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Conserved domains on  [gi|2527644665|ref|WP_288640907|]
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HesA/MoeB/ThiF family protein [uncultured Methanosphaera sp.]

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]; ...
 10-244 5.72e-68

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: 209.60  E-value: 5.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEV--FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKK 87
Cdd:COG0476     9 SRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  88 ESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL-TIITNDTPSY 166
Cdd:COG0476    89 RLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVtVFIPGDTPCY 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527644665 167 EELFKLKSNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMTsFRIIDF 244
Cdd:COG0476   169 RCLFPEPPEP-----------GPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPL-AGRLLLFDALTME-FRTIKL 233
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 10-244 5.72e-68

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: 209.60  E-value: 5.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEV--FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKK 87
Cdd:COG0476     9 SRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  88 ESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL-TIITNDTPSY 166
Cdd:COG0476    89 RLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVtVFIPGDTPCY 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527644665 167 EELFKLKSNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMTsFRIIDF 244
Cdd:COG0476   169 RCLFPEPPEP-----------GPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPL-AGRLLLFDALTME-FRTIKL 233
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 10-244 4.12e-63

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: 196.54  E-value: 4.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQ---KEvFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAK 86
Cdd:cd00757     3 SRQillPE-IGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  87 KESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIIT-NDTPS 165
Cdd:cd00757    82 ERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIpGEGPC 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527644665 166 YEELFKLKSNGKTLDKSKeylLGistkkpqVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMtSFRIIDF 244
Cdd:cd00757   162 YRCLFPEPPPPGVPSCAE---AG-------VLGPLVGVIGSLQALEALKILLGIGEPL-AGRLLLFDALSM-SFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 10-241 2.22e-56

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: 179.76  E-value: 2.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQ--KEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKK 87
Cdd:pfam00899   2 SRQlaLPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  88 ESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLT-IITNDTPSY 166
Cdd:pfam00899  82 RLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTvVIPGKTPCY 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527644665 167 EELFKLKsngktlDKSKEYLLGISTkkpQVLGTTPAIFGALEVNETIKYILESKDALFAPKVLLWDIFDMTSFRI 241
Cdd:pfam00899 162 RCLFPED------PPPKLVPSCTVA---GVLGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDALTMTFREL 227
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 16-216 9.75e-39

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: 133.64  E-value: 9.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  16 FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPN 95
Cdd:TIGR02356  11 IGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  96 LNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIITND--TPSYEELFKLK 173
Cdd:TIGR02356  91 IQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGgeGPCLRCLFPDI 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2527644665 174 SNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYI 216
Cdd:TIGR02356 171 ADT-----------GPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
1-148 1.38e-36

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 128.05  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   1 MTELYNQMISRqkevFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQiRSNLDTIDKS 80
Cdd:PRK08644    7 MEEFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527644665  81 KVEtAKKESL-KINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCA 148
Cdd:PRK08644   82 KVE-ALKENLlEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLEHPGKKLVAA 149
 
Name Accession Description Interval E-value
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 10-244 5.72e-68

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: 209.60  E-value: 5.72e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEV--FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKK 87
Cdd:COG0476     9 SRQILLpeIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  88 ESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL-TIITNDTPSY 166
Cdd:COG0476    89 RLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVtVFIPGDTPCY 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527644665 167 EELFKLKSNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMTsFRIIDF 244
Cdd:COG0476   169 RCLFPEPPEP-----------GPSCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPL-AGRLLLFDALTME-FRTIKL 233
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 10-244 4.12e-63

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: 196.54  E-value: 4.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQ---KEvFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAK 86
Cdd:cd00757     3 SRQillPE-IGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  87 KESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIIT-NDTPS 165
Cdd:cd00757    82 ERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIpGEGPC 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527644665 166 YEELFKLKSNGKTLDKSKeylLGistkkpqVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMtSFRIIDF 244
Cdd:cd00757   162 YRCLFPEPPPPGVPSCAE---AG-------VLGPLVGVIGSLQALEALKILLGIGEPL-AGRLLLFDALSM-SFRTLKL 228
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 10-241 2.22e-56

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: 179.76  E-value: 2.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQ--KEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKK 87
Cdd:pfam00899   2 SRQlaLPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  88 ESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLT-IITNDTPSY 166
Cdd:pfam00899  82 RLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTvVIPGKTPCY 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527644665 167 EELFKLKsngktlDKSKEYLLGISTkkpQVLGTTPAIFGALEVNETIKYILESKDALFAPKVLLWDIFDMTSFRI 241
Cdd:pfam00899 162 RCLFPED------PPPKLVPSCTVA---GVLGPTTAVVAGLQALEALKLLLGKGEPNLAGRLLQFDALTMTFREL 227
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 16-216 9.75e-39

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: 133.64  E-value: 9.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  16 FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPN 95
Cdd:TIGR02356  11 IGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVAAQRLRELNSD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  96 LNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIITND--TPSYEELFKLK 173
Cdd:TIGR02356  91 IQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDPGgeGPCLRCLFPDI 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2527644665 174 SNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYI 216
Cdd:TIGR02356 171 ADT-----------GPSCATAGVIGPVVGVIGSLQALEALKLL 202
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
1-148 1.38e-36

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 128.05  E-value: 1.38e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   1 MTELYNQMISRqkevFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQiRSNLDTIDKS 80
Cdd:PRK08644    7 MEEFEAMLASR----HTPKLLEKLKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQ-QYFISQIGMP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527644665  81 KVEtAKKESL-KINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCA 148
Cdd:PRK08644   82 KVE-ALKENLlEINPFVEIEAHNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLEHPGKKLVAA 149
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 22-147 1.41e-35

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: 126.18  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  22 EKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGY 101
Cdd:cd00755     7 EKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEVDAV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2527644665 102 DTTITPENISQIFKGN-DIVIDAVDNVYTRVMISREARKQNMAFIHC 147
Cdd:cd00755    87 EEFLTPDNSEDLLGGDpDFVVDAIDSIRAKVALIAYCRKRKIPVISS 133
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 21-145 3.72e-34

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: 122.88  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  21 QEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITG 100
Cdd:COG1179    19 LERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTA 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2527644665 101 YDTTITPENISQIFKGN-DIVIDAVDNVYTRVMISREARKQNMAFI 145
Cdd:COG1179    99 IDEFVTPENADELLSEDyDYVIDAIDSVSAKAALIAWCRRRGIPII 144
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 29-159 5.64e-32

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: 114.29  E-value: 5.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTITPE 108
Cdd:cd01483     2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISED 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2527644665 109 NISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTII 159
Cdd:cd01483    82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVI 132
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 1-223 2.69e-31

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 117.79  E-value: 2.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   1 MTELYnqmiSRQkEVFT---ESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQ-IRSNLDT 76
Cdd:PRK07688    1 MNERY----SRQ-ELFSpigEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQqLYTESDV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  77 IDK-SKVETAKKESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVG- 154
Cdd:PRK07688   76 KNNlPKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGl 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665 155 QLTIITNDTPSYEELFK-LKSNGKTLDKSkeyllGISTkkPQVLgttpaIFGALEVNETIKYILESKDAL 223
Cdd:PRK07688  156 SYTIIPGKTPCLRCLLQsIPLGGATCDTA-----GIIS--PAVQ-----IVASYQVTEALKLLVGDYEAL 213
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 1-242 4.39e-31

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 114.94  E-value: 4.39e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   1 MTELYNQMI---SRQ---KEVFTESQqEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNL 74
Cdd:PRK05690    2 MAELSDEEMlryNRQiilRGFDFDGQ-EKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  75 DTIDKSKVETAKKESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVG 154
Cdd:PRK05690   81 ATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665 155 QLTIIT--NDTPSYEELFKLKSNGktldkskeyllGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWD 232
Cdd:PRK05690  161 QVTVFTyqDDEPCYRCLSRLFGEN-----------ALTCVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPL-SGRLLLYD 228

                         250
                  ....*....|
gi 2527644665 233 IFDMtSFRII 242
Cdd:PRK05690  229 AMTM-QFREM 237
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
14-240 3.29e-29

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 112.80  E-value: 3.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  14 EVFTESQQeKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKIN 93
Cdd:PRK08762  124 EVGEEGQR-RLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALN 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  94 PNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIIT-----NDTPSYEE 168
Cdd:PRK08762  203 PDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSVFDagrqrGQAPCYRC 282

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527644665 169 LFKLKSNGKtldkskeylLGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMTsFR 240
Cdd:PRK08762  283 LFPEPPPPE---------LAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPL-TGRLLTFDALAMR-FR 343
PRK08328 PRK08328
hypothetical protein; Provisional
 11-243 2.16e-28

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 107.57  E-value: 2.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  11 RQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDK-SKVETAKKES 89
Cdd:PRK08328   12 RQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSAKWKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  90 LKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL-TIITNDTPSYEE 168
Cdd:PRK08328   92 ERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVtTIVPGKTKRLRE 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2527644665 169 LFklksngKTLDKSKEyllgistkKPQVLGTTPAIFGALEVNETIKYILESKDALFApKVLLWDIFdMTSFRIID 243
Cdd:PRK08328  172 IF------PKVKKKKG--------KFPILGATAGVIGSIQAMEVIKLITGYGEPLLN-KLLIVDLA-NNVFEVVE 230
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 29-148 9.77e-28

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 104.00  E-value: 9.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQiRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTITPE 108
Cdd:cd01487     2 VGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQ-QYFLSQIGEPKVEALKENLREINPFVKIEAINIKIDEN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2527644665 109 NISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCA 148
Cdd:cd01487    81 NLEGLFGDCDIVVEAFDNAETKAMLAESLLGNKNKPVVCA 120
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
21-240 1.19e-27

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 108.67  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  21 QEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITG 100
Cdd:PRK07411   33 QKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVDL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665 101 YDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIIT-NDTPSYEELFKlksngktl 179
Cdd:PRK07411  113 YETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATVFNyEGGPNYRDLYP-------- 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527644665 180 dKSKEYLLGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALfAPKVLLWDIFDMtSFR 240
Cdd:PRK07411  185 -EPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTL-SGRLLLYNALDM-KFR 242
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 16-241 5.95e-27

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 106.50  E-value: 5.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  16 FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPN 95
Cdd:PRK05600   31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  96 LNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIItNDTPSYEE-----LF 170
Cdd:PRK05600  111 IRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTVLRFHGELAVF-NSGPDHRGvglrdLF 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527644665 171 KLKSNGKTLDKSKEyllgistkkPQVLGTTPAIFGALEVNETIKYILESKDALFApKVLLWDIFDMT--SFRI 241
Cdd:PRK05600  190 PEQPSGDSIPDCAT---------AGVLGATTAVIGALMATEAIKFLTGIGDVQPG-TVLSYDALTATtrSFRV 252
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 1-223 1.40e-25

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 102.50  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   1 MTELYnqmiSRQkEVFT---ESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNR-QIRSNLDT 76
Cdd:PRK12475    1 MQERY----SRQ-ILFSgigEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRqQLYTEEDA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  77 IDKSKVETAKKESL-KINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVG- 154
Cdd:PRK12475   76 KQKKPKAIAAKEHLrKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGv 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527644665 155 QLTIITNDTPSYEELFK-LKSNGKTLDKSkeyllGIstkkpqvlgTTPA--IFGALEVNETIKYILESKDAL 223
Cdd:PRK12475  156 TYTIIPGKTPCLRCLMEhVPVGGATCDTA-----GI---------IQPAvqIVVAYQVTEALKILVEDFEAL 213
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 21-242 2.44e-24

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 99.78  E-value: 2.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  21 QEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITG 100
Cdd:PRK07878   37 QKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665 101 YDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIITNDTPsyeelfklksNGKTLD 180
Cdd:PRK07878  117 HEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSIYRFEGQASVFWEDAP----------DGLGLN 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527644665 181 KSKEYL------LGISTKKPQVLGTTPAIFGALEVNETIKYILESKDALFApKVLLWDIFDMTsFRII 242
Cdd:PRK07878  187 YRDLYPeppppgMVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLG-RLMVYDALEMT-YRTI 252
PRK08223 PRK08223
hypothetical protein; Validated
 4-190 4.10e-24

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 97.45  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   4 LYNQMISRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVE 83
Cdd:PRK08223    5 DYDEAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  84 TAKKESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVD--NVYTRVMISREARKQNMAFIHCAVETTVGQLTIITN 161
Cdd:PRK08223   85 VLAEMVRDINPELEIRAFPEGIGKENADAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDP 164

                         170       180
                  ....*....|....*....|....*....
gi 2527644665 162 DTPSYEELFKLKSNGKTLDKSKEYLLGIS 190
Cdd:PRK08223  165 GGMSFDDYFDLSDGMNEVEKAVRFLAGLA 193
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 16-170 3.08e-23

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 96.09  E-value: 3.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  16 FTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPN 95
Cdd:PRK05597   18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527644665  96 LNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTIITND-TPSYEELF 170
Cdd:PRK05597   98 VKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAGhGPIYEDLF 173
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 3-134 1.01e-21

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: 89.16  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   3 ELYNQMISRQkevfTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQiRSNLDTIDKSKV 82
Cdd:TIGR02354   2 EFRRALVARH----TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQ-QYKASQVGEPKT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2527644665  83 ETAKKESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMIS 134
Cdd:TIGR02354  77 EALKENISEINPYTEIEAYDEKITEENIDKFFKDADIVCEAFDNAEAKAMLV 128
PRK14851 PRK14851
hypothetical protein; Provisional
 3-196 4.43e-19

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 85.68  E-value: 4.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   3 ELYNQMISRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKV 82
Cdd:PRK14851   20 EYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPKL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  83 ETAKKESLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVD--NVYTRVMISREARKQNMAFIHCAVETTVGQLTIIT 160
Cdd:PRK14851  100 AVMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDffQFEIRRTLFNMAREKGIPVITAGPLGYSSAMLVFT 179

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2527644665 161 NDTPSYEELFKLKSNGKTLDKSKEYLLGISTKKPQV 196
Cdd:PRK14851  180 PQGMGFDDYFNIGGKMPEEQKYLRFAMGLAPRPTHI 215
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 29-159 2.02e-18

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: 82.43  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTIT-P 107
Cdd:cd01489     2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKdP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2527644665 108 ENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTII 159
Cdd:cd01489    82 DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVI 133
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 29-127 3.40e-17

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 78.31  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTITPE 108
Cdd:PRK15116   33 ICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPD 112

                          90       100
                  ....*....|....*....|
gi 2527644665 109 NISQIFKGN-DIVIDAVDNV 127
Cdd:PRK15116  113 NVAEYMSAGfSYVIDAIDSV 132
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 12-135 5.02e-16

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: 76.85  E-value: 5.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   12 QKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFE-----NLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAK 86
Cdd:TIGR01408  405 QIAVFGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVGtgkkgMITVTDPDLIEKSNLNRQFLFRPHHIGKPKSYTAA 484

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2527644665   87 KESLKINPNLNITGYDTTITP--ENI--SQIFKGNDIVIDAVDNVYTRVMISR 135
Cdd:TIGR01408  485 DATLKINPQIKIDAHQNRVGPetETIfnDEFYEKLDVVINALDNVEARRYVDS 537
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 29-167 1.40e-14

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: 70.69  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTITPE 108
Cdd:cd01484     2 VLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGPE 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527644665 109 NI--SQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL-TIITNDTPSYE 167
Cdd:cd01484    82 QDfnDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAqVILPGMTECIE 143
PRK14852 PRK14852
hypothetical protein; Provisional
 10-125 7.59e-14

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 70.49  E-value: 7.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKES 89
Cdd:PRK14852  316 SRNLGLVDYAGQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMTERA 395

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2527644665  90 LKINPNLNITGYDTTITPENISQIFKGNDIVIDAVD 125
Cdd:PRK14852  396 LSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGID 431
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 29-130 4.47e-13

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: 67.00  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDTTITPE 108
Cdd:cd01488     2 ILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQDK 81

                          90       100
                  ....*....|....*....|..
gi 2527644665 109 NISqIFKGNDIVIDAVDNVYTR 130
Cdd:cd01488    82 DEE-FYRQFNIIICGLDSIEAR 102
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 29-135 1.42e-11

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: 63.46  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFEN-----LTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKESLKINPNLNITGYDT 103
Cdd:cd01490     2 VFLVGAGAIGCELLKNFALMGVGTgesgeITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQN 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2527644665 104 TITP--ENI--SQIFKGNDIVIDAVDNVYTRVMISR 135
Cdd:cd01490    82 RVGPetEHIfnDEFWEKLDGVANALDNVDARMYVDR 117
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 10-159 1.23e-08

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: 53.19  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQ--IRSNLDTIDKSKVETAKK 87
Cdd:cd01485     3 DRQIRLWGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAASYE 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527644665  88 ESLKINP--NLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQLTII 159
Cdd:cd01485    83 FLQELNPnvKLSIVEEDSLSNDSNIEEYLQKFTLVIATEENYERTAKVNDVCRKHHIPFISCATYGLIGYAFFD 156
PRK07877 PRK07877
Rv1355c family protein;
10-140 3.77e-08

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 53.46  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEVFTESQQEKIRNTPVLVMGCGgLGGTVIEQLVRAG-FENLTIVDQDVFDKTNLNRqIRSNLDTIDKSKVETAKKE 88
Cdd:PRK07877   91 DRNRNKITAEEQERLGRLRIGVVGLS-VGHAIAHTLAAEGlCGELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARR 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2527644665  89 SLKINPNLNITGYDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQ 140
Cdd:PRK07877  169 IAELDPYLPVEVFTDGLTEDNVDAFLDGLDVVVEECDSLDVKVLLREAARAR 220
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 2-145 1.73e-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: 49.98  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   2 TELYNqmisRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSK 81
Cdd:cd01492     1 IALYD----RQIRLWGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527644665  82 VETAKKESLKINPNLNITGyDTTITPENISQIFKGNDIVIDAVDNVYTRVMISREARKQNMAFI 145
Cdd:cd01492    77 AEASLERLRALNPRVKVSV-DTDDISEKPEEFFSQFDVVVATELSRAELVKINELCRKLGVKFY 139
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 10-156 1.47e-05

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: 44.95  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  10 SRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKES 89
Cdd:cd01491     3 SRQLYVLGHEAMKKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEASQARL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527644665  90 LKINPNLNITGYDTTITPENISQifkgNDIVIDAVDNVYTRVMISREARKQNMAFIHCAVETTVGQL 156
Cdd:cd01491    83 AELNPYVPVTVSTGPLTTDELLK----FQVVVLTDASLEDQLKINEFCHSPGIKFISADTRGLFGSI 145
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 10-111 1.77e-05

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: 45.65  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665   10 SRQKEVFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTIDKSKVETAKKES 89
Cdd:TIGR01408    8 SRQLYVLGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVVKKL 87

                           90       100
                   ....*....|....*....|..
gi 2527644665   90 LKINPNLNITGYDTTITPENIS 111
Cdd:TIGR01408   88 AELNPYVHVSSSSVPFNEEFLD 109
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 15-138 5.28e-05

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


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 43.77  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  15 VFTESQQEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTI---DKSKVETAKKESLK 91
Cdd:TIGR01381 327 LHPDLQLERYSQLKVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSNFEDCllgGRGKAETAQKALKR 406

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527644665  92 INPNLNITGYDTTI-----------TPE------NISQIFKGNDIVIDAVDnvytrvmiSREAR 138
Cdd:TIGR01381 407 IFPSIQATGHRLTVpmpghpidekdVPElekdiaRLEQLIKDHDVVFLLLD--------SREAR 462
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 29-138 1.86e-04

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 41.98  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAGFENLTIVDQDVFDKTNLNRQIRSNLDTI--DKSKVETAKKESLKINPNLNITGYDTTI- 105
Cdd:cd01486     2 CLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVLSIp 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2527644665 106 -----TPENISQIFKgNDI-----VIDAVDNVYTrVMISREAR 138
Cdd:cd01486    82 mpghpISESEVPSTL-KDVkrleeLIKDHDVIFL-LTDSRESR 122
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 29-133 1.44e-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: 37.57  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  29 VLVMGCGGLGGTVIEQLVRAG-FENLTIVDQdvfdktnlnrqirsnldTIDKSKVETAKKESLKINPnlnitgydTTITP 107
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdVDRITVADR-----------------TLEKAQALAAKLGGVRFIA--------VAVDA 55

                          90       100       110
                  ....*....|....*....|....*....|
gi 2527644665 108 ENISQI----FKGNDIVIDAVDNVYTRVMI 133
Cdd:pfam03435  56 DNYEAVlaalLKEGDLVVNLSPPTLSLDVL 85
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 24-60 5.19e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 36.48  E-value: 5.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2527644665  24 IRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDQDV 60
Cdd:cd01065    17 LKGKKVLILGAGGAARAVAYALAELGAAKIVIVNRTL 53
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 21-126 7.71e-03

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. 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: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 36.82  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527644665  21 QEKIRNTPVLVMGCGGLGGTVIEQLVRAGFENLTIVDqdvfdktnlnrqirsnldtIDKSKVETAKKEslkinpnlnitG 100
Cdd:cd08240   171 MPLVADEPVVIIGAGGLGLMALALLKALGPANIIVVD-------------------IDEAKLEAAKAA-----------G 220

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2527644665 101 YDTTITPENIS---QIFK----GNDIVIDAVDN 126
Cdd:cd08240   221 ADVVVNGSDPDaakRIIKaaggGVDAVIDFVNN 253
 
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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