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Conserved domains on  [gi|2288724026|ref|WP_258238485|]
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ThiF family adenylyltransferase [Arcobacter sp. CECT 8986]

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]; ...
 6-198 6.82e-55

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: 175.70  E-value: 6.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKL--WGEETQDSLQNKKVAIIGSGglgcslgiALG--------ASGIGEFTLVDFDEVGVHNIHRQIGFKVGD 75
Cdd:COG0476     6 ERYSRQILLpeIGEEGQEKLKAARVLVVGAG--------GLGspvalylaAAGVGTLTLVDDDVVELSNLQRQILYTEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  76 DGKYKADVLKELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELlaGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2288724026 154 CFF---EKASYEAVF-----QINDRKPNGIACPIVMHIASLQANLAIRYLAGL 198
Cdd:COG0476   158 TVFipgDTPCYRCLFpeppePGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGI 210
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-198 6.82e-55

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: 175.70  E-value: 6.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKL--WGEETQDSLQNKKVAIIGSGglgcslgiALG--------ASGIGEFTLVDFDEVGVHNIHRQIGFKVGD 75
Cdd:COG0476     6 ERYSRQILLpeIGEEGQEKLKAARVLVVGAG--------GLGspvalylaAAGVGTLTLVDDDVVELSNLQRQILYTEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  76 DGKYKADVLKELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELlaGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2288724026 154 CFF---EKASYEAVF-----QINDRKPNGIACPIVMHIASLQANLAIRYLAGL 198
Cdd:COG0476   158 TVFipgDTPCYRCLFpeppePGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGI 210
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 8-212 1.47e-43

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: 146.25  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQI--KLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:pfam00899   1 YSRQLalPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYKESF-----QDFAKrglEFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFEK-- 158
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLtpenaEELIK---SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPgk 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2288724026 159 -ASYEAVFQINDRKP-------NGIACPIVMHIASLQANLAIRYLAGLTVKKDILYYLSFDN 212
Cdd:pfam00899 158 tPCYRCLFPEDPPPKlvpsctvAGVLGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDA 219
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 10-197 1.00e-42

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: 143.77  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  10 RQIKL--WGEETQDSLQNKKVAIIGSGglgcslgiALG--------ASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKY 79
Cdd:cd00757     4 RQILLpeIGEEGQEKLKNARVLVVGAG--------GLGspaaeylaAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  80 KADVLKELMESRCPYTKVTAY-----KESFQDFAKRgleFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVC 154
Cdd:cd00757    76 KAEAAAERLRAINPDVEIEAYnerldAENAEELIAG---YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVT 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2288724026 155 FF---EKASYEAVF------QINDRKPNGIACPIVMHIASLQANLAIRYLAG 197
Cdd:cd00757   153 VFipgEGPCYRCLFpeppppGVPSCAEAGVLGPLVGVIGSLQALEALKILLG 204
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-195 4.23e-36

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: 125.93  E-value: 4.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:TIGR02356   2 YARQLLLpdIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF----EKA 159
Cdd:TIGR02356  82 QRLRELNSDIQVTALKERVTAENLELLinNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFdpggEGP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288724026 160 SYEAVFQ-INDRKPN----GIACPIVMHIASLQANLAIRYL 195
Cdd:TIGR02356 162 CLRCLFPdIADTGPScataGVIGPVVGVIGSLQALEALKLL 202
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 10-198 1.58e-22

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 93.79  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  10 RQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKEL 87
Cdd:PRK05600   24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  88 MESRCPYTKVTAYKESFQdfAKRGLEF----DLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFEKASYEA 163
Cdd:PRK05600  104 LKEIQPDIRVNALRERLT--AENAVELlngvDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2288724026 164 VFQIND---RKPNGIACP----------IVMHIASLQANLAIRYLAGL 198
Cdd:PRK05600  182 GVGLRDlfpEQPSGDSIPdcatagvlgaTTAVIGALMATEAIKFLTGI 229
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 6-198 6.82e-55

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: 175.70  E-value: 6.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKL--WGEETQDSLQNKKVAIIGSGglgcslgiALG--------ASGIGEFTLVDFDEVGVHNIHRQIGFKVGD 75
Cdd:COG0476     6 ERYSRQILLpeIGEEGQEKLKAARVLVVGAG--------GLGspvalylaAAGVGTLTLVDDDVVELSNLQRQILYTEAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  76 DGKYKADVLKELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:COG0476    78 VGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELlaGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2288724026 154 CFF---EKASYEAVF-----QINDRKPNGIACPIVMHIASLQANLAIRYLAGL 198
Cdd:COG0476   158 TVFipgDTPCYRCLFpeppePGPSCAEAGVLGPLVGVIGSLQATEAIKLLTGI 210
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 8-212 1.47e-43

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: 146.25  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQI--KLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:pfam00899   1 YSRQLalPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYKESF-----QDFAKrglEFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFEK-- 158
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLtpenaEELIK---SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPgk 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2288724026 159 -ASYEAVFQINDRKP-------NGIACPIVMHIASLQANLAIRYLAGLTVKKDILYYLSFDN 212
Cdd:pfam00899 158 tPCYRCLFPEDPPPKlvpsctvAGVLGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDA 219
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 10-197 1.00e-42

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: 143.77  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  10 RQIKL--WGEETQDSLQNKKVAIIGSGglgcslgiALG--------ASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKY 79
Cdd:cd00757     4 RQILLpeIGEEGQEKLKNARVLVVGAG--------GLGspaaeylaAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  80 KADVLKELMESRCPYTKVTAY-----KESFQDFAKRgleFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVC 154
Cdd:cd00757    76 KAEAAAERLRAINPDVEIEAYnerldAENAEELIAG---YDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVT 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2288724026 155 FF---EKASYEAVF------QINDRKPNGIACPIVMHIASLQANLAIRYLAG 197
Cdd:cd00757   153 VFipgEGPCYRCLFpeppppGVPSCAEAGVLGPLVGVIGSLQALEALKILLG 204
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 8-195 4.23e-36

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: 125.93  E-value: 4.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:TIGR02356   2 YARQLLLpdIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF----EKA 159
Cdd:TIGR02356  82 QRLRELNSDIQVTALKERVTAENLELLinNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFdpggEGP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288724026 160 SYEAVFQ-INDRKPN----GIACPIVMHIASLQANLAIRYL 195
Cdd:TIGR02356 162 CLRCLFPdIADTGPScataGVIGPVVGVIGSLQALEALKLL 202
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 43-167 1.58e-26

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: 99.65  E-value: 1.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  43 ALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYTKVTAYKESFQDF--AKRGLEFDLIIDA 120
Cdd:cd01483    17 NLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDnlDDFLDGVDLVIDA 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2288724026 121 TDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFEKASYEAVFQI 167
Cdd:cd01483    97 IDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAAEAL 143
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 10-198 1.58e-22

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 93.79  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  10 RQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKEL 87
Cdd:PRK05600   24 RQLALpgFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAER 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  88 MESRCPYTKVTAYKESFQdfAKRGLEF----DLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFEKASYEA 163
Cdd:PRK05600  104 LKEIQPDIRVNALRERLT--AENAVELlngvDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVFNSGPDHR 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2288724026 164 VFQIND---RKPNGIACP----------IVMHIASLQANLAIRYLAGL 198
Cdd:PRK05600  182 GVGLRDlfpEQPSGDSIPdcatagvlgaTTAVIGALMATEAIKFLTGI 229
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 16-198 5.38e-21

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 89.77  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYT 95
Cdd:PRK07878   33 GVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  96 KVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV-CFFEKASYEAVFQINDRKP 172
Cdd:PRK07878  113 NVRLHEFRLDPSNAVELfsQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQAsVFWEDAPDGLGLNYRDLYP 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2288724026 173 N----------------GIACPivmHIASLQANLAIRYLAGL 198
Cdd:PRK07878  193 EppppgmvpscaeggvlGVLCA---SIGSIMGTEAIKLITGI 231
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 8-197 2.37e-20

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 86.05  E-value: 2.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:PRK05690   13 YNRQIILrgFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESAR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF----EKA 159
Cdd:PRK05690   93 AALARINPHIAIETINARLDDDELAALiaGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTVFtyqdDEP 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2288724026 160 SYEAVFQINdrKPNGIAC-------PIVMHIASLQANLAIRYLAG 197
Cdd:PRK05690  173 CYRCLSRLF--GENALTCveagvmaPLVGVIGSLQAMEAIKLLTG 215
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 16-142 5.43e-20

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: 84.58  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYT 95
Cdd:cd00755     2 GEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPEC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2288724026  96 KVTAYKESFQDFAKRGL---EFDLIIDATDNLPTRAAINEYCISKNQPWI 142
Cdd:cd00755    82 EVDAVEEFLTPDNSEDLlggDPDFVVDAIDSIRAKVALIAYCRKRKIPVI 131
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 6-140 1.59e-19

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: 83.59  E-value: 1.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKLWGEETQDSLQNKKVAIIGsgglgcslgI---------ALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDD 76
Cdd:COG1179     5 RRFSRTERLYGEEGLERLANAHVAVVG---------LggvgswaaeALARSGVGRLTLVDLDDVCESNINRQLHALDSTV 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2288724026  77 GKYKADVLKElmesRC----PYTKVTAYK-----ESFQDFAKRGleFDLIIDATDNLPTRAAINEYCISKNQP 140
Cdd:COG1179    76 GRPKVEVMAE----RIrdinPDCEVTAIDefvtpENADELLSED--YDYVIDAIDSVSAKAALIAWCRRRGIP 142
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
3-156 7.83e-18

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 80.93  E-value: 7.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   3 EIHEFFNRQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYK 80
Cdd:PRK07411   14 DEYERYSRHLILpeVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  81 ADVLKELMESRCPYTKVTAYKESFQdfAKRGLE----FDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF 156
Cdd:PRK07411   94 IESAKNRILEINPYCQVDLYETRLS--SENALDilapYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVF 171
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
16-156 1.25e-17

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 80.44  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYT 95
Cdd:PRK08762  126 GEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDV 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2288724026  96 KVTAYKESFQ-DFAKRGLE-FDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF 156
Cdd:PRK08762  206 QVEAVQERVTsDNVEALLQdVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVF 268
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
16-198 1.82e-14

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 69.50  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQiGFKVGDDGKYKADVLKELMESRCPYT 95
Cdd:PRK08644   19 TPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMPKVEALKENLLEINPFV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  96 KVTAY---------KESFQDfakrgleFDLIIDATDNLPTRAAINEYCISKNQPWI--------YGSVEEFhgQVCFFEK 158
Cdd:PRK08644   98 EIEAHnekidedniEELFKD-------CDIVVEAFDNAETKAMLVETVLEHPGKKLvaasgmagYGDSNSI--KTRRIGK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2288724026 159 ASYEAVFQINDRKP-NGIACPIVMHIASLQANLAIRYLAGL 198
Cdd:PRK08644  169 NFYIVGDFVTEAKPgNPLMAPRVNIAAAHQANLVLRLILGE 209
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 1-198 4.39e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 70.29  E-value: 4.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   1 MSEIHEFFNRQIKL--WGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGK 78
Cdd:PRK05597    2 KNLDIARYRRQIMLgeIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  79 YKADVLKELMESRCPYTKVTAYKESFQ-----DFAKrglEFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:PRK05597   82 PKAESAREAMLALNPDVKVTVSVRRLTwsnalDELR---DADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2288724026 154 CFFEKAS---YEAVF-------QINDRKPNGIACPIVMHIASLQANLAIRYLAGL 198
Cdd:PRK05597  159 SVFHAGHgpiYEDLFptppppgSVPSCSQAGVLGPVVGVVGSAMAMEALKLITGV 213
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 4-145 1.45e-13

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 68.60  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   4 IHEFFNRQI--KLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKY-- 79
Cdd:PRK12475    1 MQERYSRQIlfSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQKkp 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2288724026  80 KADVLKELMESRCPYTKVTAY-----KESFQDFAKrglEFDLIIDATDNLPTRAAINEYCISKNQPWIYGS 145
Cdd:PRK12475   81 KAIAAKEHLRKINSEVEIVPVvtdvtVEELEELVK---EVDLIIDATDNFDTRLLINDLSQKYNIPWIYGG 148
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 16-221 2.00e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 68.10  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGglgcslgiALGA--------SGIGEFTLVDFDEVGVHNIHRQIGFKVGD--DGKYKADVLK 85
Cdd:PRK07688   15 GEEGQQKLREKHVLIIGAG--------ALGTanaemlvrAGVGKVTIVDRDYVEWSNLQRQQLYTESDvkNNLPKAVAAK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  86 ELMESRCPYTKVTAYkesFQDFAKRGLE-----FDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFFekas 160
Cdd:PRK07688   87 KRLEEINSDVRVEAI---VQDVTAEELEelvtgVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTI---- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026 161 yeavfqINDRKP------------------NGIACPIVMHIASLQANLAIRYLAGltvKKDIL--YYLSFDndgVLQNQK 220
Cdd:PRK07688  160 ------IPGKTPclrcllqsiplggatcdtAGIISPAVQIVASYQVTEALKLLVG---DYEALrdGLVSFD---VWKNEY 227


                  .
gi 2288724026 221 F 221
Cdd:PRK07688  228 S 228
PRK08223 PRK08223
hypothetical protein; Validated
 2-199 3.39e-13

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 67.02  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   2 SEIHEFFNRQIKLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKA 81
Cdd:PRK08223    4 FDYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  82 DVLKELMESRCPYTKVTAYKESFQ-DFAKRGLE-FDLIIDATD--NLPTRAAINEYCISKNQPWIYGSVEEFHGQVCFF- 156
Cdd:PRK08223   84 EVLAEMVRDINPELEIRAFPEGIGkENADAFLDgVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFd 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2288724026 157 -EKASYEAVFQINDrkpngiACPivmhiaslQANLAIRYLAGLT 199
Cdd:PRK08223  164 pGGMSFDDYFDLSD------GMN--------EVEKAVRFLAGLA 193
PRK08328 PRK08328
hypothetical protein; Provisional
 6-153 5.75e-13

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 65.59  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKY-KADVL 84
Cdd:PRK08328    8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKNpKPLSA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2288724026  85 KELMESRCPYTKVTAY-----KESFQDFAKrglEFDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:PRK08328   88 KWKLERFNSDIKIETFvgrlsEENIDEVLK---GVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQV 158
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 16-130 6.78e-12

thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with one the E. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the divergent clade of putative ThiF proteins such found in Campylobacter. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 162819  Cd Length: 200  Bit Score: 62.19  E-value: 6.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  16 GEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQiGFKVGDDGKYKADVLKELMESRCPYT 95
Cdd:TIGR02354  12 TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQ-QYKASQVGEPKTEALKENISEINPYT 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2288724026  96 KVTAY-----KESFQDFAKrglEFDLIIDATDNLPTRAAI 130
Cdd:TIGR02354  91 EIEAYdekitEENIDKFFK---DADIVCEAFDNAEAKAML 127
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 42-192 2.57e-11

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 60.09  E-value: 2.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  42 IALGASGIGEFTLVDFDEVGVHNIHRQiGFKVGDDGKYKADVLKELMESRCPYTKVTAYKESFQDFAKRGL--EFDLIID 119
Cdd:cd01487    16 VLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLfgDCDIVVE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026 120 ATDNLPTRAAINEYCIS-KNQP--------WIYGSVEEFHGQVcffEKASYEAVFQINDRKP-NGIACPIVMHIASLQAN 189
Cdd:cd01487    95 AFDNAETKAMLAESLLGnKNKPvvcasgmaGFGDSNNIKTKKI---SDNFYICGDLVNEAKEgLGLMAPRVNICAAHQAN 171


                  ...
gi 2288724026 190 LAI 192
Cdd:cd01487   172 LVL 174
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 27-151 5.56e-11

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: 60.28  E-value: 5.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  27 KVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYTKVTAYKESFQD 106
Cdd:cd01484     1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2288724026 107 FAKRGLEF----DLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHG 151
Cdd:cd01484    81 EQDFNDTFfeqfHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKG 129
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 27-153 2.73e-10

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: 58.93  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  27 KVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYTKVTAYKESFQD 106
Cdd:cd01489     1 KVLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2288724026 107 fAKRGLE----FDLIIDATDNLPTRAAINEYCISKNQPWIYGSVEEFHGQV 153
Cdd:cd01489    81 -PDFNVEffkqFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQV 130
PRK14851 PRK14851
hypothetical protein; Provisional
 6-122 3.14e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 59.49  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   6 EFFNRQIKLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLK 85
Cdd:PRK14851   24 AAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKLAVMK 103

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2288724026  86 ELMESRCPYTKVTAYKESF-QDFAKRGLE-FDLIIDATD 122
Cdd:PRK14851  104 EQALSINPFLEITPFPAGInADNMDAFLDgVDVVLDGLD 142
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 43-134 1.40e-09

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 56.74  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  43 ALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYTKVTAYKE--SFQDFAKR-GLEFDLIID 119
Cdd:PRK15116   48 ALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDfiTPDNVAEYmSAGFSYVID 127

                          90
                  ....*....|....*
gi 2288724026 120 ATDNLPTRAAINEYC 134
Cdd:PRK15116  128 AIDSVRPKAALIAYC 142
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 27-153 6.92e-08

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


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 51.59  E-value: 6.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  27 KVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKELMESRCPYTKVTAYKESFQD 106
Cdd:cd01488     1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2288724026 107 ----FAKrglEFDLIIDATDNLPTRAAIN------------EYCIsknqPWIYGSVEEFHGQV 153
Cdd:cd01488    81 kdeeFYR---QFNIIICGLDSIEARRWINgtlvslllyedpESII----PLIDGGTEGFKGHA 136
PRK14852 PRK14852
hypothetical protein; Provisional
 8-122 3.24e-07

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 50.46  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKADVLKEL 87
Cdd:PRK14852  315 FSRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTER 394

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2288724026  88 MESRCPYTKVTAY-----KESFQDFAKrglEFDLIIDATD 122
Cdd:PRK14852  395 ALSVNPFLDIRSFpegvaAETIDAFLK---DVDLLVDGID 431
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 8-153 4.33e-07

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: 48.83  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKLWGEETQDSLQNKKVAIIGSGglgcslgiALGA--------SGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKY 79
Cdd:cd01492     4 YDRQIRLWGLEAQKRLRSARILLIGLK--------GLGAeiaknlvlSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026  80 KADVLKELMESRCPYTKVTAYKESF----QDFAKrglEFDLIIdATDnlPTRAA---INEYCISKNQPWIYGSVEEFHGQ 152
Cdd:cd01492    76 RAEASLERLRALNPRVKVSVDTDDIsekpEEFFS---QFDVVV-ATE--LSRAElvkINELCRKLGVKFYATGVHGLFGF 149


                  .
gi 2288724026 153 V 153
Cdd:cd01492   150 V 150
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 8-142 2.15e-06

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: 46.65  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKLWGEETQDSLQNKKVAIIGSGGLGCSLGIALGASGIGEFTLVDFDEVGVHNIHRQ--IGFKVGDDGKYKADVLK 85
Cdd:cd01485     2 YDRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAASY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2288724026  86 ELMESRCPYTKVTAYKE-------SFQDFAKRgleFDLIIDATDNLPTRAAINEYCISKNQPWI 142
Cdd:cd01485    82 EFLQELNPNVKLSIVEEdslsndsNIEEYLQK---FTLVIATEENYERTAKVNDVCRKHHIPFI 142
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 8-143 1.19e-03

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 39.21  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   8 FNRQIKLWGEETQDSLQNKKVAIIGSGglgcslgiALGAS--------GIGEFTLVD-----FDEVGVHnihrqigFKVG 74
Cdd:cd01493     3 YDRQLRLWGEHGQAALESAHVCLLNAT--------ATGTEilknlvlpGIGSFTIVDgskvdEEDLGNN-------FFLD 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2288724026  75 DD--GKYKADVLKELMESRCPYTKVTAYKESFQD--------FAKrgleFDLIIDATDNLPTRAAINEYCISKNQPWIY 143
Cdd:cd01493    68 ASslGKSRAEATCELLQELNPDVNGSAVEESPEAlldndpsfFSQ----FTVVIATNLPESTLLRLADVLWSANIPLLY 142
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 8-140 3.23e-03

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: 38.33  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026    8 FNRQIKLWGEETQDSLQNKKVAIIGSGGL-----GCSLGIALGASGIGEFTLVDFDEVGVHNIHRQIGFKVGDDGKYKAD 82
Cdd:TIGR01408  402 YDAQIAVFGDTFQQKLQNLNIFLVGCGAIgcemlKNFALMGVGTGKKGMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSY 481

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2288724026   83 VLKELMESRCPYTKVTAYKES--------FQDfakrglEF----DLIIDATDNLPTRAAINEYCISKNQP 140
Cdd:TIGR01408  482 TAADATLKINPQIKIDAHQNRvgpetetiFND------EFyeklDVVINALDNVEARRYVDSRCLAFLKP 545
 
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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