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Conserved domains on  [gi|821224001|gb|KKY96057|]
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molybdopterin biosynthesis protein MoeB [Klebsiella variicola]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 11422192)

HesA/MoeB/ThiF family protein is an E1-like enzyme containing an NAD/FAD-binding fold that is involved in molybdopterin and thiamine biosynthesis

CATH:  3.40.50.720
EC:  2.7.7.-
Gene Ontology:  GO:0016779
PubMed:  12660720|11713534|12504674

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 1.12e-126

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: 358.67  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   2 NDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDR 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  82 PKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 162 TPPwAQGCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLALQRSRNC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 821224001 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 1.12e-126

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: 358.67  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   2 NDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDR 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  82 PKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 162 TPPwAQGCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLALQRSRNC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 821224001 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-234 3.55e-111

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: 319.04  E-value: 3.55e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTpPWAQ 167
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFI-PGEG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821224001 168 GCYRCLWPDSDEPQ-RNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLAL 234
Cdd:cd00757  160 PCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-209 4.37e-109

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: 312.76  E-value: 4.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001    8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPWAQ 167
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 821224001  168 GCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLL 209
Cdd:TIGR02356 161 PCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-240 5.22e-102

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 296.37  E-value: 5.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 RPKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMV 160
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 161 LTPPWAQGCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLALQRSRN 239
Cdd:PRK05690 165 FTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlSGRLLLYDAMTMQFREMKLKRDPG 244


                 .
gi 821224001 240 C 240
Cdd:PRK05690 245 C 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-242 3.39e-97

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: 284.15  E-value: 3.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001    9 YSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAK 88
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   89 TRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPwAQG 168
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPG-KTP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821224001  169 CYRCLWPDSDEPQ--RNCRTAGIVGPVVGMMGTLQALEAIKLLSG--MTTPRNTLRLFDARTSNWRNLALQ-RSRNCPV 242
Cdd:pfam00899 160 CYRCLFPEDPPPKlvPSCTVAGVLGPTTAVVAGLQALEALKLLLGkgEPNLAGRLLQFDALTMTFRELRLAlKNPNCPV 238
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 2-245 1.12e-126

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: 358.67  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   2 NDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDR 81
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  82 PKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVL 161
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 162 TPPwAQGCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLALQRSRNC 240
Cdd:COG0476  161 IPG-DTPCYRCLFPEPPEPGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlAGRLLLFDALTMEFRTIKLPRDPDC 239


                 ....*
gi 821224001 241 PVCGG 245
Cdd:COG0476  240 PVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 8-234 3.55e-111

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: 319.04  E-value: 3.55e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTpPWAQ 167
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFI-PGEG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821224001 168 GCYRCLWPDSDEPQ-RNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLAL 234
Cdd:cd00757  160 PCYRCLFPEPPPPGvPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPlAGRLLLFDALSMSFRTLKL 228
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-209 4.37e-109

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: 312.76  E-value: 4.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001    8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPWAQ 167
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 821224001  168 GCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLL 209
Cdd:TIGR02356 161 PCLRCLFPDIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-240 5.22e-102

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 296.37  E-value: 5.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 RPKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMV 160
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 161 LTPPWAQGCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLALQRSRN 239
Cdd:PRK05690 165 FTYQDDEPCYRCLSRLFGENALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlSGRLLLYDAMTMQFREMKLKRDPG 244


                 .
gi 821224001 240 C 240
Cdd:PRK05690 245 C 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 9-242 3.39e-97

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: 284.15  E-value: 3.39e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001    9 YSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAK 88
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   89 TRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPwAQG 168
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPG-KTP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821224001  169 CYRCLWPDSDEPQ--RNCRTAGIVGPVVGMMGTLQALEAIKLLSG--MTTPRNTLRLFDARTSNWRNLALQ-RSRNCPV 242
Cdd:pfam00899 160 CYRCLFPEDPPPKlvPSCTVAGVLGPTTAVVAGLQALEALKLLLGkgEPNLAGRLLQFDALTMTFRELRLAlKNPNCPV 238
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-244 1.08e-84

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 257.25  E-value: 1.08e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 RPKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMV 160
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 161 LTP--PWAQG-CYRCLWPDSDEPQ--RNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFDARTSNWRNLAL 234
Cdd:PRK08762 268 FDAgrQRGQApCYRCLFPEPPPPElaPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPlTGRLLTFDALAMRFRELRL 347

                        250
                 ....*....|
gi 821224001 235 QRSRNCPVCG 244
Cdd:PRK08762 348 PPDPHCPVCA 357
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 5-229 1.22e-65

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 207.80  E-value: 1.22e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   5 DFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKA 84
Cdd:PRK05597   5 DIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  85 AAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLtpp 164
Cdd:PRK05597  85 ESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVF--- 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 165 WAQG--CYRCLWPDSDEPQR--NCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTPR-NTLRLFDARTSNW 229
Cdd:PRK05597 162 HAGHgpIYEDLFPTPPPPGSvpSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLiGKLGYYDSLDGTW 231
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-244 1.32e-63

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 201.76  E-value: 1.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDhdfmRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK07688   1 MNE----RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 R--PKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVG-FGGQ 157
Cdd:PRK07688  77 NnlPKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGsYGLS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 158 LMVL---TPpwaqgCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMT-TPRNTLRLFDArtsnWRN-- 231
Cdd:PRK07688 157 YTIIpgkTP-----CLRCLLQSIPLGGATCDTAGIISPAVQIVASYQVTEALKLLVGDYeALRDGLVSFDV----WKNey 227

                        250
                 ....*....|....*..
gi 821224001 232 ----LALQRSRNCPVCG 244
Cdd:PRK07688 228 scmnVQKLKKDNCPSCG 244
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 8-241 6.58e-59

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 191.46  E-value: 6.58e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:PRK07878  22 RYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVL--TPPW 165
Cdd:PRK07878 102 RDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFweDAPD 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 166 AQG-CYRCLWPDSDEPQR--NCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTPR-NTLRLFDARTSNWRNLALQRSRNCP 241
Cdd:PRK07878 182 GLGlNYRDLYPEPPPPGMvpSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLlGRLMVYDALEMTYRTIKIRKDPSTP 261
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-242 9.95e-56

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 183.01  E-value: 9.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDHDFMRYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 RPKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMV 160
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 161 LTppwAQG--CYRCLWPDSDEPQR--NCRTAGIVGPVVGMMGTLQALEAIKLLSGM-TTPRNTLRLFDARTSNWRNLALQ 235
Cdd:PRK07411 171 FN---YEGgpNYRDLYPEPPPPGMvpSCAEGGVLGILPGIIGVIQATETIKIILGAgNTLSGRLLLYNALDMKFRELKLR 247


                 ....*..
gi 821224001 236 RSRNCPV 242
Cdd:PRK07411 248 PNPERPV 254
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 8-244 3.16e-53

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 175.30  E-value: 3.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID--RPKAA 85
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  86 AAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTP-- 163
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPgk 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001 164 -PwaqgCYRCLWPDSDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSG-MTTPRNTLRLFDArtsnWRN------LALQ 235
Cdd:PRK12475 164 tP----CLRCLMEHVPVGGATCDTAGIIQPAVQIVVAYQVTEALKILVEdFEALRETFLSFDI----WNNqnmsikVNKQ 235


                 ....*....
gi 821224001 236 RSRNCPVCG 244
Cdd:PRK12475 236 KKDTCPSCG 244
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 8-236 3.04e-48

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 163.13  E-value: 3.04e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLEDIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:PRK05600  21 RTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  88 KTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLT-PPWA 166
Cdd:PRK05600 101 AERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNsGPDH 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821224001 167 QGC-YRCLWPD--SDEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTPR-NTLRLFDARTSNWRNLALQR 236
Cdd:PRK05600 181 RGVgLRDLFPEqpSGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQpGTVLSYDALTATTRSFRVGA 254
PRK08328 PRK08328
hypothetical protein; Provisional
 1-223 1.06e-45

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 152.64  E-value: 1.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   1 MNDHDFMRYSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDID 80
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  81 R-PKAAAAKTRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLM 159
Cdd:PRK08328  80 KnPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821224001 160 VLTPPWAQGcYRCLWPdsdEPQRNCRTAGIVGPVVGMMGTLQALEAIKLLSGMTTP-RNTLRLFD 223
Cdd:PRK08328 160 TIVPGKTKR-LREIFP---KVKKKKGKFPILGATAGVIGSIQAMEVIKLITGYGEPlLNKLLIVD 220
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 30-164 1.80e-37

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: 128.54  E-value: 1.80e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKLVALQQRLSG 109
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 821224001 110 EALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPP 164
Cdd:cd01483   81 DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIG 135
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 8-158 1.99e-32

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: 118.65  E-value: 1.99e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSR-QLLLEDiaiEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAA 86
Cdd:COG1179    6 RFSRtERLYGE---EGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821224001  87 AKTRLSQLNPQIKLVALQQRLSGEALrAEV--AKADVVLDCTDNMVTRQAINAACVALDTPLVtaSAVGFGGQL 158
Cdd:COG1179   83 MAERIRDINPDCEVTAIDEFVTPENA-DELlsEDYDYVIDAIDSVSAKAALIAWCRRRGIPII--SSMGAGGKL 153
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 21-158 2.32e-28

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: 107.69  E-value: 2.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  21 EGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKL 100
Cdd:cd00755    4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 821224001 101 VALQQRLSGEALRAEVAKA-DVVLDCTDNMVTRQAINAACVALDTPLVtaSAVGFGGQL 158
Cdd:cd00755   84 DAVEEFLTPDNSEDLLGGDpDFVVDAIDSIRAKVALIAYCRKRKIPVI--SSMGAGGKL 140
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 30-156 2.63e-28

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: 105.93  E-value: 2.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSeDIDRPKAAAAKTRLSQLNPQIKLVALQQRLSG 109
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 821224001 110 EALRAEVAKADVVLDCTDNMVTRQAI-NAACVALDTPLVTASAVGFGG 156
Cdd:cd01487   80 NNLEGLFGDCDIVVEAFDNAETKAMLaESLLGNKNKPVVCASGMAGFG 127
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
23-156 6.98e-28

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 105.71  E-value: 6.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  23 QQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSeDIDRPKAAAAKTRLSQLNPQIKLVA 102
Cdd:PRK08644  23 LEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQQYFIS-QIGMPKVEALKENLLEINPFVEIEA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 821224001 103 LQQRLSGEALRAEVAKADVVLDCTDNMVTRQAI-NAACVALDTPLVTASAV-GFGG 156
Cdd:PRK08644 102 HNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLvETVLEHPGKKLVAASGMaGYGD 157
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 30-183 1.05e-23

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: 95.34  E-value: 1.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKLVALQQRLSG 109
Cdd:cd01484    1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821224001 110 EALRAE--VAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPWAQgCYRClwpDSDEPQRN 183
Cdd:cd01484   81 EQDFNDtfFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTE-CIEC---TLYPPQKN 152
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 30-172 1.52e-23

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: 96.68  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKLVALQQRLSG 109
Cdd:cd01489    1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821224001 110 EALRAEVAKA-DVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTPPWAQgCYRC 172
Cdd:cd01489   81 PDFNVEFFKQfDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTE-CYEC 143
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 24-209 1.02e-22

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: 91.85  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   24 QKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSeDIDRPKAAAAKTRLSQLNPQIKLVAL 103
Cdd:TIGR02354  17 QKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKAS-QVGEPKTEALKENISEINPYTEIEAY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  104 QQRLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVAL--DTPLVTASAV-GFGGQLMVLTPPWAQGCYRCLWPDSDEP 180
Cdd:TIGR02354  96 DEKITEENIDKFFKDADIVCEAFDNAEAKAMLVNAVLEKykDKYLIAASGLaGYDDANSIKTRKISKHFYLCGDGKSDAK 175

                         170       180
                  ....*....|....*....|....*....
gi 821224001  181 QRNcrtaGIVGPVVGMMGTLQALEAIKLL 209
Cdd:TIGR02354 176 QGL----GLMAPRVQICAAHQANLVLELI 200
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 9-228 1.17e-21

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: 88.89  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   9 YSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAK 88
Cdd:cd01492    4 YDRQIRL--WGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  89 TRLSQLNPQIKLVALQQRLSGEAlRAEVAKADVVL--DCTDNMVTRqaINAACVALDTPLVTASAVGFGGQLMV-LTPPw 165
Cdd:cd01492   82 ERLRALNPRVKVSVDTDDISEKP-EEFFSQFDVVVatELSRAELVK--INELCRKLGVKFYATGVHGLFGFVFAdLLAP- 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821224001 166 aqgcyrclwpdsdepqrncrTAGIVGPVVgmmgtlqALEAIKLLSGMTTPRNTLRLFDARTSN 228
Cdd:cd01492  158 --------------------VAAVVGGIL-------AQDVINALSKRESPLNNFFVFDGETSE 193
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-163 4.48e-19

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: 86.10  E-value: 4.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001     8 RYSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGT-----LTLADDDAVHLSNLQRQILFTSEDIDRP 82
Cdd:TIGR01408  401 RYDAQIAV--FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTgkkgmITVTDPDLIEKSNLNRQFLFRPHHIGKP 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001    83 KAAAAKTRLSQLNPQIKLVALQQRLSGEALR----AEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQL 158
Cdd:TIGR01408  479 KSYTAADATLKINPQIKIDAHQNRVGPETETifndEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNT 558


                   ....*
gi 821224001   159 MVLTP 163
Cdd:TIGR01408  559 QVVVP 563
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 9-160 1.61e-18

Ubiquitin activating enzyme (E1), repeat 1. 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 first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 82.32  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   9 YSRQL-LLEDIAIegqQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:cd01491    2 YSRQLyVLGHEAM---KKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEAS 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821224001  88 KTRLSQLNPQIKLVAlqqrLSGEALRAEVAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMV 160
Cdd:cd01491   79 QARLAELNPYVPVTV----STGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSIFC 147
PRK08223 PRK08223
hypothetical protein; Validated
 18-163 1.75e-18

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 82.42  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  18 IAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQ 97
Cdd:PRK08223  17 ITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPE 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821224001  98 IKLVALQQRLSGEALRAEVAKADVVLDCTDNMV--TRQAINAACVALDTPLVTASAVGFGGQLMVLTP 163
Cdd:PRK08223  97 LEIRAFPEGIGKENADAFLDGVDVYVDGLDFFEfdARRLVFAACQQRGIPALTAAPLGMGTALLVFDP 164
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 30-163 2.15e-16

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: 77.71  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLG-----SPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKLVALQ 104
Cdd:cd01490    1 KVFLVGAGAIGcellkNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821224001 105 QRLSGEAlrAEV------AKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLMVLTP 163
Cdd:cd01490   81 NRVGPET--EHIfndefwEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVVIP 143
PRK14852 PRK14852
hypothetical protein; Provisional
 9-163 1.28e-15

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 75.89  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   9 YSRQLLLEDIAieGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAK 88
Cdd:PRK14852 315 FSRNLGLVDYA--GQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMT 392

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821224001  89 TRLSQLNPQIKLVALQQRLSGEALRAEVAKADVVLDCTDNM---VTRQAINAAcVALDTPLVTASAVGFGGQLMVLTP 163
Cdd:PRK14852 393 ERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFaldIRRRLFNRA-LELGIPVITAGPLGYSCALLVFMP 469
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 22-158 2.91e-15

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 73.30  E-value: 2.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  22 GQQKL---LASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQI 98
Cdd:PRK15116  21 GEKALqlfADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPEC 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821224001  99 KLVALQQRLSGEALrAEVAKA--DVVLDCTDNMVTRQAINAACVALDTPLVTASavGFGGQL 158
Cdd:PRK15116 101 RVTVVDDFITPDNV-AEYMSAgfSYVIDAIDSVRPKAALIAYCRRNKIPLVTTG--GAGGQI 159
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 30-172 9.02e-15

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 72.00  E-value: 9.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKLVALQQRLsg 109
Cdd:cd01488    1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKI-- 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821224001 110 EALRAEVAKA-DVVLDCTDNMVTRQAINAACVAL------DT--PLVTASAVGFGGQLMVLTPPWAqGCYRC 172
Cdd:cd01488   79 QDKDEEFYRQfNIIICGLDSIEARRWINGTLVSLllyedpESiiPLIDGGTEGFKGHARVILPGIT-ACIEC 149
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 9-227 4.74e-14

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: 68.60  E-value: 4.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   9 YSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSE--DIDRPKAAA 86
Cdd:cd01485    2 YDRQIRL--WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEvsNSGMNRAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  87 AKTRLSQLNPQIKL-VALQQRLSGEALRAE-VAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGGQLmvltpp 164
Cdd:cd01485   80 SYEFLQELNPNVKLsIVEEDSLSNDSNIEEyLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYA------ 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821224001 165 waqgcyRCLWPdsdepqrncrTAGIVGPVVgmmgtlqALEAIKLLSGMTTPRNTLRLFDARTS 227
Cdd:cd01485  154 ------FFDFP----------IAAFLGGVV-------AQEAIKSISGKFTPLNNLYIYDGFES 193
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 9-112 2.41e-13

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: 69.15  E-value: 2.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001     9 YSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAK 88
Cdd:TIGR01408    7 YSRQLYV--LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90       100
                   ....*....|....*....|....
gi 821224001    89 TRLSQLNPQIKLVALQQRLSGEAL 112
Cdd:TIGR01408   85 KKLAELNPYVHVSSSSVPFNEEFL 108
PRK14851 PRK14851
hypothetical protein; Provisional
 22-163 9.48e-13

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 67.19  E-value: 9.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  22 GQQKLLA-SRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAAKTRLSQLNPQIKL 100
Cdd:PRK14851  36 GEQERLAeAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEI 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821224001 101 VALQQRLSGEALRAEVAKADVVLDCTDNM---VTRQAINAAcVALDTPLVTASAVGFGGQLMVLTP 163
Cdd:PRK14851 116 TPFPAGINADNMDAFLDGVDVVLDGLDFFqfeIRRTLFNMA-REKGIPVITAGPLGYSSAMLVFTP 180
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 30-172 4.03e-11

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: 61.62  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  30 RVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDI--DRPKAAAAKTRLSQLNPQI--------- 98
Cdd:cd01486    1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIdatgivlsi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  99 --------KLVALQQRLSGEALRAEVAKADVVLDCTDNMVTRQ------------AINAAcVALDTPLVT------ASAV 152
Cdd:cd01486   81 pmpghpisESEVPSTLKDVKRLEELIKDHDVIFLLTDSRESRWlptllsaaknklVINAA-LGFDSYLVMrhgagpQSQS 159

                        170       180
                 ....*....|....*....|
gi 821224001 153 GFGGQLMVLTPPWAQGCYRC 172
Cdd:cd01486  160 GSGDSSSDSIPGSRLGCYFC 179
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 8-156 3.83e-09

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: 56.16  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   8 RYSRQLLLedIAIEGQQKLLASRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDIDRPKAAAA 87
Cdd:cd01493    2 KYDRQLRL--WGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEAT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821224001  88 KTRLSQLNPQIKLVALQQrlSGEALRAE----VAKADVVLDCTDNMVTRQAINAACVALDTPLVTASAVGFGG 156
Cdd:cd01493   80 CELLQELNPDVNGSAVEE--SPEALLDNdpsfFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYG 150
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 29-172 6.47e-08

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 53.02  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   29 SRVLIIGLGGLGSPAALYLAGAGVGTLTLADDDAVHLSNLQRQILFTSEDI---DRPKAAAAKTRLSQLNPQIKLVAL-- 103
Cdd:TIGR01381 339 LKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKRIFPSIQATGHrl 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  104 -------------QQRLSGEALRAE--VAKADVVLDCTDNMVTRQ------------AINAAcVALDTPLVTASAVGFGG 156
Cdd:TIGR01381 419 tvpmpghpidekdVPELEKDIARLEqlIKDHDVVFLLLDSREARWlptvlcsrhkkiAISAA-LGFDSYVVMRHGIGRSE 497

                         170       180
                  ....*....|....*....|.
gi 821224001  157 -----QLMVLTPPWAQGCYRC 172
Cdd:TIGR01381 498 svsdvSSSDSVPYSRLGCYFC 518
PRK07877 PRK07877
Rv1355c family protein;
18-124 2.71e-06

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 48.06  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001  18 IAIEGQQKLLASRVLIIGLGgLGSPAALYLAGAGV-GTLTLADDDAVHLSNLQRqILFTSEDIDRPKAAAAKTRLSQLNP 96
Cdd:PRK07877  97 ITAEEQERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDP 174

                         90       100
                 ....*....|....*....|....*...
gi 821224001  97 QIKLVALQQRLSGEALRAEVAKADVVLD 124
Cdd:PRK07877 175 YLPVEVFTDGLTEDNVDAFLDGLDVVVE 202
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 31-153 2.82e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 36.80  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821224001   31 VLIIGLGGLGSPAALYLAGAG-VGTLTLADddavhlsnlqrqilftsEDIDRPKAAAAKTRLSQLNPqIKLVALQQRlsg 109
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdVDRITVAD-----------------RTLEKAQALAAKLGGVRFIA-VAVDADNYE--- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 821224001  110 EALRAEVAKADVVLDCTDNMVTRQAInAACVALDTPLVTASAVG 153
Cdd:pfam03435  60 AVLAALLKEGDLVVNLSPPTLSLDVL-KACIETGVHYVDTSYLR 102
 
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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