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Conserved domains on  [gi|1317696658|gb|PLA86923|]
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molybdopterin-synthase adenylyltransferase MoeB [Enterobacter bugandensis]

Protein Classification

molybdopterin-synthase adenylyltransferase MoeB( domain architecture ID 11481509)

molybdopterin-synthase adenylyltransferase MoeB catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD

EC:  2.7.7.80
Gene Ontology:  GO:0006777
PubMed:  11713534

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-245 6.04e-156

molybdopterin biosynthesis protein MoeB; Provisional


:

Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 432.73  E-value: 6.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   1 MTVELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSD 80
Cdd:PRK05690    1 MMAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  81 ATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEG 160
Cdd:PRK05690   81 ATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 161 QISVFTYADGEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLM 240
Cdd:PRK05690  161 QVTVFTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK 240


                  ....*
gi 1317696658 241 RNPGC 245
Cdd:PRK05690  241 RDPGC 245
 
Name Accession Description Interval E-value
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-245 6.04e-156

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 432.73  E-value: 6.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   1 MTVELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSD 80
Cdd:PRK05690    1 MMAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  81 ATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEG 160
Cdd:PRK05690   81 ATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 161 QISVFTYADGEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLM 240
Cdd:PRK05690  161 QVTVFTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK 240


                  ....*
gi 1317696658 241 RNPGC 245
Cdd:PRK05690  241 RDPGC 245
moeB TIGR02355
molybdopterin synthase sulfurylase MoeB; This model describes the molybdopterin biosynthesis ...
 9-248 1.86e-138

molybdopterin synthase sulfurylase MoeB; This model describes the molybdopterin biosynthesis protein MoeB in E. coli and related species. The enzyme covalently modifies the molybdopterin synthase MoaD by sulfurylation. This enzyme is closely related to ThiF, a thiamine biosynthesis enzyme that modifies ThiS by an analogous adenylation. Both MoeB and ThiF belong to the HesA/MoeB/ThiF family (pfam00899). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 131408 [Multi-domain]  Cd Length: 240  Bit Score: 388.40  E-value: 1.86e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   9 EMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKV 88
Cdd:TIGR02355   1 EMLRYNRQIILRGFDFDGQEALKASRVLIVGLGGLGCAASQYLAAAGVGNLTLLDFDTVSLSNLQRQVLHSDANIGQPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  89 DSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYA 168
Cdd:TIGR02355  81 ESAKDALTQINPHIAINPINAKLDDAELAALIAEHDIVVDCTDNVEVRNQLNRQCFAAKVPLVSGAAIRMEGQVSVFTYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 169 DGEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNPGCEIC 248
Cdd:TIGR02355 161 DGEPCYRCLSRLFGENALSCVEAGVMAPVVGVVGSLQAMEAIKVLAGIGKPLSGKILMIDAMTMSFREMKLPKNPTCPVC 240
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-250 9.27e-107

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: 308.21  E-value: 9.27e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   6 SDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQ 85
Cdd:COG0476     1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  86 PKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVF 165
Cdd:COG0476    81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 166 TYADGePCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNPGC 245
Cdd:COG0476   161 IPGDT-PCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDC 239


                  ....*
gi 1317696658 246 EICGG 250
Cdd:COG0476   240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 12-239 3.60e-89

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: 263.18  E-value: 3.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSA 91
Cdd:cd00757     1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  92 RTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGe 171
Cdd:cd00757    81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEG- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 172 PCYRCLSRLFGE-NALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKL 239
Cdd:cd00757   160 PCYRCLFPEPPPpGVPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-247 5.70e-69

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: 212.12  E-value: 5.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  13 YNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSAR 92
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  93 TALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGeP 172
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKT-P 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 173 CYRCLS--RLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPA-AGKIVMYDAMTCQFREMKL-MRNPGCEI 247
Cdd:pfam00899 160 CYRCLFpeDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlAGRLLQFDALTMTFRELRLaLKNPNCPV 238
 
Name Accession Description Interval E-value
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-245 6.04e-156

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 432.73  E-value: 6.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   1 MTVELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSD 80
Cdd:PRK05690    1 MMAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  81 ATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEG 160
Cdd:PRK05690   81 ATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 161 QISVFTYADGEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLM 240
Cdd:PRK05690  161 QVTVFTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK 240


                  ....*
gi 1317696658 241 RNPGC 245
Cdd:PRK05690  241 RDPGC 245
moeB TIGR02355
molybdopterin synthase sulfurylase MoeB; This model describes the molybdopterin biosynthesis ...
 9-248 1.86e-138

molybdopterin synthase sulfurylase MoeB; This model describes the molybdopterin biosynthesis protein MoeB in E. coli and related species. The enzyme covalently modifies the molybdopterin synthase MoaD by sulfurylation. This enzyme is closely related to ThiF, a thiamine biosynthesis enzyme that modifies ThiS by an analogous adenylation. Both MoeB and ThiF belong to the HesA/MoeB/ThiF family (pfam00899). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 131408 [Multi-domain]  Cd Length: 240  Bit Score: 388.40  E-value: 1.86e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   9 EMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKV 88
Cdd:TIGR02355   1 EMLRYNRQIILRGFDFDGQEALKASRVLIVGLGGLGCAASQYLAAAGVGNLTLLDFDTVSLSNLQRQVLHSDANIGQPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  89 DSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYA 168
Cdd:TIGR02355  81 ESAKDALTQINPHIAINPINAKLDDAELAALIAEHDIVVDCTDNVEVRNQLNRQCFAAKVPLVSGAAIRMEGQVSVFTYQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 169 DGEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNPGCEIC 248
Cdd:TIGR02355 161 DGEPCYRCLSRLFGENALSCVEAGVMAPVVGVVGSLQAMEAIKVLAGIGKPLSGKILMIDAMTMSFREMKLPKNPTCPVC 240
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-250 9.27e-107

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: 308.21  E-value: 9.27e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   6 SDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQ 85
Cdd:COG0476     1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  86 PKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVF 165
Cdd:COG0476    81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 166 TYADGePCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNPGC 245
Cdd:COG0476   161 IPGDT-PCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLPRDPDC 239


                  ....*
gi 1317696658 246 EICGG 250
Cdd:COG0476   240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 12-239 3.60e-89

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: 263.18  E-value: 3.60e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSA 91
Cdd:cd00757     1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  92 RTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGe 171
Cdd:cd00757    81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEG- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 172 PCYRCLSRLFGE-NALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKL 239
Cdd:cd00757   160 PCYRCLFPEPPPpGVPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
5-249 4.87e-69

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 216.80  E-value: 4.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   5 LSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVG 84
Cdd:PRK08762  108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  85 QPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISV 164
Cdd:PRK08762  188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 165 FTYAD---GEPCYRCL--SRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKL 239
Cdd:PRK08762  268 FDAGRqrgQAPCYRCLfpEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRL 347

                         250
                  ....*....|
gi 1317696658 240 MRNPGCEICG 249
Cdd:PRK08762  348 PPDPHCPVCA 357
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 13-247 5.70e-69

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: 212.12  E-value: 5.70e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  13 YNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSAR 92
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  93 TALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGeP 172
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKT-P 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 173 CYRCLS--RLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPA-AGKIVMYDAMTCQFREMKL-MRNPGCEI 247
Cdd:pfam00899 160 CYRCLFpeDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPNlAGRLLQFDALTMTFRELRLaLKNPNCPV 238
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 12-213 2.26e-61

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; 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 the Escherichia. 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 more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 191.80  E-value: 2.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSA 91
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  92 RTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGE 171
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1317696658 172 PCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVL 213
Cdd:TIGR02356 161 PCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
2-247 1.70e-55

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 182.63  E-value: 1.70e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   2 TVELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDA 81
Cdd:PRK07411    8 EIQLSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  82 TVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQ 161
Cdd:PRK07411   88 WVGKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQ 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 162 ISVFTYADGePCYRClsrLFGEN-----ALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFRE 236
Cdd:PRK07411  168 ATVFNYEGG-PNYRD---LYPEPpppgmVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKFRE 243

                         250
                  ....*....|.
gi 1317696658 237 MKLMRNPGCEI 247
Cdd:PRK07411  244 LKLRPNPERPV 254
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 4-246 1.44e-51

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 172.20  E-value: 1.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   4 ELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATV 83
Cdd:PRK07878   14 ELTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  84 GQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQIS 163
Cdd:PRK07878   94 GRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQAS 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 164 VFtYADGE----PCYRClsrLFGEN-----ALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQF 234
Cdd:PRK07878  174 VF-WEDAPdglgLNYRD---LYPEPpppgmVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLGRLMVYDALEMTY 249

                         250
                  ....*....|..
gi 1317696658 235 REMKLMRNPGCE 246
Cdd:PRK07878  250 RTIKIRKDPSTP 261
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 12-243 4.34e-49

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 165.05  E-value: 4.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSA 91
Cdd:PRK05597    8 RYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  92 RTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQlnAGCFAHK--TPLVSGAAIRMEGQISVFtYAD 169
Cdd:PRK05597   88 REAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHL--ASWAAARlgIPHVWASILGFDAQLSVF-HAG 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 170 GEPCYRclsRLFGENAL-----TCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNP 243
Cdd:PRK05597  165 HGPIYE---DLFPTPPPpgsvpSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLIGKLGYYDSLDGTWEYIPVVGNP 240
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 3-243 1.17e-38

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 138.09  E-value: 1.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   3 VELSDQEMMRYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDAT 82
Cdd:PRK05600   12 MQLPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  83 VGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQI 162
Cdd:PRK05600   92 VGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGEL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 163 SVFTYADGEPCYRcLSRLF-----GENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREM 237
Cdd:PRK05600  172 AVFNSGPDHRGVG-LRDLFpeqpsGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQPGTVLSYDALTATTRSF 250


                  ....*.
gi 1317696658 238 KLMRNP 243
Cdd:PRK05600  251 RVGADP 256
PRK08328 PRK08328
hypothetical protein; Provisional
 5-239 9.64e-31

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 113.74  E-value: 9.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   5 LSDQEMMRYNRQIVLrgFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVG 84
Cdd:PRK08328    2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  85 Q-PKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVAVRNQLNAgcFAHKT--PLVSGAAIRMEGQ 161
Cdd:PRK08328   80 KnPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDD--YAHKKgiPLVHGAVEGTYGQ 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317696658 162 ISvfTYADGEPcyRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKL 239
Cdd:PRK08328  158 VT--TIVPGKT--KRLREIFPKVKKKKGKFPILGATAGVIGSIQAMEVIKLITGYGEPLLNKLLIVDLANNVFEVVEL 231
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 12-249 1.18e-30

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 116.25  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQ--PKVD 89
Cdd:PRK07688    4 RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVKNnlPKAV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  90 SARTALARINPNVQftlIDAMLDD---DALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGqISvFT 166
Cdd:PRK07688   84 AAKKRLEEINSDVR---VEAIVQDvtaEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYG-LS-YT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 167 YADGE-PCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKLMRNP-- 243
Cdd:PRK07688  159 IIPGKtPCLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDYEALRDGLVSFDVWKNEYSCMNVQKLKkd 238


                  ....*.
gi 1317696658 244 GCEICG 249
Cdd:PRK07688  239 NCPSCG 244
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 12-249 1.04e-25

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 102.89  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFDFEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHS--DATVGQPKVD 89
Cdd:PRK12475    4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTeeDAKQKKPKAI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  90 SARTALARINPNVQftlIDAMLDD---DALFAQIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQisVFT 166
Cdd:PRK12475   84 AAKEHLRKINSEVE---IVPVVTDvtvEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGV--TYT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 167 YADGE-PCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREMKL--MRNP 243
Cdd:PRK12475  159 IIPGKtPCLRCLMEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVEDFEALRETFLSFDIWNNQNMSIKVnkQKKD 238


                  ....*.
gi 1317696658 244 GCEICG 249
Cdd:PRK12475  239 TCPSCG 244
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 55-158 5.33e-24

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: 96.30  E-value: 5.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQtLHS-DATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQH-DLVLDCTDN 132
Cdd:COG1179    47 GVGRLTLVDLDDVCESNINRQ-LHAlDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELLSEDyDYVIDAIDS 125

                          90       100
                  ....*....|....*....|....*...
gi 1317696658 133 VAVRNQLNAGCFAHKTPLVS--GAAIRM 158
Cdd:COG1179   126 VSAKAALIAWCRRRGIPIISsmGAGGKL 153
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 41-165 5.82e-24

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 93.49  E-value: 5.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  41 GGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQI 120
Cdd:cd01483     8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1317696658 121 AQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVF 165
Cdd:cd01483    88 DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 55-189 1.91e-22

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: 91.90  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQtLHS-DATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQI-AQHDLVLDCTDN 132
Cdd:cd00755    34 GVGKLTLIDFDVVCVSNLNRQ-IHAlLSTVGKPKVEVMAERIRDINPECEVDAVEEFLTPDNSEDLLgGDPDFVVDAIDS 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317696658 133 VAVRNQLNAGCFAHKTPLVS--GAAIRME-GQISVftyAD-----GEPCYRC----LSRLFGENALTCV 189
Cdd:cd00755   113 IRAKVALIAYCRKRKIPVISsmGAGGKLDpTRIRV---ADisktsGDPLARKvrkrLRKRGIFFGVPVV 178
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 55-206 6.21e-14

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: 67.79  E-value: 6.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDaTVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVA 134
Cdd:cd01487    22 GVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLFGDCDIVVEAFDNAE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 135 VRNQLnAGCFAHKT--PLV--SGAA-------IRMEgQISVFTYADGEpcyrclsrLFGENALTCveaGVMAPLVGVIGS 203
Cdd:cd01487   101 TKAML-AESLLGNKnkPVVcaSGMAgfgdsnnIKTK-KISDNFYICGD--------LVNEAKEGL---GLMAPRVNICAA 167


                  ...
gi 1317696658 204 LQA 206
Cdd:cd01487   168 HQA 170
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 41-176 1.70e-13

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: 68.56  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  41 GGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLI-DAMLDDDALFAQ 119
Cdd:cd01489     8 GGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYhANIKDPDFNVEF 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1317696658 120 IAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGEpCYRC 176
Cdd:cd01489    88 FKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTE-CYEC 143
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
55-132 6.97e-12

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 62.95  E-value: 6.97e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDaTVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDN 132
Cdd:PRK08644   51 GVGNLKLVDFDVVEPSNLNRQQYFIS-QIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDN 127
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-164 1.10e-11

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


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 64.14  E-value: 1.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   12 RYNRQIVLRGFDFegQEALKAANVLVVGLGGLGCAAAQYLAAAGV-----GRMTLLDFDTVSVSNLQRQTLHSDATVGQP 86
Cdd:TIGR01408  401 RYDAQIAVFGDTF--QQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKP 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658   87 KVDSARTALARINPnvQFTlIDAMLD----------DDALFAQIaqhDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAI 156
Cdd:TIGR01408  479 KSYTAADATLKINP--QIK-IDAHQNrvgpetetifNDEFYEKL---DVVINALDNVEARRYVDSRCLAFLKPLLESGTL 552


                   ....*...
gi 1317696658  157 RMEGQISV 164
Cdd:TIGR01408  553 GTKGNTQV 560
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 55-162 3.44e-11

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 61.74  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQH-DLVLDCTDNV 133
Cdd:PRK15116   53 GIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYMSAGfSYVIDAIDSV 132

                          90       100       110
                  ....*....|....*....|....*....|
gi 1317696658 134 AVRNQLNAGCFAHKTPLVS-GAAirmEGQI 162
Cdd:PRK15116  133 RPKAALIAYCRRNKIPLVTtGGA---GGQI 159
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 41-176 2.39e-10

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: 58.74  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  41 GGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQ- 119
Cdd:cd01484     8 GGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPEQDFNDt 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1317696658 120 -IAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFTYADGEpCYRC 176
Cdd:cd01484    88 fFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTE-CIEC 144
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 57-153 6.85e-10

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 58.45  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  57 GRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQftlIDAMLD----------DDALFAQIaqhDLV 126
Cdd:cd01490    29 GEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLK---ITALQNrvgpetehifNDEFWEKL---DGV 102

                          90       100
                  ....*....|....*....|....*...
gi 1317696658 127 LDCTDNVAVRNQLNAGCFAHKTPLV-SG 153
Cdd:cd01490   103 ANALDNVDARMYVDRRCVYYRKPLLeSG 130
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 55-132 7.07e-10

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: 57.19  E-value: 7.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTlHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDN 132
Cdd:TIGR02354  44 GIGKLILVDFDVVEPSNLNRQQ-YKASQVGEPKTEALKENISEINPYTEIEAYDEKITEENIDKFFKDADIVCEAFDN 120
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 13-232 4.85e-08

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 51.52  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  13 YNRQIVLRGFdfEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSAR 92
Cdd:cd01492     4 YDRQIRLWGL--EAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  93 TALARINPNVQFTLIDAMLD--DDALFaqiAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVSGAAIRMEGqisvFTYADg 170
Cdd:cd01492    82 ERLRALNPRVKVSVDTDDISekPEEFF---SQFDVVVATELSRAELVKINELCRKLGVKFYATGVHGLFG----FVFAD- 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317696658 171 epcyrclsrlfgenaltcveagVMAPLVGVIGSLQAMEAIKVLAHYGTPAAGKIVmYDAMTC 232
Cdd:cd01492   154 ----------------------LLAPVAAVVGGILAQDVINALSKRESPLNNFFV-FDGETS 192
PRK08223 PRK08223
hypothetical protein; Validated
 55-166 1.82e-07

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 50.84  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTD--N 132
Cdd:PRK08223   50 GIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDffE 129

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1317696658 133 VAVRNQLNAGCFAHKTPLVSGAAIRMEGQISVFT 166
Cdd:PRK08223  130 FDARRLVFAACQQRGIPALTAAPLGMGTALLVFD 163
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 55-132 5.43e-07

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: 49.68  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTL--HSDATVGQPKVDSARTALARINPNVQFTLID---AMLDD--------------DA 115
Cdd:cd01486    22 GVRHITFVDSGKVSYSNPVRQSLftFEDCKGGKPKAEAAAERLKEIFPSIDATGIVlsiPMPGHpisesevpstlkdvKR 101

                          90
                  ....*....|....*..
gi 1317696658 116 LFAQIAQHDLVLDCTDN 132
Cdd:cd01486   102 LEELIKDHDVIFLLTDS 118
cyclo_dehyd_2 TIGR03882
bacteriocin biosynthesis cyclodehydratase domain; This model describes a ThiF-like domain of a ...
 172-250 5.32e-04

bacteriocin biosynthesis cyclodehydratase domain; This model describes a ThiF-like domain of a fusion protein found in clusters associated with the production of TOMMs (thiazole/oxazole-modified microcins), small bacteriocins with characteristic heterocycle modifications. This domain is presumed to act as a cyclodehydratase, as do members of the SagC family modeled by TIGR03603.


Pssm-ID: 274832  Cd Length: 164  Bit Score: 39.65  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658 172 PCYRCL---------SRLFGENALTCVEAGVMAPLVGVIG-----SLQAMEAIKVLAHYGTPAAGKIVMYDAMTCQFREM 237
Cdd:TIGR03882  25 GCWHCLatrlranrpDEAFLARLQGTPLAGPRPPWLTPAAlaavaALAAAELAKWLAGERPRLEGAVLTLDLATLTVSRH 104

                          90
                  ....*....|...
gi 1317696658 238 KLMRNPGCEICGG 250
Cdd:TIGR03882 105 PLLPRPQCPVCGD 117
PRK14851 PRK14851
hypothetical protein; Provisional
 55-139 5.68e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 41.00  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVA 134
Cdd:PRK14851   66 GIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDFFQ 145


                  ....*..
gi 1317696658 135 --VRNQL 139
Cdd:PRK14851  146 feIRRTL 152
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 13-219 1.29e-03

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 38.94  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  13 YNRQIVLRGFDfeGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNLQRQTL--HSDATVGQPKVDS 90
Cdd:cd01485     2 YDRQIRLWGDE--AQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFldAEVSNSGMNRAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  91 ARTALARINPNVQFTLIDAM----LDDDALFAQIAQHDLVLDCTDNVAVrnQLNAGCFAHKTPLVSGAairmegqisvft 166
Cdd:cd01485    80 SYEFLQELNPNVKLSIVEEDslsnDSNIEEYLQKFTLVIATEENYERTA--KVNDVCRKHHIPFISCA------------ 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1317696658 167 yadgepCYRCLSRLFGEnaltcveagvmAPLVGVIGSLQAMEAIKVLAHYGTP 219
Cdd:cd01485   146 ------TYGLIGYAFFD-----------FPIAAFLGGVVAQEAIKSISGKFTP 181
PRK07877 PRK07877
Rv1355c family protein;
57-151 1.30e-03

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 39.59  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  57 GRMTLLDFDTVSVSNLQR--QTLHSdatVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVA 134
Cdd:PRK07877  132 GELRLADFDTLELSNLNRvpAGVFD---LGVNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFLDGLDVVVEECDSLD 208

                          90
                  ....*....|....*..
gi 1317696658 135 VRNQLNAGCFAHKTPLV 151
Cdd:PRK07877  209 VKVLLREAARARRIPVL 225
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 12-173 5.66e-03

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 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. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 37.67  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  12 RYNRQIVLRGFdfEGQEALKAANVLVVGLGGLGCAAAQYLAAAGVGRMTLLDFDTVSVSNL-QRQTLHSDAtVGQPKVDS 90
Cdd:cd01493     2 KYDRQLRLWGE--HGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLgNNFFLDASS-LGKSRAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  91 ARTALARINPNVQFTLI----DAMLDDDALFaqIAQHDLVLDCTDNVAVRNQLNAGCFAHKTPLVsgaAIRMEGQISVFT 166
Cdd:cd01493    79 TCELLQELNPDVNGSAVeespEALLDNDPSF--FSQFTVVIATNLPESTLLRLADVLWSANIPLL---YVRSYGLYGYIR 153


                  ....*..
gi 1317696658 167 YADGEPC 173
Cdd:cd01493   154 IQLKEHT 160
PRK14852 PRK14852
hypothetical protein; Provisional
 55-165 7.52e-03

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 37.37  E-value: 7.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696658  55 GVGRMTLLDFDTVSVSNLQRQTLHSDATVGQPKVDSARTALARINPNVQFTLIDAMLDDDALFAQIAQHDLVLDCTDNVA 134
Cdd:PRK14852  355 GIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFA 434

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1317696658 135 --VRNQLNAGCFAHKTPLVSGAAIRMEGQISVF 165
Cdd:PRK14852  435 ldIRRRLFNRALELGIPVITAGPLGYSCALLVF 467
 
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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