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Conserved domains on  [gi|290463335|sp|B4NDE5|]
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RecName: Full=Ubiquitin-like modifier-activating enzyme 5; Short=Ubiquitin-activating enzyme 5

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 ...
 51-296 1.93e-68

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


:

Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 216.19  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  51 PYSRLMALQRMNIVKDyERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 129
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 130 AARTLTFINPDVKIETHNYNITTvdnfDNFLTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGVSEn 209
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDA----ENAEELIAG--------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 210 aVSGHIQFIRPGDTACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSD--YLGYNAL 287
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463335 288 NDFFPKMTL 296
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 ...
 51-296 1.93e-68

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


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 216.19  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  51 PYSRLMALQRMNIVKDyERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 129
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 130 AARTLTFINPDVKIETHNYNITTvdnfDNFLTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGVSEn 209
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDA----ENAEELIAG--------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 210 aVSGHIQFIRPGDTACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSD--YLGYNAL 287
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463335 288 NDFFPKMTL 296
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 52-302 1.63e-51

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: 172.83  E-value: 1.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335   52 YSRLMALQRMnIVKDYERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAA 130
Cdd:pfam00899   1 YSRQLALPLI-GEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  131 ARTLTFINPDVKIETHNYNITTvDNFDNFLttisqsgtepgTPVDLILSCVDNFEARMAINAACNEHSLNWFESGVSenA 210
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  211 VSGHIQFIRPGDTACFACAPPlvvaeNIDERTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVS---DYLGYNAL 287
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDAL 220

                         250
                  ....*....|....*.
gi 290463335  288 NDFFPKMTLK-PNPQC 302
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 81-302 2.86e-39

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: 140.65  E-value: 2.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvdnfDNF 159
Cdd:COG0476   36 GGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE----ENA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 160 LTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGVSEnaVSGHIQFIRPGDTACFACAPPLVVAENID 239
Cdd:COG0476  112 LELLAG--------ADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPS 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463335 240 ERTlkregvcAASLPTTMGITAGFLVQNALKYLLNFGEVSD--YLGYNALNDFFPKMTLKPNPQC 302
Cdd:COG0476  182 CAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
88-197 2.90e-20

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 88.37  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  88 ADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNFLttisqsg 167
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|
gi 290463335 168 tepgTPVDLILSCVDNFEARMAINAACNEH 197
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETKAMLVETVLEH 141
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 91-192 3.35e-11

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 62.19  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335   91 LTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNFLTTIsqsgtep 170
Cdd:TIGR02354  40 LARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAYDEKITE-ENIDKFFKDA------- 111

                          90       100
                  ....*....|....*....|...
gi 290463335  171 gtpvDLILSCVDNFEAR-MAINA 192
Cdd:TIGR02354 112 ----DIVCEAFDNAEAKaMLVNA 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 ...
 51-296 1.93e-68

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


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 216.19  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  51 PYSRLMALQRMNIVKDyERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 129
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 130 AARTLTFINPDVKIETHNYNITTvdnfDNFLTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGVSEn 209
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERLDA----ENAEELIAG--------YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 210 aVSGHIQFIRPGDTACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSD--YLGYNAL 287
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463335 288 NDFFPKMTL 296
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 52-302 1.63e-51

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: 172.83  E-value: 1.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335   52 YSRLMALQRMnIVKDYERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAA 130
Cdd:pfam00899   1 YSRQLALPLI-GEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  131 ARTLTFINPDVKIETHNYNITTvDNFDNFLttisqsgtepgTPVDLILSCVDNFEARMAINAACNEHSLNWFESGVSenA 210
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  211 VSGHIQFIRPGDTACFACAPPlvvaeNIDERTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVS---DYLGYNAL 287
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDAL 220

                         250
                  ....*....|....*.
gi 290463335  288 NDFFPKMTLK-PNPQC 302
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 81-302 2.86e-39

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: 140.65  E-value: 2.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvdnfDNF 159
Cdd:COG0476   36 GGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTE----ENA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 160 LTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGVSEnaVSGHIQFIRPGDTACFACAPPLVVAENID 239
Cdd:COG0476  112 LELLAG--------ADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCYRCLFPEPPEPGPS 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463335 240 ERTlkregvcAASLPTTMGITAGFLVQNALKYLLNFGEVSD--YLGYNALNDFFPKMTLKPNPQC 302
Cdd:COG0476  182 CAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
88-197 2.90e-20

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 88.37  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  88 ADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNFLttisqsg 167
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100       110
                 ....*....|....*....|....*....|
gi 290463335 168 tepgTPVDLILSCVDNFEARMAINAACNEH 197
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETKAMLVETVLEH 141
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 91-302 4.94e-19

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 85.67  E-value: 4.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  91 LTRCGIGKLILFDYDKVELANMNRLFFTPDQA-GLSKVEAAARTLTFINPDVKIETHNYNITTvdnfDNFLTTISQsgte 169
Cdd:PRK05690  51 LAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATiGQPKVESARAALARINPHIAIETINARLDD----DELAALIAG---- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 170 pgtpVDLILSCVDNFEARMAINAACNEHS--LnwfesgVSENAV--SGHIQFIRPGDTA-CFACAPPLVVAENIderTLK 244
Cdd:PRK05690 123 ----HDLVLDCTDNVATRNQLNRACFAAKkpL------VSGAAIrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCV 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290463335 245 REGVCAAsLPTTMGItagflVQ--NALKYLLNFGE--VSDYLGYNALNDFFPKMTLKPNPQC 302
Cdd:PRK05690 190 EAGVMAP-LVGVIGS-----LQamEAIKLLTGYGEplSGRLLLYDAMTMQFREMKLKRDPGC 245
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 88-228 1.78e-17

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 82.73  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  88 ADMLTRCGIGKLILFDYDKVELANMNR--LFFTPD-QAGLSKVEAAARTLTFINPDVKIETHNYNItTVDNFDNFLTTis 164
Cdd:PRK07688  40 AEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTESDvKNNLPKAVAAKKRLEEINSDVRVEAIVQDV-TAEELEELVTG-- 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 290463335 165 qsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESGvsenAVS--GHIQFIRPGDTACFAC 228
Cdd:PRK07688 117 ---------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGKTPCLRC 169
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
81-302 1.79e-17

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 83.14  E-value: 1.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvdnfDNF 159
Cdd:PRK08762 144 GGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRqILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTS----DNV 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 160 LTTISQsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNwfesgVSENAV---SGHIQFIRPGDTA----CFAC---- 228
Cdd:PRK08762 220 EALLQD--------VDVVVDGADNFPTRYLLNDACVKLGKP-----LVYGAVfrfEGQVSVFDAGRQRgqapCYRClfpe 286

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290463335 229 APPLVVAENIDErtlkrEGVCAAsLPTTMGitagfLVQ--NALKYLLNFGE--VSDYLGYNALNDFFPKMTLKPNPQC 302
Cdd:PRK08762 287 PPPPELAPSCAE-----AGVLGV-LPGVIG-----LLQatEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDPHC 353
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 81-207 4.34e-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: 77.31  E-value: 4.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTVDNFDNF 159
Cdd:cd01483    8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 290463335 160 LttisqsgtepgtPVDLILSCVDNFEARMAINAACNEHSLNWFESGVS 207
Cdd:cd01483   88 D------------GVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL 123
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 52-228 2.15e-14

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 73.61  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  52 YSRLMALQRMNiVKDYERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR--LFFTPD-QAGLSKVE 128
Cdd:PRK12475   5 YSRQILFSGIG-EEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTEEDaKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 129 AAARTLTFINPDVKIETHNYNItTVDNFDNFLTTisqsgtepgtpVDLILSCVDNFEARMAINAACNEHSLNWFESG-VS 207
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDV-TVEELEELVKE-----------VDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVG 151

                        170       180
                 ....*....|....*....|.
gi 290463335 208 ENAVSghiQFIRPGDTACFAC 228
Cdd:PRK12475 152 SYGVT---YTIIPGKTPCLRC 169
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 81-205 1.15e-13

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: 69.94  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNF 159
Cdd:cd00755   20 GGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRqIHALLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTP-DNSEDL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 290463335 160 LttisqsgtepGTPVDLILSCVDNFEARMAINAACNEHSLNWFESG 205
Cdd:cd00755   99 L----------GGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSM 134
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 88-151 1.97e-13

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: 68.18  E-value: 1.97e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 290463335  88 ADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNIT 151
Cdd:cd01487   15 AVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKID 78
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 91-192 3.35e-11

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 62.19  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335   91 LTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNFLTTIsqsgtep 170
Cdd:TIGR02354  40 LARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAYDEKITE-ENIDKFFKDA------- 111

                          90       100
                  ....*....|....*....|...
gi 290463335  171 gtpvDLILSCVDNFEAR-MAINA 192
Cdd:TIGR02354 112 ----DIVCEAFDNAEAKaMLVNA 130
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 81-230 3.80e-11

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: 63.55  E-value: 3.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITT----VDN 155
Cdd:cd01489    8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463335 156 FDNFlttisqsgtepgtpvDLILSCVDNFEARMAINAACNEHSLNWFESGVSenAVSGHIQFIRPGDTACFACAP 230
Cdd:cd01489   88 FKQF---------------DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 81-231 8.86e-11

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: 61.44  E-value: 8.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTVDNF-DN 158
Cdd:cd01484    8 GGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFnDT 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463335 159 FLTTIsqsgtepgtpvDLILSCVDNFEARMAINAACNEHSLNWFESGVSenAVSGHIQFIRPGDTACFACA--PP 231
Cdd:cd01484   88 FFEQF-----------HIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 81-197 2.40e-10

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: 60.48  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNF 159
Cdd:COG1179   33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRqLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTP-ENADEL 111

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 290463335 160 LTtisqsgtepgTPVDLILSCVDNFEARMAINAACNEH 197
Cdd:COG1179  112 LS----------EDYDYVIDAIDSVSAKAALIAWCRRR 139
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 97-220 1.85e-09

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: 59.23  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  97 GKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLTFINPDVKIETHNYNI--TTVDNF-DNFLTTisqsgtepgt 172
Cdd:cd01490   29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgpETEHIFnDEFWEK---------- 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 290463335 173 pVDLILSCVDNFEARMAINAACNEHSLNWFESGVSenAVSGHIQFIRP 220
Cdd:cd01490   99 -LDGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 91-233 2.25e-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: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  91 LTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARtltFIN---PDVKIETHNYNITTVDnfDNFLTTISqs 166
Cdd:cd01488   18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAK---FVNdrvPGVNVTPHFGKIQDKD--EEFYRQFN-- 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290463335 167 gtepgtpvdLILSCVDNFEARMAINA-AC------NEHSLNWFESGVSEnAVSGHIQFIRPGDTACFAC----APPLV 233
Cdd:cd01488   91 ---------IIICGLDSIEARRWINGtLVslllyeDPESIIPLIDGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
PRK08223 PRK08223
hypothetical protein; Validated
 88-194 3.28e-08

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 54.30  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  88 ADMLT--RCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvDNFDNFLTTis 164
Cdd:PRK08223  41 IHLLTlaRLGIGKFTIADFDVFELRNFNRQAgAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFLDG-- 117

                         90       100       110
                 ....*....|....*....|....*....|..
gi 290463335 165 qsgtepgtpVDLILSCVDNFE--ARMAINAAC 194
Cdd:PRK08223 118 ---------VDVYVDGLDFFEfdARRLVFAAC 140
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 47-187 3.46e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 54.88  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  47 VDSNPYSRLMALQRMNIVKDyERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLS 125
Cdd:PRK05597   4 LDIARYRRQIMLGEIGQQGQ-QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRqVIHSTAGVGQP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290463335 126 KVEAAARTLTFINPDVKIETHNYNITtvdnFDNFLTTISQSgtepgtpvDLILSCVDNFEAR 187
Cdd:PRK05597  83 KAESAREAMLALNPDVKVTVSVRRLT----WSNALDELRDA--------DVILDGSDNFDTR 132
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 97-220 2.95e-07

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 52.58  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335    97 GKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLTFINPDVKIETHNYNI--TTVDNFDNflttisqsgtEPGTP 173
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgpETETIFND----------EFYEK 518

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 290463335   174 VDLILSCVDNFEARMAINAAC--NEHSLnwFESGVSenAVSGHIQFIRP 220
Cdd:TIGR01408  519 LDVVINALDNVEARRYVDSRClaFLKPL--LESGTL--GTKGNTQVVVP 563
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 40-300 7.88e-07

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 50.65  E-value: 7.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  40 DRMSAEVVDSNPYSRLMALQRMNIvKDYERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFT 118
Cdd:PRK05600  10 PFMQLPTSELRRTARQLALPGFGI-EQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRqILFG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 119 PDQAGLSKVEAAARTLTFINPDVKIETHNYNIT-------------TVDNFDNFLTT--ISQSGTEPGTPvdLILSCVDN 183
Cdd:PRK05600  89 ASDVGRPKVEVAAERLKEIQPDIRVNALRERLTaenavellngvdlVLDGSDSFATKflVADAAEITGTP--LVWGTVLR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 184 FEARMAInaacnehslnwFESGVSENAVSGHIQF-IRPGDTACFACAPplvvaenidertlkregvcAASLPTTMGITAG 262
Cdd:PRK05600 167 FHGELAV-----------FNSGPDHRGVGLRDLFpEQPSGDSIPDCAT-------------------AGVLGATTAVIGA 216

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 290463335 263 FLVQNALKYLLNFGEV--SDYLGYNALNDFFPKMTLKPNP 300
Cdd:PRK05600 217 LMATEAIKFLTGIGDVqpGTVLSYDALTATTRSFRVGADP 256
PRK08328 PRK08328
hypothetical protein; Provisional
 68-187 8.16e-07

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 49.79  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  68 ERIREKTVAVVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR--LFFTPDQAGLSKVEAAARTLTFINPDVKIET 145
Cdd:PRK08328  23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 290463335 146 HnYNITTVDNFDNFLTTisqsgtepgtpVDLILSCVDNFEAR 187
Cdd:PRK08328 103 F-VGRLSEENIDEVLKG-----------VDVIVDCLDNFETR 132
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 81-197 2.07e-04

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 42.87  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKiethnynITTVDNF--- 156
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRqIHALRDNVGLAKAEVMAERIRQINPECR-------VTVVDDFitp 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 290463335 157 DNFLTTISQSgtepgtpVDLILSCVDNFEARMAINAACNEH 197
Cdd:PRK15116 112 DNVAEYMSAG-------FSYVIDAIDSVRPKAALIAYCRRN 145
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 81-302 2.50e-04

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 42.77  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335  81 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNITTvdnfDNF 159
Cdd:PRK07878  51 GGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDP----SNA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 160 LTTISQsgtepgtpVDLILSCVDNFEARMAINAAC-------NEHSLNWFESGVS---ENAVSGHiqfirpgdTACFAC- 228
Cdd:PRK07878 127 VELFSQ--------YDLILDGTDNFATRYLVNDAAvlagkpyVWGSIYRFEGQASvfwEDAPDGL--------GLNYRDl 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463335 229 ----APPLVVAENIDERTLkreGVCAASLPTTMgitagflVQNALKYLLNFGE--VSDYLGYNALNDFFPKMTLKPNPQC 302
Cdd:PRK07878 191 ypepPPPGMVPSCAEGGVL---GVLCASIGSIM-------GTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKDPST 260
PRK07877 PRK07877
Rv1355c family protein;
97-161 3.84e-04

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 42.67  E-value: 3.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463335  97 GKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLTFINPDVKIETHNYNItTVDNFDNFLT 161
Cdd:PRK07877 132 GELRLADFDTLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPYLPVEVFTDGL-TEDNVDAFLD 195
 
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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