|
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 ... |
1-241 |
2.28e-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: 213.88 E-value: 2.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 1 MALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTL 79
Cdd:cd00757 6 ILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 80 RNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGH 159
Cdd:cd00757 85 RAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 160 IQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFP 237
Cdd:cd00757 151 VTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFR 224
|
....
gi 38327032 238 TMSM 241
Cdd:cd00757 225 TLKL 228
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
1-247 |
1.66e-50 |
|
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: 168.20 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 1 MALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTL 79
Cdd:pfam00899 5 LALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 80 RNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGH 159
Cdd:pfam00899 84 REINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 160 IQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFF 236
Cdd:pfam00899 150 VTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTF 224
|
250
....*....|..
gi 38327032 237 PTMSMK-PNPQC 247
Cdd:pfam00899 225 RELRLAlKNPNC 236
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-247 |
2.91e-32 |
|
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 120.62 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:COG0476 23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACF 171
Cdd:COG0476 103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38327032 172 ACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 247
Cdd:COG0476 169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
|
|
| PRK08644 |
PRK08644 |
sulfur carrier protein ThiS adenylyltransferase ThiF; |
33-143 |
3.79e-19 |
|
sulfur carrier protein ThiS adenylyltransferase ThiF;
Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 84.52 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 33 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 112
Cdd:PRK08644 44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115
|
90 100 110
....*....|....*....|....*....|..
gi 38327032 113 leegKPVDLVLSCVDNFEA-RMTINTACNELG 143
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
|
|
| thiF_fam2 |
TIGR02354 |
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
12-137 |
2.18e-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: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 12 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:TIGR02354 16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 38327032 92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 137
Cdd:TIGR02354 96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiF_MoeB_HesA_family |
cd00757 |
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
1-241 |
2.28e-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: 213.88 E-value: 2.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 1 MALKRMGIVSDyEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTL 79
Cdd:cd00757 6 ILLPEIGEEGQ-EKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqILHTEADVGQPKAEAAAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 80 RNINPDVLFEVHNYNItTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGH 159
Cdd:cd00757 85 RAINPDVEIEAYNERL-DAENAEELI-----------AGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLG--FEGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 160 IQLIIPGESACFACAPPLVVAANIdektlkREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFP 237
Cdd:cd00757 151 VTVFIPGEGPCYRCLFPEPPPPGV------PSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlaGRLLLFDALSMSFR 224
|
....
gi 38327032 238 TMSM 241
Cdd:cd00757 225 TLKL 228
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
1-247 |
1.66e-50 |
|
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: 168.20 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 1 MALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTL 79
Cdd:pfam00899 5 LALPLIG-EDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFlFREADIGKPKAEVAAERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 80 RNINPDVLFEVHNYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGH 159
Cdd:pfam00899 84 REINPDVEVEAYTERLTP-ENAEELI-----------KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVL--GFKGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 160 IQLIIPGESACFACAPPlvvaaNIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSF---YLGYNAMQDFF 236
Cdd:pfam00899 150 VTVVIPGKTPCYRCLFP-----EDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNLagrLLQFDALTMTF 224
|
250
....*....|..
gi 38327032 237 PTMSMK-PNPQC 247
Cdd:pfam00899 225 RELRLAlKNPNC 236
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
13-247 |
2.91e-32 |
|
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440244 [Multi-domain] Cd Length: 244 Bit Score: 120.62 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:COG0476 23 EKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRqILYTEADVGRPKVEAAAERLRALNPDVEVEAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESACF 171
Cdd:COG0476 103 PERLTE-ENALELL-----------AGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIG--FEGQVTVFIPGDTPCY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38327032 172 ACAPPLVVAANIDEKTlkregvcAASLPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNPQC 247
Cdd:COG0476 169 RCLFPEPPEPGPSCAE-------AGVLGPLVGVIGSLQATEAIKLLTGIGEPLAgrLLLFDALTMEFRTIKLPRDPDC 239
|
|
| PRK08644 |
PRK08644 |
sulfur carrier protein ThiS adenylyltransferase ThiF; |
33-143 |
3.79e-19 |
|
sulfur carrier protein ThiS adenylyltransferase ThiF;
Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 84.52 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 33 AEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMdrisngg 112
Cdd:PRK08644 44 AVALARSGVGNLKLVDFDVVEPSNLNRQQYFISQIGMPKVEALKENLLEINPFVEIEAHNEKIDE-DNIEELF------- 115
|
90 100 110
....*....|....*....|....*....|..
gi 38327032 113 leegKPVDLVLSCVDNFEA-RMTINTACNELG 143
Cdd:PRK08644 116 ----KDCDIVVEAFDNAETkAMLVETVLEHPG 143
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
33-173 |
1.53e-18 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 85.04 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 33 AEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNItTVENFQHFMDRis 109
Cdd:PRK07688 40 AEMLVRAGVGKVTIVDRDYVEWSNLQRqqLYTeSDVKNNLPKAVAAKKRLEEINSDVRVEAIVQDV-TAEELEELVTG-- 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38327032 110 nggleegkpVDLVLSCVDNFEARMTINTACNELGQTWMESGvsenAVS--GHIQLIIPGESACFAC 173
Cdd:PRK07688 117 ---------VDLIIDATDNFETRFIVNDAAQKYGIPWIYGA----CVGsyGLSYTIIPGKTPCLRC 169
|
|
| E1_enzyme_family |
cd01483 |
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
20-170 |
7.75e-16 |
|
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.
Pssm-ID: 238760 [Multi-domain] Cd Length: 143 Bit Score: 73.46 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVlfevhnyNITTV 98
Cdd:cd01483 2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRqFLARQADIGKPKAEVAARRLNELNPGV-------NVTAV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38327032 99 EnfqhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESAC 170
Cdd:cd01483 75 P------EGISEDNLDDfLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGL--GLGGDIQVIDIGSLSA 139
|
|
| PRK12475 |
PRK12475 |
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
13-173 |
9.00e-15 |
|
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 74.38 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFF-QPHQAGLSKVQAAEHTLRNINPDVlfE 89
Cdd:PRK12475 20 RKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqqLYTeEDAKQKKPKAIAAKEHLRKINSEV--E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 90 VHNYNI-TTVENFQHFMdrisnggleegKPVDLVLSCVDNFEARMTINTACNELGQTWMESG-VSENAVSghiQLIIPGE 167
Cdd:PRK12475 98 IVPVVTdVTVEELEELV-----------KEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGcVGSYGVT---YTIIPGK 163
|
....*.
gi 38327032 168 SACFAC 173
Cdd:PRK12475 164 TPCLRC 169
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
20-247 |
1.37e-13 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 70.81 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFqpH---QAGLSKVQAAEHTLRNINPDVlfevhnynit 96
Cdd:PRK08762 138 VLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQIL--HtedRVGQPKVDSAAQRLAALNPDV---------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 97 TVENFQhfmDRISNGGLEE-GKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSEnaVSGHIQLIIPGESA----CF 171
Cdd:PRK08762 206 QVEAVQ---ERVTSDNVEAlLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFR--FEGQVSVFDAGRQRgqapCY 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 172 AC----APPLVVAANIDEKtlkreGVCAAsLPTTMGVvagILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNP 245
Cdd:PRK08762 281 RClfpePPPPELAPSCAEA-----GVLGV-LPGVIGL---LQATEAIKLLLGIGDplTGRLLTFDALAMRFRELRLPPDP 351
|
..
gi 38327032 246 QC 247
Cdd:PRK08762 352 HC 353
|
|
| Uba2_SUMO |
cd01489 |
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ... |
26-175 |
2.13e-12 |
|
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.
Pssm-ID: 238766 [Multi-domain] Cd Length: 312 Bit Score: 67.02 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT----VEN 100
Cdd:cd01489 8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFlFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKDpdfnVEF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38327032 101 FQHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACAP 175
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 ... |
40-176 |
4.18e-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: 64.91 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 40 GIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPdvlfevhNYNITTvenFQHFMDRISNGGLEEGKP 118
Cdd:cd01484 22 GFGQIHVIDMDTIDVSNLNRQFlFRPKDIGRPKSEVAAEAVNDRNP-------NCKVVP---YQNKVGPEQDFNDTFFEQ 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 119 VDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESACFACA--PP 176
Cdd:cd01484 92 FHIIVNALDNIIARRYVNGMLIFLIVPLIESGTE--GFKGNAQVILPGMTECIECTlyPP 149
|
|
| E1_ThiF_like |
cd01487 |
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
20-138 |
1.46e-11 |
|
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.
Pssm-ID: 238764 [Multi-domain] Cd Length: 174 Bit Score: 62.40 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 20 VAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVE 99
Cdd:cd01487 2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENN 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 38327032 100 NFQHFMDrisnggleegkpVDLVLSCVDNFEA-RMTINTA 138
Cdd:cd01487 82 LEGLFGD------------CDIVVEAFDNAETkAMLAESL 109
|
|
| YgdL_like |
cd00755 |
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
13-131 |
1.83e-11 |
|
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.
Pssm-ID: 238384 [Multi-domain] Cd Length: 231 Bit Score: 63.01 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPH----QAGLSKVQAAEHTLRNINPDVLF 88
Cdd:cd00755 7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNR---QIHallsTVGKPKVEVMAERIRDINPECEV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 38327032 89 EVHNYNITTvENFQHFMdrisnggleeGKPVDLVLSCVDNFEA 131
Cdd:cd00755 84 DAVEEFLTP-DNSEDLL----------GGDPDFVVDAIDSIRA 115
|
|
| thiF_fam2 |
TIGR02354 |
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
12-137 |
2.18e-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: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 12 YEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:TIGR02354 16 VQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKASQVGEPKTEALKENISEINPYTEIEAY 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 38327032 92 NYNITTvENFQHFMdrisnggleegKPVDLVLSCVDNFEAR-MTINT 137
Cdd:TIGR02354 96 DEKITE-ENIDKFF-----------KDADIVCEAFDNAEAKaMLVNA 130
|
|
| PRK05690 |
PRK05690 |
molybdopterin biosynthesis protein MoeB; Provisional |
13-247 |
3.26e-10 |
|
molybdopterin biosynthesis protein MoeB; Provisional
Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 59.47 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVH 91
Cdd:PRK05690 28 EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRqVLHDDATIGQPKVESARAALARINPHIAIETI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 92 NYNITtvenfQHFMDRISNGgleegkpVDLVLSCVDNFEARMTINTACNELGQTWmesgVSENAV--SGHIQLIIPGESA 169
Cdd:PRK05690 108 NARLD-----DDELAALIAG-------HDLVLDCTDNVATRNQLNRACFAAKKPL----VSGAAIrmEGQVTVFTYQDDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 170 -CFACAPPLVVAANIdekTLKREGVCAAsLPttmGVVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPNPQ 246
Cdd:PRK05690 172 pCYRCLSRLFGENAL---TCVEAGVMAP-LV---GVIGSLQAMEAIKLLTGYGEplSGRLLLYDAMTMQFREMKLKRDPG 244
|
.
gi 38327032 247 C 247
Cdd:PRK05690 245 C 245
|
|
| PRK08328 |
PRK08328 |
hypothetical protein; Provisional |
13-221 |
1.52e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 57.50 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR--LFFQPHQAGLSKVQAAEHTLRNINPDVLFEV 90
Cdd:PRK08328 23 EKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRqiLHWEEDLGKNPKPLSAKWKLERFNSDIKIET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 91 hnynittvenfqhFMDRISNGGLEEG-KPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIPGESA 169
Cdd:PRK08328 103 -------------FVGRLSEENIDEVlKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVE--GTYGQVTTIVPGKTK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 38327032 170 CFACAPPlvvaaNIDEKTLKREGVCAaslptTMGVVAGILVQNVLKFLLNFG 221
Cdd:PRK08328 168 RLREIFP-----KVKKKKGKFPILGA-----TAGVIGSIQAMEVIKLITGYG 209
|
|
| TcdA |
COG1179 |
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
13-143 |
1.78e-08 |
|
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440792 Cd Length: 247 Bit Score: 54.32 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 13 EKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRlffQPHqA-----GLSKVQAAEHTLRNINPDVl 87
Cdd:COG1179 20 ERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINR---QLH-AldstvGRPKVEVMAERIRDINPDC- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 38327032 88 fevhnyNITTVENFqhfmdrISNGGLEE--GKPVDLVLSCVDNFEARMTINTACNELG 143
Cdd:COG1179 95 ------EVTAIDEF------VTPENADEllSEDYDYVIDAIDSVSAKAALIAWCRRRG 140
|
|
| PRK05600 |
PRK05600 |
thiamine biosynthesis protein ThiF; Validated |
36-245 |
1.16e-07 |
|
thiamine biosynthesis protein ThiF; Validated
Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 52.96 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 36 LTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfqhfmdriSNGGLE 114
Cdd:PRK05600 60 LASAGVGTITLIDDDTVDVSNIHRqILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLT------------AENAVE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 115 EGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAvsGHIQLIIPGESAC-------FACAPPLVVAANidekt 187
Cdd:PRK05600 128 LLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFH--GELAVFNSGPDHRgvglrdlFPEQPSGDSIPD----- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38327032 188 lkregvCAAS--LPTTMGVVAGILVQNVLKFLLNFGTVSF--YLGYNAMQDFFPTMSMKPNP 245
Cdd:PRK05600 201 ------CATAgvLGATTAVIGALMATEAIKFLTGIGDVQPgtVLSYDALTATTRSFRVGADP 256
|
|
| Uba3_RUB |
cd01488 |
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ... |
36-178 |
2.00e-07 |
|
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.
Pssm-ID: 238765 [Multi-domain] Cd Length: 291 Bit Score: 51.59 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 36 LTRCGIGKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT--VENFQHFmdrisngg 112
Cdd:cd01488 18 LALSGFRNIHVIDMDTIDVSNLNRQFlFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDkdEEFYRQF-------- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38327032 113 leegkpvDLVLSCVDNFEARMTIN-TACNELGQTWMES------GVSEnAVSGHIQLIIPGESACFAC----APPLV 178
Cdd:cd01488 90 -------NIIICGLDSIEARRWINgTLVSLLLYEDPESiiplidGGTE-GFKGHARVILPGITACIECsldlFPPQV 158
|
|
| Ube1 |
TIGR01408 |
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ... |
42-165 |
2.88e-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: 52.20 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 42 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDrisngglEEGKPV 119
Cdd:TIGR01408 449 GMITVTDPDLIEKSNLNRQFlFRPHHIGKPKSYTAADATLKINPQIKIDAHQNRVgPETETI--FND-------EFYEKL 519
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 38327032 120 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 165
Cdd:TIGR01408 520 DVVINALDNVEARRYVDSRCLAFLKPLLESGTL--GTKGNTQVVVP 563
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
2-143 |
3.29e-07 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 51.41 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 2 ALKRMGiVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLR 80
Cdd:PRK05597 14 MLGEIG-QQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGvGQPKAESAREAML 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 38327032 81 NINPDVLFEVHNYNITTvenfqhfmdrisNGGLEEGKPVDLVLSCVDNFEARMTINTACNELG 143
Cdd:PRK05597 93 ALNPDVKVTVSVRRLTW------------SNALDELRDADVILDGSDNFDTRHLASWAAARLG 143
|
|
| PRK08223 |
PRK08223 |
hypothetical protein; Validated |
36-143 |
1.69e-06 |
|
hypothetical protein; Validated
Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 48.91 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 36 LTRCGIGKLLLFDYDKVELANMNRLFFQPHQA-GLSKVQAAEHTLRNINPDVLFEVHNYNITTvENFQHFMDrisnggle 114
Cdd:PRK08223 46 LARLGIGKFTIADFDVFELRNFNRQAGAMMSTlGRPKAEVLAEMVRDINPELEIRAFPEGIGK-ENADAFLD-------- 116
|
90 100 110
....*....|....*....|....*....|.
gi 38327032 115 egkPVDLVLSCVDNFE--ARMTINTACNELG 143
Cdd:PRK08223 117 ---GVDVYVDGLDFFEfdARRLVFAACQQRG 144
|
|
| Ube1_repeat2 |
cd01490 |
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
42-165 |
2.60e-06 |
|
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.
Pssm-ID: 238767 [Multi-domain] Cd Length: 435 Bit Score: 48.82 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 42 GKLLLFDYDKVELANMNRLF-FQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNI-TTVENFqhFMDRISNGgleegkpV 119
Cdd:cd01490 29 GEITVTDMDNIEKSNLNRQFlFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVgPETEHI--FNDEFWEK-------L 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 38327032 120 DLVLSCVDNFEARMTINTACNELGQTWMESGVSenAVSGHIQLIIP 165
Cdd:cd01490 100 DGVANALDNVDARMYVDRRCVYYRKPLLESGTL--GTKGNTQVVIP 143
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
26-247 |
2.45e-04 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 42.77 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITT---VENF 101
Cdd:PRK07878 51 GGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRqVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPsnaVELF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 102 QHFmdrisnggleegkpvDLVLSCVDNFEARMTINTACNELGQ--TW-----MESGVS---ENAVSGHiqliipgeSACF 171
Cdd:PRK07878 131 SQY---------------DLILDGTDNFATRYLVNDAAVLAGKpyVWgsiyrFEGQASvfwEDAPDGL--------GLNY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 172 AC-----APPLVVAANIDEKTLkreGVCAASlpttmgvVAGILVQNVLKFLLNFGT--VSFYLGYNAMQDFFPTMSMKPN 244
Cdd:PRK07878 188 RDlypepPPPGMVPSCAEGGVL---GVLCAS-------IGSIMGTEAIKLITGIGEplLGRLMVYDALEMTYRTIKIRKD 257
|
...
gi 38327032 245 PQC 247
Cdd:PRK07878 258 PST 260
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
26-247 |
2.04e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 39.72 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 26 GGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNR-LFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITtvenfqhf 104
Cdd:PRK07411 47 GGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRqVIHGTSWVGKPKIESAKNRILEINPYCQVDLYETRLS-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38327032 105 mdriSNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTwmesgvsenAVSGHIqLIIPGESACF------------- 171
Cdd:PRK07411 119 ----SENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKP---------NVYGSI-FRFEGQATVFnyeggpnyrdlyp 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38327032 172 ACAPPLVVAANidektlkREGVCAASLPttmGVVAGILVQNVLKFLLNFGTV--SFYLGYNAMQDFFPTMSMKPNPQC 247
Cdd:PRK07411 185 EPPPPGMVPSC-------AEGGVLGILP---GIIGVIQATETIKIILGAGNTlsGRLLLYNALDMKFRELKLRPNPER 252
|
|
|