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Conserved domains on  [gi|290463331|sp|B4L1K2|]
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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 ...
 45-290 1.70e-71

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: 223.51  E-value: 1.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  45 PYSRLMALQRMNIVKDyERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 123
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 124 AARTLSFINPDVVIETHNYNItTVENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSEn 203
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 204 aVSGHIQFIRPGETACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVSD--YLGYNAL 281
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463331 282 NDFFPKMTL 290
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 ...
 45-290 1.70e-71

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: 223.51  E-value: 1.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  45 PYSRLMALQRMNIVKDyERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 123
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 124 AARTLSFINPDVVIETHNYNItTVENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSEn 203
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 204 aVSGHIQFIRPGETACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVSD--YLGYNAL 281
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463331 282 NDFFPKMTL 290
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 46-296 3.56e-53

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: 176.68  E-value: 3.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331   46 YSRLMALQRMnIVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAA 124
Cdd:pfam00899   1 YSRQLALPLI-GEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  125 ARTLSFINPDVVIETHNYNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSenA 204
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  205 VSGHIQFIRPGETACFACAPPlvvaeNIDERTLKREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVS---DYLGYNAL 281
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDAL 220

                         250
                  ....*....|....*.
gi 290463331  282 NDFFPKMTLK-PNAEC 296
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-296 3.29e-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: 140.26  E-value: 3.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETH 140
Cdd:COG0476   23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 141 NYNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSEnaVSGHIQFIRPGETACF 220
Cdd:COG0476  103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290463331 221 ACAPPLVVAENIDERTlkregvcAASLPTTMGITAGLLVQNALKYLLNFGEVSD--YLGYNALNDFFPKMTLKPNAEC 296
Cdd:COG0476  169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
82-187 1.87e-20

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 88.76  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  82 ADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITTvENFDKFLttisesg 161
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100
                 ....*....|....*....|....*..
gi 290463331 162 lqkgQPVDLVLSCVDNFEA-RMAINAA 187
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETV 138
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 59-186 1.42e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 66.05  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331   59 KDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIE 138
Cdd:TIGR02354  14 KIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 290463331  139 THNYNITTvENFDKFLTTIsesglqkgqpvDLVLSCVDNFEAR-MAINA 186
Cdd:TIGR02354  94 AYDEKITE-ENIDKFFKDA-----------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 ...
 45-290 1.70e-71

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: 223.51  E-value: 1.70e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  45 PYSRLMALQRMNIVKDyERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEA 123
Cdd:cd00757    1 RYSRQILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 124 AARTLSFINPDVVIETHNYNItTVENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSEn 203
Cdd:cd00757   80 AAERLRAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 204 aVSGHIQFIRPGETACFACAPPLVVAENIdertlkREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVSD--YLGYNAL 281
Cdd:cd00757  147 -FEGQVTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAgrLLLFDAL 219


                 ....*....
gi 290463331 282 NDFFPKMTL 290
Cdd:cd00757  220 SMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 46-296 3.56e-53

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: 176.68  E-value: 3.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331   46 YSRLMALQRMnIVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAA 124
Cdd:pfam00899   1 YSRQLALPLI-GEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  125 ARTLSFINPDVVIETHNYNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSenA 204
Cdd:pfam00899  80 AERLREINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--G 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  205 VSGHIQFIRPGETACFACAPPlvvaeNIDERTLKREGVCAASLPTTMGITAGLLVQNALKYLLNFGEVS---DYLGYNAL 281
Cdd:pfam00899 146 FKGQVTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlagRLLQFDAL 220

                         250
                  ....*....|....*.
gi 290463331  282 NDFFPKMTLK-PNAEC 296
Cdd:pfam00899 221 TMTFRELRLAlKNPNC 236
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 62-296 3.29e-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: 140.26  E-value: 3.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETH 140
Cdd:COG0476   23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 141 NYNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSEnaVSGHIQFIRPGETACF 220
Cdd:COG0476  103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290463331 221 ACAPPLVVAENIDERTlkregvcAASLPTTMGITAGLLVQNALKYLLNFGEVSD--YLGYNALNDFFPKMTLKPNAEC 296
Cdd:COG0476  169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
82-187 1.87e-20

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 88.76  E-value: 1.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  82 ADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITTvENFDKFLttisesg 161
Cdd:PRK08644  44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115

                         90       100
                 ....*....|....*....|....*..
gi 290463331 162 lqkgQPVDLVLSCVDNFEA-RMAINAA 187
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETV 138
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 62-222 3.34e-19

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 87.74  E-value: 3.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR--LFFTPD-QAGLSKVEAAARTLSFINPDVVIE 138
Cdd:PRK07688  20 QKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTESDvKNNLPKAVAAKKRLEEINSDVRVE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 139 THNYNItTVENFDKFLTTisesglqkgqpVDLVLSCVDNFEARMAINAACNENNLNWFESGvsenAVS--GHIQFIRPGE 216
Cdd:PRK07688 100 AIVQDV-TAEELEELVTG-----------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGK 163


                 ....*.
gi 290463331 217 TACFAC 222
Cdd:PRK07688 164 TPCLRC 169
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 69-201 1.12e-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: 79.23  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  69 VAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITTV 147
Cdd:cd01483    2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISED 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 290463331 148 ENFDKFLttisesglqkgqPVDLVLSCVDNFEARMAINAACNENNLNWFESGVS 201
Cdd:cd01483   82 NLDDFLD------------GVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL 123
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 62-199 6.24e-17

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: 79.19  E-value: 6.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETH 140
Cdd:cd00755    7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRqIHALLSTVGKPKVEVMAERIRDINPECEVDAV 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 290463331 141 NYNITTvENFDKFLttisesglqkGQPVDLVLSCVDNFEARMAINAACNENNLNWFESG 199
Cdd:cd00755   87 EEFLTP-DNSEDLL----------GGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSM 134
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 46-222 7.03e-17

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 80.93  E-value: 7.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  46 YSRLMALQRMNiVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR--LFFTPD-QAGLSKVE 122
Cdd:PRK12475   5 YSRQILFSGIG-EEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTEEDaKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 123 AAARTLSFINPDVVIETHNYNItTVENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESG-VS 201
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDV-TVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVG 151

                        170       180
                 ....*....|....*....|.
gi 290463331 202 ENAVSghiQFIRPGETACFAC 222
Cdd:PRK12475 152 SYGVT---YTIIPGKTPCLRC 169
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
63-296 5.00e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 78.90  E-value: 5.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  63 RIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETHN 141
Cdd:PRK08762 132 RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRqILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQ 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 142 YNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNE-------NNLNWFESGVSENAVSGHiqfirP 214
Cdd:PRK08762 212 ERVTS-DNVEALL-----------QDVDVVVDGADNFPTRYLLNDACVKlgkplvyGAVFRFEGQVSVFDAGRQ-----R 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 215 GETACFAC----APPLVVAENIDErtlkrEGVCAAsLPTTMGItagLLVQNALKYLLNFGE--VSDYLGYNALNDFFPKM 288
Cdd:PRK08762 275 GQAPCYRClfpePPPPELAPSCAE-----AGVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFREL 345


                 ....*...
gi 290463331 289 TLKPNAEC 296
Cdd:PRK08762 346 RLPPDPHC 353
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 46-296 1.00e-15

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 76.04  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  46 YSRLMALQRMNIVKDyERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQA-GLSKVEAA 124
Cdd:PRK05690  13 YNRQIILRGFDFDGQ-EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATiGQPKVESA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 125 ARTLSFINPDVVIETHNYNITTvENFDKFLTTisesglqkgqpVDLVLSCVDNFEARMAINAACnennlnwFESG---VS 201
Cdd:PRK05690  92 RAALARINPHIAIETINARLDD-DELAALIAG-----------HDLVLDCTDNVATRNQLNRAC-------FAAKkplVS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 202 ENAV--SGHIQFIRPGETA-CFACAPPLVVAENIderTLKREGVCAAsLPttmGITAGLLVQNALKYLLNFGE--VSDYL 276
Cdd:PRK05690 153 GAAIrmEGQVTVFTYQDDEpCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLL 225

                        250       260
                 ....*....|....*....|
gi 290463331 277 GYNALNDFFPKMTLKPNAEC 296
Cdd:PRK05690 226 LYDAMTMQFREMKLKRDPGC 245
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 62-193 2.50e-13

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: 69.34  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETH 140
Cdd:COG1179   20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRqLHALDSTVGRPKVEVMAERIRDINPDCEVTAI 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 290463331 141 NYNITTvENFDKFLTtisesglqkgQPVDLVLSCVDNFEARMAINAACNENNL 193
Cdd:COG1179  100 DEFVTP-ENADELLS----------EDYDYVIDAIDSVSAKAALIAWCRRRGI 141
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 89-225 1.31e-12

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 66.83  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  89 GIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITTVENF-DKFLttisesglqkgQ 166
Cdd:cd01484   22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFnDTFF-----------E 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290463331 167 PVDLVLSCVDNFEARMAINAACNENNLNWFESGVSenAVSGHIQFIRPGETACFACA--PP 225
Cdd:cd01484   91 QFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 59-186 1.42e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 66.05  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331   59 KDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIE 138
Cdd:TIGR02354  14 KIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 290463331  139 THNYNITTvENFDKFLTTIsesglqkgqpvDLVLSCVDNFEAR-MAINA 186
Cdd:TIGR02354  94 AYDEKITE-ENIDKFFKDA-----------DIVCEAFDNAEAKaMLVNA 130
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 69-152 5.07e-12

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 63.94  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  69 VAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITT-- 146
Cdd:cd01487    2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEnn 81

                         90
                 ....*....|....*..
gi 290463331 147 -----------VENFDK 152
Cdd:cd01487   82 leglfgdcdivVEAFDN 98
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 75-224 1.88e-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: 64.32  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  75 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITT----VEN 149
Cdd:cd01489    8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463331 150 FDKFlttisesglqkgqpvDLVLSCVDNFEARMAINAACNENNLNWFESGVSenAVSGHIQFIRPGETACFACAP 224
Cdd:cd01489   88 FKQF---------------DLVFNALDNLAARRHVNKMCLAADVPLIESGTT--GFLGQVQVIKKGKTECYECQP 145
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 41-181 1.70e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 55.65  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  41 VDSNPYSRLMALQRMNIVKDyERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLS 119
Cdd:PRK05597   4 LDIARYRRQIMLGEIGQQGQ-QSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRqVIHSTAGVGQP 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 290463331 120 KVEAAARTLSFINPDVVIETHNYNITtvenFDKFLTTISESglqkgqpvDLVLSCVDNFEAR 181
Cdd:PRK05597  83 KAESAREAMLALNPDVKVTVSVRRLT----WSNALDELRDA--------DVILDGSDNFDTR 132
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 91-214 1.86e-08

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: 55.76  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  91 GKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLSFINPDVVIETHNYNI-TTVENF--DKFLTTisesglqkgq 166
Cdd:cd01490   29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgPETEHIfnDEFWEK---------- 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 290463331 167 pVDLVLSCVDNFEARMAINAACNENNLNWFESGVSenAVSGHIQFIRP 214
Cdd:cd01490   99 -LDGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
PRK08328 PRK08328
hypothetical protein; Provisional
 62-217 2.20e-08

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 54.42  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR--LFFTPDQAGLSKVEAAARTLSFINPDVVIET 139
Cdd:PRK08328  23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 290463331 140 HnYNITTVENFDKFLttisesglqkgQPVDLVLSCVDNFEARMAINAACNENNLNWFESGVSenAVSGHIQFIRPGET 217
Cdd:PRK08328 103 F-VGRLSEENIDEVL-----------KGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKT 166
PRK08223 PRK08223
hypothetical protein; Validated
 62-188 2.35e-08

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 55.07  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLSFINPDVVIETH 140
Cdd:PRK08223  23 QRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAgAMMSTLGRPKAEVLAEMVRDINPELEIRAF 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 290463331 141 NYNITTvENFDKFLttisesglqkgQPVDLVLSCVDNFE--ARMAINAAC 188
Cdd:PRK08223 103 PEGIGK-ENADAFL-----------DGVDVYVDGLDFFEfdARRLVFAAC 140
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 91-225 4.07e-08

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: 55.28  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331    91 GKLILFDYDKVELANMNRLF-FTPDQAGLSKVEAAARTLSFINPDVVIETHNYNI-TTVENF--DKFLTTIsesglqkgq 166
Cdd:TIGR01408  449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETIfnDEFYEKL--------- 519

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 290463331   167 pvDLVLSCVDNFEARMAINAACNENNLNWFESGVSenAVSGHIQFIRPGETACFACA--PP 225
Cdd:TIGR01408  520 --DVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVPHLTESYGSSrdPP 576
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 85-181 6.36e-08

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 54.12  E-value: 6.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  85 LTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNITtvenfdkflttiSESGLQ 163
Cdd:PRK05600  60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127

                         90
                 ....*....|....*...
gi 290463331 164 KGQPVDLVLSCVDNFEAR 181
Cdd:PRK05600 128 LLNGVDLVLDGSDSFATK 145
PRK07877 PRK07877
Rv1355c family protein;
91-155 1.37e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.74  E-value: 1.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 290463331  91 GKLILFDYDKVELANMNRLFFTPDQAGLSKVEAAARTLSFINPDVVIETHNYNItTVENFDKFLT 155
Cdd:PRK07877 132 GELRLADFDTLELSNLNRVPAGVFDLGVNKAVVAARRIAELDPYLPVEVFTDGL-TEDNVDAFLD 195
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
46-318 1.51e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 40.49  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  46 YSRLMALQRMNiVKDYERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAA 124
Cdd:PRK07411  19 YSRHLILPEVG-LEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 125 ARTLSFINPDVVIETHNYNITtvenfdkflttiSESGLQKGQPVDLVLSCVDNFEARMAINAAC---NENNlnwfesgvs 201
Cdd:PRK07411  98 KNRILEINPYCQVDLYETRLS------------SENALDILAPYDVVVDGTDNFPTRYLVNDACvllNKPN--------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331 202 enaVSGHIqFIRPGETACF-------------ACAPPLVVAENidertlkREGVCAASLPttmGITAGLLVQNALKYLLN 268
Cdd:PRK07411 157 ---VYGSI-FRFEGQATVFnyeggpnyrdlypEPPPPGMVPSC-------AEGGVLGILP---GIIGVIQATETIKIILG 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 290463331 269 FGEV--SDYLGYNALNDFFPKMTLKPNAECDDRYCLQRQKEFQARPQPKEQQ 318
Cdd:PRK07411 223 AGNTlsGRLLLYNALDMKFRELKLRPNPERPVIEKLIDYEQFCGIPQAKAAE 274
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 75-191 2.24e-03

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 39.40  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  75 GGVGSVTADMLTRCGIGKLILFDYDKVELANMNR-LFFTPDQAGLSKVEAAARTLSFINPDVviethnyNITTVenfDKF 153
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRqIHALRDNVGLAKAEVMAERIRQINPEC-------RVTVV---DDF 108

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 290463331 154 LTTISESGLQKGQpVDLVLSCVDNFEARMAINAACNEN 191
Cdd:PRK15116 109 ITPDNVAEYMSAG-FSYVIDAIDSVRPKAALIAYCRRN 145
PRK14851 PRK14851
hypothetical protein; Provisional
 62-187 3.46e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 39.46  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 290463331  62 ERIRDKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLF--FTPDqAGLSKVEAAARTLSFINPDVVIET 139
Cdd:PRK14851  39 ERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFgaRVPS-FGRPKLAVMKEQALSINPFLEITP 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 290463331 140 HNYNITTvENFDKFLTTisesglqkgqpVDLVLSCVDNFE---ARMAINAA 187
Cdd:PRK14851 118 FPAGINA-DNMDAFLDG-----------VDVVLDGLDFFQfeiRRTLFNMA 156
 
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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