|
Name |
Accession |
Description |
Interval |
E-value |
| YgdL_like |
cd00755 |
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
82-316 |
7.23e-95 |
|
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: 285.65 E-value: 7.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 82 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 161
Cdd:cd00755 1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 162 CHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSR 241
Cdd:cd00755 81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334657 242 SVRHRLrRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEdenPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVI 316
Cdd:cd00755 161 KVRKRL-RKRGIFFGVPVVYSTEPPDPPKADELVCGDE---VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
|
|
| TcdA |
COG1179 |
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
101-321 |
3.14e-62 |
|
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: 202.23 E-value: 3.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 101 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 180
Cdd:COG1179 33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 181 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLrRKHGIEGGIPVV 260
Cdd:COG1179 113 SEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRL-RKRGIPKGVKVV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334657 261 FSLEKPKaKLLPFEGTNGEDENPLDYQvvpgfrvriipVLGTI---PAIFGQIMASYVITQLAG 321
Cdd:COG1179 192 YSTEQPR-KPQADGTVCDTGGTGLKCA-----------GPGSIsfvPAVFGLIAAGEVIRDLLG 243
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
78-321 |
4.13e-33 |
|
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: 125.06 E-value: 4.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 78 NIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSS 157
Cdd:pfam00899 6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 158 IFPECHIEAKVMLYDSSSEEEILSgKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADirestiD 237
Cdd:pfam00899 86 INPDVEVEAYTERLTPENAEELIK-SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK------T 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 238 PLSRSvrhrlrrkhgieggipvVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIMASYVIT 317
Cdd:pfam00899 159 PCYRC-----------------LFP-EDPPPKLVPSCTVAG--------------------VLGPTTAVVAGLQALEALK 200
|
....
gi 145334657 318 QLAG 321
Cdd:pfam00899 201 LLLG 204
|
|
| PRK15116 |
PRK15116 |
sulfur acceptor protein CsdL; Provisional |
101-264 |
4.29e-27 |
|
sulfur acceptor protein CsdL; Provisional
Pssm-ID: 185071 Cd Length: 268 Bit Score: 109.51 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 101 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 180
Cdd:PRK15116 39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 181 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLRRKHGI----EG- 255
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDFGVvknsKGk 198
|
170
....*....|
gi 145334657 256 -GIPVVFSLE 264
Cdd:PRK15116 199 lGVDCVFSTE 208
|
|
| thiF_fam2 |
TIGR02354 |
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
105-231 |
4.56e-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: 64.89 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATrADVGIPKAMCLKKHFSSIFPECHIEAkvmlYDSSSEEEILSG-- 182
Cdd:TIGR02354 34 SNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYTEIEA----YDEKITEENIDKff 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 145334657 183 -KPDFVLDCIDNIDTKvGLLAACVKRGLK---VLSATGAGARADPTRIRVADI 231
Cdd:TIGR02354 109 kDADIVCEAFDNAEAK-AMLVNAVLEKYKdkyLIAASGLAGYDDANSIKTRKI 160
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YgdL_like |
cd00755 |
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ... |
82-316 |
7.23e-95 |
|
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: 285.65 E-value: 7.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 82 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 161
Cdd:cd00755 1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 162 CHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSR 241
Cdd:cd00755 81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334657 242 SVRHRLrRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEdenPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVI 316
Cdd:cd00755 161 KVRKRL-RKRGIFFGVPVVYSTEPPDPPKADELVCGDE---VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
|
|
| TcdA |
COG1179 |
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ... |
101-321 |
3.14e-62 |
|
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: 202.23 E-value: 3.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 101 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 180
Cdd:COG1179 33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 181 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLrRKHGIEGGIPVV 260
Cdd:COG1179 113 SEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRL-RKRGIPKGVKVV 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334657 261 FSLEKPKaKLLPFEGTNGEDENPLDYQvvpgfrvriipVLGTI---PAIFGQIMASYVITQLAG 321
Cdd:COG1179 192 YSTEQPR-KPQADGTVCDTGGTGLKCA-----------GPGSIsfvPAVFGLIAAGEVIRDLLG 243
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
78-321 |
4.13e-33 |
|
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: 125.06 E-value: 4.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 78 NIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSS 157
Cdd:pfam00899 6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 158 IFPECHIEAKVMLYDSSSEEEILSgKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADirestiD 237
Cdd:pfam00899 86 INPDVEVEAYTERLTPENAEELIK-SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK------T 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 238 PLSRSvrhrlrrkhgieggipvVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIMASYVIT 317
Cdd:pfam00899 159 PCYRC-----------------LFP-EDPPPKLVPSCTVAG--------------------VLGPTTAVVAGLQALEALK 200
|
....
gi 145334657 318 QLAG 321
Cdd:pfam00899 201 LLLG 204
|
|
| PRK15116 |
PRK15116 |
sulfur acceptor protein CsdL; Provisional |
101-264 |
4.29e-27 |
|
sulfur acceptor protein CsdL; Provisional
Pssm-ID: 185071 Cd Length: 268 Bit Score: 109.51 E-value: 4.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 101 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 180
Cdd:PRK15116 39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 181 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLRRKHGI----EG- 255
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDFGVvknsKGk 198
|
170
....*....|
gi 145334657 256 -GIPVVFSLE 264
Cdd:PRK15116 199 lGVDCVFSTE 208
|
|
| E1_enzyme_family |
cd01483 |
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ... |
101-229 |
3.36e-25 |
|
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: 100.42 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 101 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 180
Cdd:cd01483 8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145334657 181 sGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVA 229
Cdd:cd01483 88 -DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIG 135
|
|
| ThiF |
COG0476 |
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ... |
105-214 |
2.23e-24 |
|
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: 101.36 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGkP 184
Cdd:COG0476 40 SPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAG-A 118
|
90 100 110
....*....|....*....|....*....|
gi 145334657 185 DFVLDCIDNIDTKVGLLAACVKRGLKVLSA 214
Cdd:COG0476 119 DLVLDCTDNFATRYLLNDACVKLGIPLVSG 148
|
|
| ThiF_MoeB_HesA_family |
cd00757 |
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ... |
105-208 |
3.91e-24 |
|
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: 100.24 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGkP 184
Cdd:cd00757 34 SPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIAG-Y 112
|
90 100
....*....|....*....|....
gi 145334657 185 DFVLDCIDNIDTKVGLLAACVKRG 208
Cdd:cd00757 113 DLVLDCTDNFATRYLINDACVKLG 136
|
|
| E1_ThiF_like |
cd01487 |
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ... |
105-233 |
8.52e-18 |
|
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: 80.89 E-value: 8.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRaDVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILsGKP 184
Cdd:cd01487 12 SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLF-GDC 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145334657 185 DFVLDCIDNIDTKVGLL-AACVKRGLKVLSATGAGARADPTRIRVADIRE 233
Cdd:cd01487 90 DIVVEAFDNAETKAMLAeSLLGNKNKPVVCASGMAGFGDSNNIKTKKISD 139
|
|
| PRK08644 |
PRK08644 |
sulfur carrier protein ThiS adenylyltransferase ThiF; |
105-233 |
1.43e-17 |
|
sulfur carrier protein ThiS adenylyltransferase ThiF;
Pssm-ID: 236320 [Multi-domain] Cd Length: 212 Bit Score: 81.06 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVaTRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILsGKP 184
Cdd:PRK08644 41 SNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELF-KDC 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145334657 185 DFVLDCIDNIDTKVGLLAACVKR-GLKVLSATGAGARADPTRIRVADIRE 233
Cdd:PRK08644 119 DIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMAGYGDSNSIKTRRIGK 168
|
|
| PRK05690 |
PRK05690 |
molybdopterin biosynthesis protein MoeB; Provisional |
107-222 |
7.75e-14 |
|
molybdopterin biosynthesis protein MoeB; Provisional
Pssm-ID: 180204 [Multi-domain] Cd Length: 245 Bit Score: 71.03 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 107 AASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDF 186
Cdd:PRK05690 47 ASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGH-DL 125
|
90 100 110
....*....|....*....|....*....|....*.
gi 145334657 187 VLDCIDNIDTKVGLLAACVKRGLKVLSatGAGARAD 222
Cdd:PRK05690 126 VLDCTDNVATRNQLNRACFAAKKPLVS--GAAIRME 159
|
|
| PRK07688 |
PRK07688 |
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated |
108-209 |
2.76e-13 |
|
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
Pssm-ID: 181084 [Multi-domain] Cd Length: 339 Bit Score: 70.79 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 108 ASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADV--GIPKAMCLKKHFSSIFPECHIEAKVMlyDSSSE--EEILSGK 183
Cdd:PRK07688 40 AEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKAVAAKKRLEEINSDVRVEAIVQ--DVTAEelEELVTGV 117
|
90 100
....*....|....*....|....*.
gi 145334657 184 pDFVLDCIDNIDTKVGLLAACVKRGL 209
Cdd:PRK07688 118 -DLIIDATDNFETRFIVNDAAQKYGI 142
|
|
| thiF_fam2 |
TIGR02354 |
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ... |
105-231 |
4.56e-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: 64.89 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 105 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATrADVGIPKAMCLKKHFSSIFPECHIEAkvmlYDSSSEEEILSG-- 182
Cdd:TIGR02354 34 SNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYTEIEA----YDEKITEENIDKff 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 145334657 183 -KPDFVLDCIDNIDTKvGLLAACVKRGLK---VLSATGAGARADPTRIRVADI 231
Cdd:TIGR02354 109 kDADIVCEAFDNAEAK-AMLVNAVLEKYKdkyLIAASGLAGYDDANSIKTRKI 160
|
|
| PRK12475 |
PRK12475 |
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional |
73-197 |
9.18e-12 |
|
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
Pssm-ID: 183547 [Multi-domain] Cd Length: 338 Bit Score: 65.91 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 73 EHLTRNIQF--FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVG--IPKA 148
Cdd:PRK12475 3 ERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145334657 149 MCLKKHFSSIFPECHIEAKVMlyDSSSEE-EILSGKPDFVLDCIDNIDTK 197
Cdd:PRK12475 83 IAAKEHLRKINSEVEIVPVVT--DVTVEElEELVKEVDLIIDATDNFDTR 130
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
82-197 |
4.29e-11 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 64.12 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 82 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 161
Cdd:PRK05597 18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97
|
90 100 110
....*....|....*....|....*....|....*.
gi 145334657 162 CHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTK 197
Cdd:PRK05597 98 VKVTVSVRRLTWSNALDELRDA-DVILDGSDNFDTR 132
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
68-214 |
4.92e-10 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 60.80 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 68 DEIVSEHLTrnIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPK 147
Cdd:PRK08762 113 DERYSRHLR--LPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334657 148 AMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTKVGLLAACVKRGLKVLSA 214
Cdd:PRK08762 191 VDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDV-DVVVDGADNFPTRYLLNDACVKLGKPLVYG 256
|
|
| PRK08328 |
PRK08328 |
hypothetical protein; Provisional |
73-197 |
5.99e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 169382 [Multi-domain] Cd Length: 231 Bit Score: 56.34 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 73 EHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGI-PKAMCL 151
Cdd:PRK08328 8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSA 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 145334657 152 KKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTK 197
Cdd:PRK08328 88 KWKLERFNSDIKIETFVGRLSEENIDEVLKGV-DVIVDCLDNFETR 132
|
|
| PRK05600 |
PRK05600 |
thiamine biosynthesis protein ThiF; Validated |
82-333 |
1.66e-06 |
|
thiamine biosynthesis protein ThiF; Validated
Pssm-ID: 235528 [Multi-domain] Cd Length: 370 Bit Score: 49.88 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 82 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 161
Cdd:PRK05600 31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 162 CHIEAKVMLYDSSSEEEILSGkPDFVLDCIDNIDTKvgllaacvkrglkvlsatgagaradptrIRVADIRESTIDPL-- 239
Cdd:PRK05600 111 IRVNALRERLTAENAVELLNG-VDLVLDGSDSFATK----------------------------FLVADAAEITGTPLvw 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 240 --------SRSVRHRLRRKHGIegGIPVVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIM 311
Cdd:PRK05600 162 gtvlrfhgELAVFNSGPDHRGV--GLRDLFP-EQPSGDSIPDCATAG--------------------VLGATTAVIGALM 218
|
250 260
....*....|....*....|...
gi 145334657 312 ASYVITQLAGV-QVQMEPIVNLD 333
Cdd:PRK05600 219 ATEAIKFLTGIgDVQPGTVLSYD 241
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
52-205 |
1.84e-06 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 49.71 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 52 SETRPDTVANGQDLLKDEIV--SEHLTrnIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSL 129
Cdd:PRK07878 2 STSLPPLVEPAAELTRDEVArySRHLI--IPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDE 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145334657 130 SSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTKVGLLAACV 205
Cdd:PRK07878 80 SNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQY-DLILDGTDNFATRYLVNDAAV 154
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
111-205 |
8.86e-06 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 47.81 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 111 LLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEakvmLYDS--SSEEEILSGKP-DFV 187
Cdd:PRK07411 57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVD----LYETrlSSENALDILAPyDVV 132
|
90
....*....|....*...
gi 145334657 188 LDCIDNIDTKVGLLAACV 205
Cdd:PRK07411 133 VDGTDNFPTRYLVNDACV 150
|
|
| PRK07877 |
PRK07877 |
Rv1355c family protein; |
117-215 |
7.91e-05 |
|
Rv1355c family protein;
Pssm-ID: 236122 [Multi-domain] Cd Length: 722 Bit Score: 44.98 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 117 GKLLLVDFDQVSLSSLNRhAVATRADVGIPKAMCLKKHFSSIFPEChieaKVMLYDS----SSEEEILSGKpDFVLDCID 192
Cdd:PRK07877 132 GELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDPYL----PVEVFTDglteDNVDAFLDGL-DVVVEECD 205
|
90 100
....*....|....*....|...
gi 145334657 193 NIDTKVGLLAACVKRGLKVLSAT 215
Cdd:PRK07877 206 SLDVKVLLREAARARRIPVLMAT 228
|
|
| PRK08223 |
PRK08223 |
hypothetical protein; Validated |
73-214 |
3.32e-04 |
|
hypothetical protein; Validated
Pssm-ID: 181302 [Multi-domain] Cd Length: 287 Bit Score: 42.36 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 73 EHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLK 152
Cdd:PRK08223 8 EAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLA 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334657 153 KHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCID--NIDTKVGLLAACVKRGLKVLSA 214
Cdd:PRK08223 88 EMVRDINPELEIRAFPEGIGKENADAFLDGV-DVYVDGLDffEFDARRLVFAACQQRGIPALTA 150
|
|
| Ube1_repeat2 |
cd01490 |
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ... |
117-205 |
1.43e-03 |
|
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: 40.74 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 117 GKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEE---EILSGKPDFVLDCIDN 193
Cdd:cd01490 29 GEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVGPETEHifnDEFWEKLDGVANALDN 108
|
90
....*....|..
gi 145334657 194 IDTKVGLLAACV 205
Cdd:cd01490 109 VDARMYVDRRCV 120
|
|
| Apg7 |
cd01486 |
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ... |
108-186 |
3.49e-03 |
|
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.
Pssm-ID: 238763 [Multi-domain] Cd Length: 307 Bit Score: 39.28 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 108 ASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADV--GIPKAMCLKKHFSSIFPECHIEAKV----MLYDSSSEEEILS 181
Cdd:cd01486 15 ARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVlsipMPGHPISESEVPS 94
|
....*
gi 145334657 182 GKPDF 186
Cdd:cd01486 95 TLKDV 99
|
|
| PRK14851 |
PRK14851 |
hypothetical protein; Provisional |
67-214 |
5.83e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 184853 [Multi-domain] Cd Length: 679 Bit Score: 39.07 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 67 KDEIVSEHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIP 146
Cdd:PRK14851 18 AAEYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRP 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334657 147 KAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCID--NIDTKVGLLAACVKRGLKVLSA 214
Cdd:PRK14851 98 KLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGV-DVVLDGLDffQFEIRRTLFNMAREKGIPVITA 166
|
|
|