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Conserved domains on  [gi|639317339|ref|WP_024594827|]
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MULTISPECIES: HesA/MoeB/ThiF family protein [unclassified Pseudoalteromonas]

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]; ...
 5-249 2.28e-115

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: 330.17  E-value: 2.28e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   5 SDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQ 84
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  85 NKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGF 164
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 165 DFRqsDSPCYGCVFPQSEAtPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFKVIKDS 242
Cdd:COG0476  161 IPG--DTPCYRCLFPEPPE-PGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlaGRLLLFDALTMEFRTIKLPRDP 237


                 ....*..
gi 639317339 243 ECKECGK 249
Cdd:COG0476  238 DCPVCGE 244
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 5-249 2.28e-115

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: 330.17  E-value: 2.28e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   5 SDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQ 84
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  85 NKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGF 164
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 165 DFRqsDSPCYGCVFPQSEAtPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFKVIKDS 242
Cdd:COG0476  161 IPG--DTPCYRCLFPEPPE-PGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlaGRLLLFDALTMEFRTIKLPRDP 237


                 ....*..
gi 639317339 243 ECKECGK 249
Cdd:COG0476  238 DCPVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 11-238 1.07e-105

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: 305.17  E-value: 1.07e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  91 GKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDFRqsD 170
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPG--E 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 171 SPCYGCVFPQSEATPVINCSNAGVISPLLGVIGSMQAQLTLNLLLG--HSEGGGFITFDALTLKQQHFKV 238
Cdd:cd00757  159 GPCYRCLFPEPPPPGVPSCAEAGVLGPLVGVIGSLQALEALKILLGigEPLAGRLLLFDALSMSFRTLKL 228
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-244 1.93e-94

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 277.11  E-value: 1.93e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   1 MNELSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKIN 80
Cdd:PRK05690   2 MAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  81 HLGQNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQ 160
Cdd:PRK05690  82 TIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 161 LMGFDFrQSDSPCYGCVFPQ-SEATpvINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFK 237
Cdd:PRK05690 162 VTVFTY-QDDEPCYRCLSRLfGENA--LTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlsGRLLLYDAMTMQFREMK 238


                 ....*..
gi 639317339 238 VIKDSEC 244
Cdd:PRK05690 239 LKRDPGC 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 12-244 9.19e-88

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: 259.88  E-value: 9.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   12 YSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAG 91
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   92 KVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDfrQSDS 171
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVI--PGKT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639317339  172 PCYGCVFPQSEA-TPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG---GGFITFDALTLKQQHFKVI-KDSEC 244
Cdd:pfam00899 159 PCYRCLFPEDPPpKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnlaGRLLQFDALTMTFRELRLAlKNPNC 236
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 11-214 7.14e-81

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: 241.11  E-value: 7.14e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   91 GKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDFRQSd 170
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGE- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 639317339  171 SPCYGCVFPqSEATPVINCSNAGVISPLLGVIGSMQAQLTLNLL 214
Cdd:TIGR02356 160 GPCLRCLFP-DIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 5-249 2.28e-115

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: 330.17  E-value: 2.28e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   5 SDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQ 84
Cdd:COG0476    1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  85 NKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGF 164
Cdd:COG0476   81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 165 DFRqsDSPCYGCVFPQSEAtPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFKVIKDS 242
Cdd:COG0476  161 IPG--DTPCYRCLFPEPPE-PGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPlaGRLLLFDALTMEFRTIKLPRDP 237


                 ....*..
gi 639317339 243 ECKECGK 249
Cdd:COG0476  238 DCPVCGE 244
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 11-238 1.07e-105

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: 305.17  E-value: 1.07e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:cd00757    1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  91 GKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDFRqsD 170
Cdd:cd00757   81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPG--E 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 171 SPCYGCVFPQSEATPVINCSNAGVISPLLGVIGSMQAQLTLNLLLG--HSEGGGFITFDALTLKQQHFKV 238
Cdd:cd00757  159 GPCYRCLFPEPPPPGVPSCAEAGVLGPLVGVIGSLQALEALKILLGigEPLAGRLLLFDALSMSFRTLKL 228
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-244 1.93e-94

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 277.11  E-value: 1.93e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   1 MNELSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKIN 80
Cdd:PRK05690   2 MAELSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  81 HLGQNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQ 160
Cdd:PRK05690  82 TIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 161 LMGFDFrQSDSPCYGCVFPQ-SEATpvINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFK 237
Cdd:PRK05690 162 VTVFTY-QDDEPCYRCLSRLfGENA--LTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPlsGRLLLYDAMTMQFREMK 238


                 ....*..
gi 639317339 238 VIKDSEC 244
Cdd:PRK05690 239 LKRDPGC 245
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
4-248 2.01e-88

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 266.49  E-value: 2.01e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   4 LSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLG 83
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  84 QNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMG 163
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 164 FDFRQSDS--PCYGCVFPQ---SEATPviNCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHF 236
Cdd:PRK08762 268 FDAGRQRGqaPCYRCLFPEpppPELAP--SCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPltGRLLTFDALAMRFREL 345

                        250
                 ....*....|..
gi 639317339 237 KVIKDSECKECG 248
Cdd:PRK08762 346 RLPPDPHCPVCA 357
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 12-244 9.19e-88

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: 259.88  E-value: 9.19e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   12 YSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAG 91
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   92 KVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDfrQSDS 171
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVI--PGKT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639317339  172 PCYGCVFPQSEA-TPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG---GGFITFDALTLKQQHFKVI-KDSEC 244
Cdd:pfam00899 159 PCYRCLFPEDPPpKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnlaGRLLQFDALTMTFRELRLAlKNPNC 236
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 11-214 7.14e-81

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: 241.11  E-value: 7.14e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   91 GKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDFRQSd 170
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGGE- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 639317339  171 SPCYGCVFPqSEATPVINCSNAGVISPLLGVIGSMQAQLTLNLL 214
Cdd:TIGR02356 160 GPCLRCLFP-DIADTGPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 3-244 1.48e-63

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 203.40  E-value: 1.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   3 ELSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHL 82
Cdd:PRK07878  14 ELTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  83 GQNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLM 162
Cdd:PRK07878  94 GRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQAS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 163 GF--DFRQSDSPCYGCVFPqsEATP---VINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQH 235
Cdd:PRK07878 174 VFweDAPDGLGLNYRDLYP--EPPPpgmVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPllGRLMVYDALEMTYRT 251


                 ....*....
gi 639317339 236 FKVIKDSEC 244
Cdd:PRK07878 252 IKIRKDPST 260
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 11-216 4.42e-60

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 193.17  E-value: 4.42e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:PRK05597   8 RYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  91 GKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDfrQSD 170
Cdd:PRK05597  88 REAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFH--AGH 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 639317339 171 SPCYGCVFPQSEAT-PVINCSNAGVISPLLGVIGSMQAQLTLNLLLG 216
Cdd:PRK05597 166 GPIYEDLFPTPPPPgSVPSCSQAGVLGPVVGVVGSAMAMEALKLITG 212
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
3-244 2.49e-55

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 181.86  E-value: 2.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   3 ELSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHL 82
Cdd:PRK07411  10 QLSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  83 GQNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLM 162
Cdd:PRK07411  90 GKPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQAT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 163 GFDFRqsDSPCYGCVFPqsEATP---VINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSE--GGGFITFDALTLKQQHFK 237
Cdd:PRK07411 170 VFNYE--GGPNYRDLYP--EPPPpgmVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNtlSGRLLLYNALDMKFRELK 245


                 ....*..
gi 639317339 238 VIKDSEC 244
Cdd:PRK07411 246 LRPNPER 252
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 4-241 3.00e-48

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 163.13  E-value: 3.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   4 LSDKETLRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLG 83
Cdd:PRK05600  14 LPTSELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  84 QNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMG 163
Cdd:PRK05600  94 RPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 164 FDfRQSDSPCYGC--VFP-QSEATPVINCSNAGVISPLLGVIGSMQAQLTLNLL--LGHSEGGGFITFDALTLKQQHFKV 238
Cdd:PRK05600 174 FN-SGPDHRGVGLrdLFPeQPSGDSIPDCATAGVLGATTAVIGALMATEAIKFLtgIGDVQPGTVLSYDALTATTRSFRV 252


                 ...
gi 639317339 239 IKD 241
Cdd:PRK05600 253 GAD 255
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-249 8.52e-47

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 158.62  E-value: 8.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   1 MNElsdketlRYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYK-- 78
Cdd:PRK07688   1 MNE-------RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTes 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  79 --INHLgqNKVAAAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALA 156
Cdd:PRK07688  74 dvKNNL--PKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 157 TKGqlMGFDFRQSDSPCYGCVF---PQSEATpvinCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDalTL 231
Cdd:PRK07688 152 SYG--LSYTIIPGKTPCLRCLLqsiPLGGAT----CDTAGIISPAVQIVASYQVTEALKLLVGDYEAlrDGLVSFD--VW 223

                        250       260
                 ....*....|....*....|..
gi 639317339 232 KQQHFKV----IKDSECKECGK 249
Cdd:PRK07688 224 KNEYSCMnvqkLKKDNCPSCGE 245
PRK08328 PRK08328
hypothetical protein; Provisional
 4-219 9.93e-47

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 155.34  E-value: 9.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   4 LSDKETLRYSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLG 83
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  84 QNKVAAAGK-VLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLM 162
Cdd:PRK08328  80 KNPKPLSAKwKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639317339 163 ----GFDFRQSDspcygcVFPqseaTPVINCSNAGVISPLLGVIGSMQAQLTLNLLLGHSE 219
Cdd:PRK08328 160 tivpGKTKRLRE------IFP----KVKKKKGKFPILGATAGVIGSIQAMEVIKLITGYGE 210
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 11-249 3.46e-43

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 149.11  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLEEVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQN--KVA 88
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKkpKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  89 AAGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGqlMGFDFRQ 168
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYG--VTYTIIP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 169 SDSPCYGCVF---PQSEATpvinCSNAGVISPLLGVIGSMQAQLTLNLLLGHSEG--GGFITFDALTLKQQHFKV--IKD 241
Cdd:PRK12475 162 GKTPCLRCLMehvPVGGAT----CDTAGIIQPAVQIVVAYQVTEALKILVEDFEAlrETFLSFDIWNNQNMSIKVnkQKK 237


                 ....*...
gi 639317339 242 SECKECGK 249
Cdd:PRK12475 238 DTCPSCGL 245
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 33-166 1.59e-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: 1.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  33 TVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVTHCRKLDE 112
Cdd:cd01483    1 RVLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 639317339 113 SNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKGQLMGFDF 166
Cdd:cd01483   81 DNLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDI 134
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 11-154 1.78e-30

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: 113.25  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:COG1179    6 RFSRTERL--YGEEGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVM 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639317339  91 GKVLASLNNQINIVTHCRKLDESNATNML-KDADIILDCSDNFSTRYSVNRYCIANKTPLIS--GAA 154
Cdd:COG1179   84 AERIRDINPDCEVTAIDEFVTPENADELLsEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISsmGAG 150
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
29-220 2.13e-28

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 107.25  E-value: 2.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  29 LKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQvLYKINHLGQNKVAAAGKVLASLNNQINIVTHCR 108
Cdd:PRK08644  26 LKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMPKVEALKENLLEINPFVEIEAHNE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 109 KLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIAN-KTPLISGAALATKGQLMGFDFRQSDSPCYGCVFPQSEATPvi 187
Cdd:PRK08644 105 KIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMAGYGDSNSIKTRRIGKNFYIVGDFVTEAKP-- 182

                        170       180       190
                 ....*....|....*....|....*....|...
gi 639317339 188 ncsNAGVISPLLGVIGSMQAQLTLNLLLGHSEG 220
Cdd:PRK08644 183 ---GNPLMAPRVNIAAAHQANLVLRLILGEEVA 212
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 33-211 1.58e-27

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: 103.62  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  33 TVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQvLYKINHLGQNKVAAAGKVLASLNNQINIVTHCRKLDE 112
Cdd:cd01487    1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 113 SNATNMLKDADIILDCSDNFSTRYSVNRYCIANKT-PLISGAALATKGQLMGFDFRQSDSPCYGCVFPQSEATPVIncsn 191
Cdd:cd01487   80 NNLEGLFGDCDIVVEAFDNAETKAMLAESLLGNKNkPVVCASGMAGFGDSNNIKTKKISDNFYICGDLVNEAKEGL---- 155

                        170       180
                 ....*....|....*....|
gi 639317339 192 aGVISPLLGVIGSMQAQLTL 211
Cdd:cd01487  156 -GLMAPRVNICAAHQANLVL 174
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 22-154 2.89e-27

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: 104.61  E-value: 2.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  22 GLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQI 101
Cdd:cd00755    2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPEC 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639317339 102 NIVTHCRKLDESNATNML-KDADIILDCSDNFSTRYSVNRYCIANKTPLIS--GAA 154
Cdd:cd00755   82 EVDAVEEFLTPDNSEDLLgGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISsmGAG 137
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 29-214 1.35e-24

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: 96.86  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   29 LKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVlYKINHLGQNKVAAAGKVLASLNNQINIVTHCR 108
Cdd:TIGR02354  19 LEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQ-YKASQVGEPKTEALKENISEINPYTEIEAYDE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  109 KLDESNATNMLKDADIILDCSDNFSTRYSV--NRYCIANKTPLISGAALATKGQLMGFDFRQSDSPCYGCVFPQSEATpv 186
Cdd:TIGR02354  98 KITEENIDKFFKDADIVCEAFDNAEAKAMLvnAVLEKYKDKYLIAASGLAGYDDANSIKTRKISKHFYLCGDGKSDAK-- 175

                         170       180
                  ....*....|....*....|....*...
gi 639317339  187 incSNAGVISPLLGVIGSMQAQLTLNLL 214
Cdd:TIGR02354 176 ---QGLGLMAPRVQICAAHQANLVLELI 200
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 34-185 6.89e-20

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: 86.66  E-value: 6.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  34 VAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVT-HCRKLDE 112
Cdd:cd01489    2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAyHANIKDP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639317339 113 SNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLI-SGAAlatkgqlmGFD-----FRQSDSPCYGCvfpQSEATP 185
Cdd:cd01489   82 DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIeSGTT--------GFLgqvqvIKKGKTECYEC---QPKETP 149
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 36-159 4.10e-18

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: 82.72  E-value: 4.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  36 VVGAGGLG-----SPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVTHCRKL 110
Cdd:cd01490    4 LVGAGAIGcellkNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 639317339 111 DESNaTNMLKDA-----DIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKG 159
Cdd:cd01490   84 GPET-EHIFNDEfweklDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKG 136
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 21-159 8.03e-18

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: 82.24  E-value: 8.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339    21 VGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGT-----LILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLA 95
Cdd:TIGR01408  409 FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGTgkkgmITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAADATL 488

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639317339    96 SLNNQINIVTHCRKLDeSNATNMLKDA-----DIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKG 159
Cdd:TIGR01408  489 KINPQIKIDAHQNRVG-PETETIFNDEfyeklDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKG 556
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 34-159 1.73e-17

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: 78.77  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  34 VAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVTHCRKLDES 113
Cdd:cd01484    2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 639317339 114 NATNM--LKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAALATKG 159
Cdd:cd01484   82 QDFNDtfFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKG 129
PRK08223 PRK08223
hypothetical protein; Validated
 26-165 1.18e-14

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 71.64  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  26 QLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVT 105
Cdd:PRK08223  22 QQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELEIRA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639317339 106 HCRKLDESNATNMLKDADIILDCSDNFS--TRYSVNRYCIANKTPLISGAALATKGQLMGFD 165
Cdd:PRK08223 102 FPEGIGKENADAFLDGVDVYVDGLDFFEfdARRLVFAACQQRGIPALTAAPLGMGTALLVFD 163
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 12-153 1.92e-12

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: 63.98  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  12 YSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINH--LGQNKVAA 89
Cdd:cd01485    2 YDRQIRL--WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNFFLDAEVsnSGMNRAAA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639317339  90 AGKVLASLNN--QINIVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGA 153
Cdd:cd01485   80 SYEFLQELNPnvKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCA 145
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 34-186 1.24e-11

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: 63.14  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  34 VAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINIVTHCRKLDES 113
Cdd:cd01488    2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 114 NATnMLKDADIILDCSDNFSTR------------YSVNRYCIanktPLISGAALATKGQ----LMGFdfrqsdSPCYGC- 176
Cdd:cd01488   82 DEE-FYRQFNIIICGLDSIEARrwingtlvslllYEDPESII----PLIDGGTEGFKGHarviLPGI------TACIECs 150

                        170
                 ....*....|..
gi 639317339 177 --VFPQSEATPV 186
Cdd:cd01488  151 ldLFPPQVTFPL 162
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 23-154 2.05e-10

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 59.43  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  23 LEGQLTLK---SSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKvaaaGKVLASLNN 99
Cdd:PRK15116  19 LYGEKALQlfaDAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAK----AEVMAERIR 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639317339 100 QINIVTHCRKLD-----ESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLIS-GAA 154
Cdd:PRK15116  95 QINPECRVTVVDdfitpDNVAEYMSAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTtGGA 155
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 12-151 1.09e-09

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: 57.28  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  12 YSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAG 91
Cdd:cd01491    2 YSRQLYV--LGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  92 KVLASLNNQINIVTHcrklDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLIS 151
Cdd:cd01491   80 ARLAELNPYVPVTVS----TGPLTTDELLKFQVVVLTDASLEDQLKINEFCHSPGIKFIS 135
PRK14852 PRK14852
hypothetical protein; Provisional
 10-164 5.23e-09

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 56.24  E-value: 5.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  10 LRYSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAA 89
Cdd:PRK14852 313 IAFSRNLGL--VDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDV 390

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639317339  90 AGKVLASLNNQINIVTHCRKLDESNATNMLKDADIILDCSDNFS---TRYSVNRyCIANKTPLISGAALATKGQLMGF 164
Cdd:PRK14852 391 MTERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDFFAldiRRRLFNR-ALELGIPVITAGPLGYSCALLVF 467
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 22-232 9.23e-09

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: 53.83  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  22 GLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQI 101
Cdd:cd01492   12 GLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASLERLRALNPRV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339 102 NIVTHCRKLDESNaTNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLISGAalatkgqLMGFdfrqsdspcYGCVFpqs 181
Cdd:cd01492   92 KVSVDTDDISEKP-EEFFSQFDVVVATELSRAELVKINELCRKLGVKFYATG-------VHGL---------FGFVF--- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639317339 182 eatpvincsnAGVISPLLGVIGSMQAQLTLNLLLGHSEG-GGFITFDALTLK 232
Cdd:cd01492  152 ----------ADLLAPVAAVVGGILAQDVINALSKRESPlNNFFVFDGETSE 193
PRK14851 PRK14851
hypothetical protein; Provisional
 24-165 7.34e-08

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 52.56  E-value: 7.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  24 EGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAGKVLASLNNQINI 103
Cdd:PRK14851  36 GEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEI 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639317339 104 VTHCRKLDESNATNMLKDADIILDCSD--NFSTRYSVNRYCIANKTPLI-------SGAALATKGQLMGFD 165
Cdd:PRK14851 116 TPFPAGINADNMDAFLDGVDVVLDGLDffQFEIRRTLFNMAREKGIPVItagplgySSAMLVFTPQGMGFD 186
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 11-138 2.02e-07

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: 51.15  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  11 RYSRHLLLEevGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAA 90
Cdd:cd01493    2 KYDRQLRLW--GEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEEDLGNNFFLDASSLGKSRAEAT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 639317339  91 GKVLASLNnqinivthcrklDESNATNMLKDADIILDCSDNFSTRYSV 138
Cdd:cd01493   80 CELLQELN------------PDVNGSAVEESPEALLDNDPSFFSQFTV 115
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-149 3.58e-06

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: 47.58  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339    12 YSRHLLLeeVGLEGQLTLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQRQVLYKINHLGQNKVAAAG 91
Cdd:TIGR01408    7 YSRQLYV--LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 639317339    92 KVLASLNNQInivtHCRKLDESNATNMLKDADIILDCSDNFSTRYSVNRYCIANKTPL 149
Cdd:TIGR01408   85 KKLAELNPYV----HVSSSSVPFNEEFLDKFQCVVLTEMSLPLQKEINDFCHSQCPPI 138
PRK06153 PRK06153
hypothetical protein; Provisional
 28-150 9.16e-05

hypothetical protein; Provisional


Pssm-ID: 235717 [Multi-domain]  Cd Length: 393  Bit Score: 43.04  E-value: 9.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  28 TLKSSTVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSNLQR-------QVLYKinhlGQNKVAAAGKVLAslNNQ 100
Cdd:PRK06153 173 KLEGQRIAIIGLGGTGSYILDLVAKTPVREIHLFDGDDFLQHNAFRspgaasiEELRE----APKKVDYFKSRYS--NMR 246

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 639317339 101 INIVTHCRKLDESNAtNMLKDADIILDCSDNFSTRYSVNRYCIANKTPLI 150
Cdd:PRK06153 247 RGIVPHPEYIDEDNV-DELDGFTFVFVCVDKGSSRKLIVDYLEALGIPFI 295
PRK07877 PRK07877
Rv1355c family protein;
24-138 6.00e-04

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 40.74  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339  24 EGQLTLKSSTVAVVGAGgLGSPALLYLAAAGV-GTLILIDDDEVELSNLQRqVLYKINHLGQNKVAAAGKVLASLNNQIN 102
Cdd:PRK07877 100 EEQERLGRLRIGVVGLS-VGHAIAHTLAAEGLcGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDPYLP 177

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 639317339 103 IVTHCRKLDESNATNMLKDADIILDCSDNFSTRYSV 138
Cdd:PRK07877 178 VEVFTDGLTEDNVDAFLDGLDVVVEECDSLDVKVLL 213
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 34-150 1.13e-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: 37.95  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639317339   34 VAVVGAGGLGSPALLYLAAAG-VGTLILIDDDEvelsnlqrqvlykinhlgqnkvAAAGKVLASLNNQINIvthCRKLDE 112
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdVDRITVADRTL----------------------EKAQALAAKLGGVRFI---AVAVDA 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 639317339  113 SNATN----MLKDADIILDCSDNFSTRySVNRYCIANKTPLI 150
Cdd:pfam03435  56 DNYEAvlaaLLKEGDLVVNLSPPTLSL-DVLKACIETGVHYV 96
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
32-62 1.18e-03

Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 39.68  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 639317339  32 STVAVVGAGGLGSPALLYLAAAGVGTLILID 62
Cdd:COG1062  177 DTVAVFGLGGVGLSAVQGARIAGASRIIAVD 207
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 32-69 6.33e-03

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 37.36  E-value: 6.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 639317339  32 STVAVVGAGGLGSPALLYLAAAGVGTLILID--DDEVELS 69
Cdd:cd08281  193 QSVAVVGLGGVGLSALLGAVAAGASQVVAVDlnEDKLALA 232
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 32-65 6.38e-03

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 37.15  E-value: 6.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 639317339  32 STVAVVGAGGLGSPALLYLAAAGVGTLILIDDDE 65
Cdd:cd05284  169 STVVVIGVGGLGHIAVQILRALTPATVIAVDRSE 202
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 33-70 8.00e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 36.96  E-value: 8.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 639317339  33 TVAVVGAGGLGSPALLYLAAAGVGTLILIDDDEVELSN 70
Cdd:cd08263  190 TVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAK 227
 
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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