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTL 149
Cdd:cd01487     1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2129192916 150 DNFEHFMDrisngaleegkpVDLVLSCVDNFEA-RMAINTA 189
Cdd:cd01487    81 NLEGLFGD------------CDIVVEAFDNAETkAMLAESL 109
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 77-226 1.40e-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: 67.79  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  77 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLD-NFEH 154
Cdd:cd01489     8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDPDfNVEF 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129192916 155 FmdrisngaleegKPVDLVLSCVDNFEARMAINTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACAP 226
Cdd:cd01489    88 F------------KQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 61-188 1.55e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 66.05  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  61 KDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVQFE 140
Cdd:TIGR02354  14 KIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2129192916 141 VHNYNITTlDNFEHFMdrisngaleegKPVDLVLSCVDNFEAR-MAINT 188
Cdd:TIGR02354  94 AYDEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 91-227 2.31e-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: 66.06  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  91 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDNF-EHFMDRIsngaleegk 168
Cdd:cd01484    22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFnDTFFEQF--------- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129192916 169 pvDLVLSCVDNFEARMAINTACNELGQIWMESGVSenAVSGHIQLIIPGESACFACA--PP 227
Cdd:cd01484    93 --HIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 64-194 4.49e-11

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: 62.41  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  64 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEHTLRNINPDVQ 138
Cdd:COG1179    20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDCE 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2129192916 139 FEVHNYNITTlDNFEHFMDRisngaleegkPVDLVLSCVDNFEARMAINTACNELG 194
Cdd:COG1179    96 VTAIDEFVTP-ENADELLSE----------DYDYVIDAIDSVSAKAALIAWCRRRG 140
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 44-197 5.00e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 63.74  E-value: 5.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  44 DSNPYSRLMALKRMGIVKDyEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSK 122
Cdd:PRK05597    5 DIARYRRQIMLGEIGQQGQ-QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQPK 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129192916 123 VQAAEHTLRNINPDVQFEVHNYNITTldnfehfmdrisNGALEEGKPVDLVLSCVDNFEARMAINTACNELG--QIW 197
Cdd:PRK05597   84 AESAREAMLALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLGipHVW 148
PRK08328 PRK08328
hypothetical protein; Provisional
 64-272 1.09e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 58.27  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  64 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEHTLRNINPDVQFEV 141
Cdd:PRK08328   23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 142 hnynittldnfehFMDRISNGALEEG-KPVDLVLSCVDNFEARMAINTACNELGqIWMESGVSEnAVSGHIQLIIPGESA 220
Cdd:PRK08328  103 -------------FVGRLSEENIDEVlKGVDVIVDCLDNFETRYLLDDYAHKKG-IPLVHGAVE-GTYGQVTTIVPGKTK 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2129192916 221 CFACAPPlvvaaNIDEKTLKREGVCAaslptTMGVVAGILVQNVLKYLLNFG 272
Cdd:PRK08328  168 RLREIFP-----KVKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 87-229 9.85e-09

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: 56.21  E-value: 9.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  87 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITTLDnfEHFMDRISngale 165
Cdd:cd01488    18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDKD--EEFYRQFN----- 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129192916 166 egkpvdLVLSCVDNFEARMAIN-TACNELGQ------IWMESGVSEnAVSGHIQLIIPGESACFAC----APPLV 229
Cdd:cd01488    91 ------IIICGLDSIEARRWINgTLVSLLLYedpesiIPLIDGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 87-183 7.02e-08

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 54.12  E-value: 7.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  87 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNITtldnfehfmdriSNGALE 165
Cdd:PRK05600   60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                          90
                  ....*....|....*...
gi 2129192916 166 EGKPVDLVLSCVDNFEAR 183
Cdd:PRK05600  128 LLNGVDLVLDGSDSFATK 145
PRK08223 PRK08223
hypothetical protein; Validated
 64-194 2.92e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 51.61  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  64 EKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLRNINPDVQFEVH 142
Cdd:PRK08223   23 QRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELEIRAF 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2129192916 143 NYNITTlDNFEHFMDrisngaleegkPVDLVLSCVDNFE--ARMAINTACNELG 194
Cdd:PRK08223  103 PEGIGK-ENADAFLD-----------GVDVYVDGLDFFEfdARRLVFAACQQRG 144
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 93-216 2.93e-07

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


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 52.29  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  93 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNI--TTLDNF-EHFMDRisngaleegk 168
Cdd:cd01490    29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpETEHIFnDEFWEK---------- 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2129192916 169 pVDLVLSCVDNFEARMAINTACNELGQIWMESGVSenAVSGHIQLIIP 216
Cdd:cd01490    99 -LDGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 93-216 7.96e-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: 51.43  E-value: 7.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916   93 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVQFEVHNYNI--TTldnfehfmDRISNGALEEGkp 169
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpET--------ETIFNDEFYEK-- 518

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2129192916  170 VDLVLSCVDNFEARMAINTACNELGQIWMESGVSenAVSGHIQLIIP 216
Cdd:TIGR01408  519 LDVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
48-298 1.59e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 49.73  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 126
Cdd:PRK07411   19 YSRHLILPEVG-LEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNYNITtldnfehfmdriSNGALEEGKPVDLVLSCVDNFEARMAINTAC------NELGQIWMES 200
Cdd:PRK07411   98 KNRILEINPYCQVDLYETRLS------------SENALDILAPYDVVVDGTDNFPTRYLVNDACvllnkpNVYGSIFRFE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 201 GVSE--NAVSGhiqliiPGESACFACAPP--LVVAANidektlkrEGVCAASLPttmGVVAGILVQNVLKYLLNFGTV-- 274
Cdd:PRK07411  166 GQATvfNYEGG------PNYRDLYPEPPPpgMVPSCA--------EGGVLGILP---GIIGVIQATETIKIILGAGNTls 228

                         250       260
                  ....*....|....*....|....
gi 2129192916 275 SYYLGYNAMQDFFPTMAMKPNPQC 298
Cdd:PRK07411  229 GRLLLYNALDMKFRELKLRPNPER 252
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 48-298 1.87e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 46.24  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  48 YSRLMALKRMGiVKDYEKIRTFTVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAA 126
Cdd:PRK07878   23 YSRHLIIPDVG-VDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 127 EHTLRNINPDVQFEVHNyniTTLDnfehfmdriSNGALEEGKPVDLVLSCVDNFEARMAINTACNELGQ--IW-----ME 199
Cdd:PRK07878  102 RDSIVEINPLVNVRLHE---FRLD---------PSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKpyVWgsiyrFE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916 200 SGVS---ENAVSGHiqliipgeSACFAC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKYLLNF 271
Cdd:PRK07878  170 GQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLITGI 231

                         250       260
                  ....*....|....*....|....*....
gi 2129192916 272 GT--VSYYLGYNAMQDFFPTMAMKPNPQC 298
Cdd:PRK07878  232 GEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 77-157 2.42e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 39.40  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129192916  77 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEHTLRNINPDVQFEVHNYNITTlDNF 152
Cdd:PRK15116   39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNR---QIHalrdNVGLAKAEVMAERIRQINPECRVTVVDDFITP-DNV 114


                  ....*
gi 2129192916 153 EHFMD 157
Cdd:PRK15116  115 AEYMS 119
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH