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Conserved domains on  [gi|334182302|ref|NP_172027|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

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 ...
 61-310 1.24e-79

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: 245.46  E-value: 1.24e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  61 PYSRLMALQRMGIVDNyERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDA 139
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 140 AVQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESG 219
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDAENAEELI----------------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 220 VSEdaVSGHIQLLVPGETACFACAPPLVVASGIdertlkREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEV--SPYLG 297
Cdd:cd00757  144 VLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLL 215

                        250
                 ....*....|...
gi 334182302 298 YNSLKDFFPTMKM 310
Cdd:cd00757  216 FDALSMSFRTLKL 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 ...
 61-310 1.24e-79

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: 245.46  E-value: 1.24e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  61 PYSRLMALQRMGIVDNyERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDA 139
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 140 AVQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESG 219
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDAENAEELI----------------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 220 VSEdaVSGHIQLLVPGETACFACAPPLVVASGIdertlkREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEV--SPYLG 297
Cdd:cd00757  144 VLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLL 215

                        250
                 ....*....|...
gi 334182302 298 YNSLKDFFPTMKM 310
Cdd:cd00757  216 FDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 62-318 5.26e-72

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: 226.37  E-value: 5.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302   62 YSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAA 140
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGV 220
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTPENAEELI----------------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  221 SedAVSGHIQLLVPGETACFACapplvVASGIDERTLKREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEVSP---YLG 297
Cdd:pfam00899 144 L--GFKGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQ 216

                         250       260
                  ....*....|....*....|..
gi 334182302  298 YNSLKDFFPTMKMR-PNPQCSN 318
Cdd:pfam00899 217 FDALTMTFRELRLAlKNPNCPV 238
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-316 1.92e-49

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: 168.00  E-value: 1.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGIVDNyERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAA 140
Cdd:COG0476    8 YSRQILLPEIGEEGQ-EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGV 220
Cdd:COG0476   87 AERLRALNPDVEVEAIPERLTEENALELL----------------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 221 SEdaVSGHIQLLVPGETACFACAPPLVVASGIDERTlkregvcAASLPTTMGVVAGLLVQNSLKFLLNFGEVSP--YLGY 298
Cdd:COG0476  151 IG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLF 221

                        250
                 ....*....|....*...
gi 334182302 299 NSLKDFFPTMKMRPNPQC 316
Cdd:COG0476  222 DALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
75-161 3.23e-26

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 104.94  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  75 DNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLE 154
Cdd:PRK08644  21 KLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIE 100


                 ....*..
gi 334182302 155 SFTMNIT 161
Cdd:PRK08644 101 AHNEKID 107
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 77-161 2.66e-19

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: 85.69  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302   77 YERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLESF 156
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95


                  ....*
gi 334182302  157 TMNIT 161
Cdd:TIGR02354  96 DEKIT 100
 
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 ...
 61-310 1.24e-79

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: 245.46  E-value: 1.24e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  61 PYSRLMALQRMGIVDNyERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDA 139
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 140 AVQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESG 219
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDAENAEELI----------------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 220 VSEdaVSGHIQLLVPGETACFACAPPLVVASGIdertlkREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEV--SPYLG 297
Cdd:cd00757  144 VLG--FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLL 215

                        250
                 ....*....|...
gi 334182302 298 YNSLKDFFPTMKM 310
Cdd:cd00757  216 FDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 62-318 5.26e-72

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: 226.37  E-value: 5.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302   62 YSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAA 140
Cdd:pfam00899   1 YSRQLALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGV 220
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTPENAEELI----------------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  221 SedAVSGHIQLLVPGETACFACapplvVASGIDERTLKREGVCAASLPTTMGVVAGLLVQNSLKFLLNFGEVSP---YLG 297
Cdd:pfam00899 144 L--GFKGQVTVVIPGKTPCYRC-----LFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQ 216

                         250       260
                  ....*....|....*....|..
gi 334182302  298 YNSLKDFFPTMKMR-PNPQCSN 318
Cdd:pfam00899 217 FDALTMTFRELRLAlKNPNCPV 238
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-316 1.92e-49

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: 168.00  E-value: 1.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGIVDNyERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAA 140
Cdd:COG0476    8 YSRQILLPEIGEEGQ-EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGV 220
Cdd:COG0476   87 AERLRALNPDVEVEAIPERLTEENALELL----------------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 221 SEdaVSGHIQLLVPGETACFACAPPLVVASGIDERTlkregvcAASLPTTMGVVAGLLVQNSLKFLLNFGEVSP--YLGY 298
Cdd:COG0476  151 IG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLF 221

                        250
                 ....*....|....*...
gi 334182302 299 NSLKDFFPTMKMRPNPQC 316
Cdd:COG0476  222 DALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
75-161 3.23e-26

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 104.94  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  75 DNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLE 154
Cdd:PRK08644  21 KLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIE 100


                 ....*..
gi 334182302 155 SFTMNIT 161
Cdd:PRK08644 101 AHNEKID 107
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 62-316 9.94e-26

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 104.54  E-value: 9.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGIvDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAA 140
Cdd:PRK05690  13 YNRQIILRGFDF-DGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRqTWMESGv 220
Cdd:PRK05690  92 RAALARINPHIAIETINARLDDDELAALI----------------AGHDLVLDCTDNVATRNQLNRACFAAK-KPLVSG- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 221 sedAV---SGHIQLLVPGETA-CFACAPPLVVASGIderTLKREGVCAAsLPttmGVVAGLLVQNSLKFLLNFGE--VSP 294
Cdd:PRK05690 154 ---AAirmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGR 223

                        250       260
                 ....*....|....*....|..
gi 334182302 295 YLGYNSLKDFFPTMKMRPNPQC 316
Cdd:PRK05690 224 LLLYDAMTMQFREMKLKRDPGC 245
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
62-317 7.14e-25

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 105.09  E-value: 7.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGIvDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAA 140
Cdd:PRK08762 116 YSRHLRLPEVGE-EGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRqILHTEDRVGQPKVDSA 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 141 VQTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGV 220
Cdd:PRK08762 195 AQRLAALNPDVQVEAVQERVTSDNVEALL----------------QDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAV 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 221 SEdaVSGHIQLLVPGETA----CFAC----APPLVVASGIDErtlkrEGVCAAsLPTTMGVvagLLVQNSLKFLLNFGEv 292
Cdd:PRK08762 259 FR--FEGQVSVFDAGRQRgqapCYRClfpePPPPELAPSCAE-----AGVLGV-LPGVIGL---LQATEAIKLLLGIGD- 326

                        250       260
                 ....*....|....*....|....*....
gi 334182302 293 sPYLG----YNSLKDFFPTMKMRPNPQCS 317
Cdd:PRK08762 327 -PLTGrlltFDALAMRFRELRLPPDPHCP 354
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 85-241 1.13e-24

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: 98.88  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  85 VAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAAVQTLAEINPDVvlesftmNITTV 163
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182302 164 qgFETFTSSLTNKSFCpskeggsGVDLVLSCVDNYEARMAVNQACNELRQTWMESGVSEDavSGHIQllVPGETACFA 241
Cdd:cd01483   75 --PEGISEDNLDDFLD-------GVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGL--GGDIQ--VIDIGSLSA 139
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 62-242 3.50e-24

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 102.38  E-value: 3.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR--LFFRPD-QVGMTKTD 138
Cdd:PRK07688   5 YSRQELFSPIG-EEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTESDvKNNLPKAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 139 AAVQTLAEINPDVVLESFTMNITTVQGFETFTssltnksfcpskeggsGVDLVLSCVDNYEARMAVNQACNELRQTWMES 218
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELVT----------------GVDLIIDATDNFETRFIVNDAAQKYGIPWIYG 147

                        170       180
                 ....*....|....*....|....*.
gi 334182302 219 GvsedAVS--GHIQLLVPGETACFAC 242
Cdd:PRK07688 148 A----CVGsyGLSYTIIPGKTPCLRC 169
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 75-212 4.40e-23

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: 97.46  E-value: 4.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  75 DNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRlffrpdQ-------VGMTKTDAAVQTLAEI 147
Cdd:COG1179   17 EGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR------QlhaldstVGRPKVEVMAERIRDI 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182302 148 NPDVvlesftmNITTVQGF---ETFTSSLTnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELR 212
Cdd:COG1179   91 NPDC-------EVTAIDEFvtpENADELLS-----------EDYDYVIDAIDSVSAKAALIAWCRRRG 140
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 62-242 1.43e-21

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 95.18  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  62 YSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR--LFFRPD-QVGMTKTD 138
Cdd:PRK12475   5 YSRQILFSGIG-EEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTEEDaKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 139 AAVQTLAEINPDVVLESFTMNItTVQGFETFTssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACNELRQTWMES 218
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDV-TVEELEELV---------------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYG 147

                        170       180
                 ....*....|....*....|....*
gi 334182302 219 G-VSEDAVSGHIqllVPGETACFAC 242
Cdd:PRK12475 148 GcVGSYGVTYTI---IPGKTPCLRC 169
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 75-203 1.55e-21

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: 92.67  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  75 DNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAAVQTLAEINPDVvl 153
Cdd:cd00755    4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRqIHALLSTVGKPKVEVMAERIRDINPEC-- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 334182302 154 esftmNITTVQGFetFTSSLTNKSFcpskegGSGVDLVLSCVDNYEARMA 203
Cdd:cd00755   82 -----EVDAVEEF--LTPDNSEDLL------GGDPDFVVDAIDSIRAKVA 118
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 85-244 5.32e-20

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: 90.13  E-value: 5.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  85 VAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEINPDVVLESFTMNITTV 163
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 164 Q-GFETFtssltnKSFcpskeggsgvDLVLSCVDNYEARMAVNQACNELRQTWMESGVSedAVSGHIQLLVPGETACFAC 242
Cdd:cd01489   82 DfNVEFF------KQF----------DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYEC 143


                 ..
gi 334182302 243 AP 244
Cdd:cd01489  144 QP 145
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 84-161 1.51e-19

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 85.51  E-value: 1.51e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182302  84 SVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLESFTMNIT 161
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKID 78
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 77-161 2.66e-19

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: 85.69  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302   77 YERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRPDQVGMTKTDAAVQTLAEINPDVVLESF 156
Cdd:TIGR02354  16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95


                  ....*
gi 334182302  157 TMNIT 161
Cdd:TIGR02354  96 DEKIT 100
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 84-245 8.58e-19

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: 84.94  E-value: 8.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  84 SVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEINPDVVLESFTMNITT 162
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 163 VQGF-ETFTSSLtnksfcpskeggsgvDLVLSCVDNYEARMAVNQACNELRQTWMESGVSedAVSGHIQLLVPGETACFA 241
Cdd:cd01484   81 EQDFnDTFFEQF---------------HIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIE 143


                 ....*.
gi 334182302 242 CA--PP 245
Cdd:cd01484  144 CTlyPP 149
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 63-323 2.72e-16

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 79.92  E-value: 2.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  63 SRLMALQRMGIvDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAAV 141
Cdd:PRK05600  23 ARQLALPGFGI-EQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 142 QTLAEINPDVVLESFTMNITTVQGFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQACnELRQTWMesgvs 221
Cdd:PRK05600 102 ERLKEIQPDIRVNALRERLTAENAVELL----------------NGVDLVLDGSDSFATKFLVADAA-EITGTPL----- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 222 edaVSGHIqLLVPGETACFACAPPlvvASGIDERTLKREGVCAASLP---------TTMGVVAGLLVQNSLKFLLNFGEV 292
Cdd:PRK05600 160 ---VWGTV-LRFHGELAVFNSGPD---HRGVGLRDLFPEQPSGDSIPdcatagvlgATTAVIGALMATEAIKFLTGIGDV 232

                        250       260       270
                 ....*....|....*....|....*....|...
gi 334182302 293 SP--YLGYNSLKDFFPTMKMRPNPQCSNVACLE 323
Cdd:PRK05600 233 QPgtVLSYDALTATTRSFRVGADPARPLVTRLR 265
PRK08328 PRK08328
hypothetical protein; Provisional
 74-291 2.10e-15

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 75.22  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  74 VDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR--LFFRPDQVGMTKTDAAVQTLAEINPDV 151
Cdd:PRK08328  19 VEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 152 VLesftmnittvqgfETFTSSLTNKSFcpsKEGGSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGVseDAVSGHIQL 231
Cdd:PRK08328  99 KI-------------ETFVGRLSEENI---DEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAV--EGTYGQVTT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 232 LVPGETACFacapplvvaSGIDERTLKREGVCAAsLPTTMGVVAGLLVQNSLKFLLNFGE 291
Cdd:PRK08328 161 IVPGKTKRL---------REIFPKVKKKKGKFPI-LGATAGVIGSIQAMEVIKLITGYGE 210
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 57-211 2.80e-15

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 76.83  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  57 VDSNPYSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMT 135
Cdd:PRK05597   4 LDIARYRRQIMLGEIG-QQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRqVIHSTAGVGQP 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182302 136 KTDAAVQTLAEINPDVvlesftmniTTVQGFETFTSSlTNKSFCpskeggSGVDLVLSCVDNYEARMAVNQACNEL 211
Cdd:PRK05597  83 KAESAREAMLALNPDV---------KVTVSVRRLTWS-NALDEL------RDADVILDGSDNFDTRHLASWAAARL 142
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 51-368 8.09e-14

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 72.43  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  51 ELSSEVVDSnpYSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRP 129
Cdd:PRK07878  14 ELTRDEVAR--YSRHLIIPDVG-VDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 130 DQVGMTKTDAAVQTLAEINP--DVVLESFTMNITTVqgFETFtssltnksfcpskeggSGVDLVLSCVDNYEARMAVNQA 207
Cdd:PRK07878  91 SDVGRSKAQSARDSIVEINPlvNVRLHEFRLDPSNA--VELF----------------SQYDLILDGTDNFATRYLVNDA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 208 CNELRQTWM-------ESGVS---EDAVSGHiqllvpgeTACFAC-----APPLVVASGIDERTLkreGVCAASLPTTMG 272
Cdd:PRK07878 153 AVLAGKPYVwgsiyrfEGQASvfwEDAPDGL--------GLNYRDlypepPPPGMVPSCAEGGVL---GVLCASIGSIMG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 273 VVAgllvqnsLKFLLNFGEvsPYLG----YNSLKDFFPTMKMRPNPQCSNVACLERQKEYMLAKPErDAAakakmEADAS 348
Cdd:PRK07878 222 TEA-------IKLITGIGE--PLLGrlmvYDALEMTYRTIKIRKDPSTPKITELIDYEAFCGVVSD-EAQ-----QAAAG 286

                        330       340
                 ....*....|....*....|..
gi 334182302 349 TTIDEGPLHD--DNEWNISVVD 368
Cdd:PRK07878 287 STITPRELKEwlDSGKKIALID 308
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
51-371 4.04e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 70.53  E-value: 4.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  51 ELSSEvvDSNPYSRLMALQRMGiVDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRP 129
Cdd:PRK07411  10 QLSKD--EYERYSRHLILPEVG-LEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 130 DQVGMTKTDAAVQTLAEINPdvvlesftmnITTVQGFETFTSSLTNKSFCPSkeggsgVDLVLSCVDNYEARMAVNQACN 209
Cdd:PRK07411  87 SWVGKPKIESAKNRILEINP----------YCQVDLYETRLSSENALDILAP------YDVVVDGTDNFPTRYLVNDACV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 210 ELrqtwmesgvSEDAVSGHIqLLVPGETACF-------------ACAPPLVVASGidertlkREGVCAASLPTTMGVVAG 276
Cdd:PRK07411 151 LL---------NKPNVYGSI-FRFEGQATVFnyeggpnyrdlypEPPPPGMVPSC-------AEGGVLGILPGIIGVIQA 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 277 llvQNSLKFLLNFGEV--SPYLGYNSLKDFFPTMKMRPNPQCSNVACLERQKEYMLAKPERDAAAKAKMEADASTTIDEG 354
Cdd:PRK07411 214 ---TETIKIILGAGNTlsGRLLLYNALDMKFRELKLRPNPERPVIEKLIDYEQFCGIPQAKAAEAAQKAEIPEMTVTELK 290

                        330
                 ....*....|....*..
gi 334182302 355 PLHDDNEWNISVVDDEN 371
Cdd:PRK07411 291 ALLDSGADDFVLIDVRN 307
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 85-150 1.14e-11

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 64.82  E-value: 1.14e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182302  85 VAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNR-LFFRPDQVGMTKTDAAVQTLAEINPD 150
Cdd:PRK15116  33 ICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRqIHALRDNVGLAKAEVMAERIRQINPE 99
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 78-245 5.51e-11

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: 64.91  E-value: 5.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302    78 ERIREFSVAIVGIGGVGsvaAEMLTRCGI--------GRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEIN 148
Cdd:TIGR01408  415 QKLQNLNIFLVGCGAIG---CEMLKNFALmgvgtgkkGMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKIN 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302   149 PdvvlesfTMNITTVQgfetftssltNKsFCPSKEGGSG------VDLVLSCVDNYEARMAVNQACNELRQTWMESGVSe 222
Cdd:TIGR01408  492 P-------QIKIDAHQ----------NR-VGPETETIFNdefyekLDVVINALDNVEARRYVDSRCLAFLKPLLESGTL- 552

                          170       180
                   ....*....|....*....|....*
gi 334182302   223 dAVSGHIQLLVPGETACFACA--PP 245
Cdd:TIGR01408  553 -GTKGNTQVVVPHLTESYGSSrdPP 576
PRK08223 PRK08223
hypothetical protein; Validated
 74-208 9.06e-11

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 62.39  E-value: 9.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  74 VDNYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRlffrpdQVGMTKT---DAAVQTLAE---- 146
Cdd:PRK08223  19 PTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNR------QAGAMMStlgRPKAEVLAEmvrd 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182302 147 INPDVVLESFTMNITTvQGFETFTssltnksfcpskeggSGVDLVLSCVD--NYEARMAVNQAC 208
Cdd:PRK08223  93 INPELEIRAFPEGIGK-ENADAFL---------------DGVDVYVDGLDffEFDARRLVFAAC 140
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 84-234 1.95e-10

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: 62.31  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  84 SVAIVGIGGVGsvaAEML---------TRCGiGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEINPDVvl 153
Cdd:cd01490    1 KVFLVGAGAIG---CELLknfalmgvgTGES-GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDL-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 154 esftmNITtvqgfetftsSLTNKsFCPSKEG------GSGVDLVLSCVDNYEARMAVNQACNELRQTWMESGVSedAVSG 227
Cdd:cd01490   75 -----KIT----------ALQNR-VGPETEHifndefWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKG 136


                 ....*..
gi 334182302 228 HIQLLVP 234
Cdd:cd01490  137 NTQVVIP 143
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 84-247 2.57e-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: 58.14  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  84 SVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEINPDVVLESFTMNITT 162
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302 163 VQgfETFTSSLTnksfcpskeggsgvdLVLSCVDNYEARMAVNQ-ACNELRQTWMES------GVSEdAVSGHIQLLVPG 235
Cdd:cd01488   81 KD--EEFYRQFN---------------IIICGLDSIEARRWINGtLVSLLLYEDPESiiplidGGTE-GFKGHARVILPG 142

                        170
                 ....*....|....*.
gi 334182302 236 ETACFAC----APPLV 247
Cdd:cd01488  143 ITACIECsldlFPPQV 158
PRK14851 PRK14851
hypothetical protein; Provisional
 78-207 1.39e-08

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 56.79  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  78 ERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLF-FRPDQVGMTKTDAAVQTLAEINPDVVLESF 156
Cdd:PRK14851  39 ERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFgARVPSFGRPKLAVMKEQALSINPFLEITPF 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334182302 157 TMNITTvQGFETFTssltnksfcpskeggSGVDLVLSCVDNYE---ARMAVNQA 207
Cdd:PRK14851 119 PAGINA-DNMDAFL---------------DGVDVVLDGLDFFQfeiRRTLFNMA 156
PRK14852 PRK14852
hypothetical protein; Provisional
 60-166 7.66e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 51.62  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  60 NPYSRLMALQRMGIVD--NYERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRP-DQVGMTK 136
Cdd:PRK14852 308 DAYTDIAFSRNLGLVDyaGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASiASFGRGK 387

                         90       100       110
                 ....*....|....*....|....*....|..
gi 334182302 137 TDAAVQTLAEINPDVVLESFTMNIT--TVQGF 166
Cdd:PRK14852 388 LDVMTERALSVNPFLDIRSFPEGVAaeTIDAF 419
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 57-167 9.83e-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: 51.04  E-value: 9.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302    57 VDSNPYSRLMAlqrmgiVDNYERIREFS---VAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANM-NRLFFRPDQV 132
Cdd:TIGR01408    2 IDEALYSRQLY------VLGDEAMQKMAksnVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLsSNFFLSEDDV 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 334182302   133 GMTKTDAAVQTLAEINPDVVLESFT--MNITTVQGFE 167
Cdd:TIGR01408   76 GRNRAEAVVKKLAELNPYVHVSSSSvpFNEEFLDKFQ 112
PRK07877 PRK07877
Rv1355c family protein;
78-166 3.81e-06

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 49.22  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  78 ERIREFSVAIVGIGgVGSVAAEMLTRCGI-GRLLLYDYDTVELANMNRLffrPDQV---GMTKTDAAVQTLAEINPDVVL 153
Cdd:PRK07877 103 ERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNRV---PAGVfdlGVNKAVVAARRIAELDPYLPV 178

                         90
                 ....*....|....*
gi 334182302 154 ESFTMNIT--TVQGF 166
Cdd:PRK07877 179 EVFTDGLTedNVDAF 193
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 79-179 4.75e-06

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 48.03  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  79 RIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFF-RPDQVGMTKTDAAVQTLAEINPDVVLESFT 157
Cdd:cd01491   16 KLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYlREEDIGKNRAEASQARLAELNPYVPVTVST 95

                         90       100
                 ....*....|....*....|..
gi 334182302 158 MNITTVQGFETFTSSLTNKSFC 179
Cdd:cd01491   96 GPLTTDELLKFQVVVLTDASLE 117
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 78-211 2.36e-04

Ubiquitin activating enzyme (E1), repeat 1-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. The 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 first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 42.02  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  78 ERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFFRP---DQVGMTKTDAAVQTLAEINPDVvle 154
Cdd:cd01485   15 NKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDaevSNSGMNRAAASYEFLQELNPNV--- 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334182302 155 sftmNITTVQGFETFTSSLTNKSFCPSkeggsgvDLVLSCVDNYEARMAVNQACNEL 211
Cdd:cd01485   92 ----KLSIVEEDSLSNDSNIEEYLQKF-------TLVIATEENYERTAKVNDVCRKH 137
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 78-162 6.71e-04

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 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. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 40.74  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182302  78 ERIREFSVAIVGIGGVGSVAAEMLTRCGIGRLLLYDYDTVELANMNRLFF-RPDQVGMTKTDAAVQTLAEINPDVVLESF 156
Cdd:cd01492   17 KRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLiPAEDLGQNRAEASLERLRALNPRVKVSVD 96


                 ....*.
gi 334182302 157 TMNITT 162
Cdd:cd01492   97 TDDISE 102
 
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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