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Conserved domains on  [gi|6322825|ref|NP_012898|]
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tRNA threonylcarbamoyladenosine dehydratase [Saccharomyces cerevisiae S288C]

Protein Classification

tRNA threonylcarbamoyladenosine dehydratase( domain architecture ID 10091512)

tRNA threonylcarbamoyladenosine dehydratase catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine to form cyclic t(6)A in tRNA

CATH:  2.40.30.180
EC:  6.1.-.-
Gene Ontology:  GO:0008641|GO:0061503|GO:0016887|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 76-314 7.45e-100

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: 297.98  E-value: 7.45e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   76 LGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPW 155
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  156 CEIDPINELWTLQNGERLTLGNgtPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPL 235
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD--PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322825  236 ARVVRRKLKKRGILSGIPVVFSAEKPDPKKAKLLPLPDEeyergkVDELSALKDFRVRILPVLGTMPSLFGLTITTWIL 314
Cdd:cd00755 159 ARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 76-314 7.45e-100

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: 297.98  E-value: 7.45e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   76 LGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPW 155
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  156 CEIDPINELWTLQNGERLTLGNgtPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPL 235
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD--PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322825  236 ARVVRRKLKKRGILSGIPVVFSAEKPDPKKAKLLPLPDEeyergkVDELSALKDFRVRILPVLGTMPSLFGLTITTWIL 314
Cdd:cd00755 159 ARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 104-321 2.51e-57

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: 189.14  E-value: 2.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  104 SLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLtLGNGtPDFI 183
Cdd:COG1179  42 ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADEL-LSED-YDYV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  184 VDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPLARVVRRKLKKRGILSGIPVVFSAEKPDP 263
Cdd:COG1179 120 IDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRK 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322825  264 kkakllPLPDEEYERGKVDELSAlkdfrvrilPVLGT---MPSLFGLTITTWILSNISDKP 321
Cdd:COG1179 200 ------PQADGTVCDTGGTGLKC---------AGPGSisfVPAVFGLIAAGEVIRDLLGKA 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-252 1.67e-31

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: 120.44  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825     72 NVEFLGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMRE 151
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    152 IAPWCEIDPINELWTLQNGERLTlgnGTPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDlatTE 231
Cdd:pfam00899  86 INPDVEVEAYTERLTPENAEELI---KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK---TP 159

                         170       180
                  ....*....|....*....|...
gi 6322825    232 --EDPLARVVRRKLKKRGILSGI 252
Cdd:pfam00899 160 cyRCLFPEDPPPKLVPSCTVAGV 182
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 97-259 1.37e-22

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 96.80  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    97 VGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTlg 176
Cdd:PRK15116  41 VGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM-- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   177 NGTPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPLARVVRRKLKK--------RGI 248
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSdfgvvknsKGK 198

                        170
                 ....*....|.
gi 6322825   249 LsGIPVVFSAE 259
Cdd:PRK15116 199 L-GVDCVFSTE 208
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 77-193 2.35e-08

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: 54.10  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825     77 GEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAIlNDVGTPKVECLRRHMREIAPWC 156
Cdd:TIGR02354  12 TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYT 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6322825    157 EIDPINELWTLQNGERLTlgnGTPDFIVDCIDNIDTK 193
Cdd:TIGR02354  91 EIEAYDEKITEENIDKFF---KDADIVCEAFDNAEAK 124
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 76-314 7.45e-100

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: 297.98  E-value: 7.45e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   76 LGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPW 155
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  156 CEIDPINELWTLQNGERLTLGNgtPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPL 235
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGD--PDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPL 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322825  236 ARVVRRKLKKRGILSGIPVVFSAEKPDPKKAKLLPLPDEeyergkVDELSALKDFRVRILPVLGTMPSLFGLTITTWIL 314
Cdd:cd00755 159 ARKVRKRLRKRGIFFGVPVVYSTEPPDPPKADELVCGDE------VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 104-321 2.51e-57

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: 189.14  E-value: 2.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  104 SLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLtLGNGtPDFI 183
Cdd:COG1179  42 ALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADEL-LSED-YDYV 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  184 VDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPLARVVRRKLKKRGILSGIPVVFSAEKPDP 263
Cdd:COG1179 120 IDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRLRKRGIPKGVKVVYSTEQPRK 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322825  264 kkakllPLPDEEYERGKVDELSAlkdfrvrilPVLGT---MPSLFGLTITTWILSNISDKP 321
Cdd:COG1179 200 ------PQADGTVCDTGGTGLKC---------AGPGSisfVPAVFGLIAAGEVIRDLLGKA 245
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-252 1.67e-31

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: 120.44  E-value: 1.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825     72 NVEFLGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMRE 151
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    152 IAPWCEIDPINELWTLQNGERLTlgnGTPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDlatTE 231
Cdd:pfam00899  86 INPDVEVEAYTERLTPENAEELI---KSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK---TP 159

                         170       180
                  ....*....|....*....|...
gi 6322825    232 --EDPLARVVRRKLKKRGILSGI 252
Cdd:pfam00899 160 cyRCLFPEDPPPKLVPSCTVAGV 182
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 95-231 2.84e-23

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: 95.03  E-value: 2.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   95 GGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELwtLQNGERLT 174
Cdd:cd01483   8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEG--ISEDNLDD 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322825  175 LGNGtPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTE 231
Cdd:cd01483  86 FLDG-VDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIGSLSAAE 141
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 97-259 1.37e-22

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 96.80  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    97 VGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTlg 176
Cdd:PRK15116  41 VGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM-- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   177 NGTPDFIVDCIDNIDTKVDLLEFAYNHGIKVISSMGASAKSDPTKLNVGDLATTEEDPLARVVRRKLKK--------RGI 248
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSdfgvvknsKGK 198

                        170
                 ....*....|.
gi 6322825   249 LsGIPVVFSAE 259
Cdd:PRK15116 199 L-GVDCVFSTE 208
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 95-209 1.71e-19

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: 87.11  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   95 GgvgswvvnSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLT 174
Cdd:COG0476  44 L--------YLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELL 115

                        90       100       110
                ....*....|....*....|....*....|....*
gi 6322825  175 LGngtPDFIVDCIDNIDTKVDLLEFAYNHGIKVIS 209
Cdd:COG0476 116 AG---ADLVLDCTDNFATRYLLNDACVKLGIPLVS 147
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
104-212 1.57e-16

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 77.97  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   104 SLVRSGCRKIRVVDFDQVSLSSLNRHSCAIlNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTLGNgtpDFI 183
Cdd:PRK08644  46 ALARSGVGNLKLVDFDVVEPSNLNRQQYFI-SQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELFKDC---DIV 121

                         90       100       110
                 ....*....|....*....|....*....|
gi 6322825   184 VDCIDNIDTKVDLLEFAYNH-GIKVISSMG 212
Cdd:PRK08644 122 VEAFDNAETKAMLVETVLEHpGKKLVAASG 151
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 104-219 1.80e-14

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


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 71.26  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825  104 SLVRSGCRKIRVVDFDQVSLSSLNRHScAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTlgnGTPDFI 183
Cdd:cd01487  17 LLARSGVGNLKLVDFDVVEPSNLNRQQ-YFLSQIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLF---GDCDIV 92

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6322825  184 VDCIDNIDTKVDLLE-FAYNHGIKVISSMGASAKSDP 219
Cdd:cd01487  93 VEAFDNAETKAMLAEsLLGNKNKPVVCASGMAGFGDS 129
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 95-210 7.80e-14

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: 70.58  E-value: 7.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   95 GGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNR---HSCAilnDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGE 171
Cdd:cd00757  30 GGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRqilHTEA---DVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAE 106

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6322825  172 RLTLGngtPDFIVDCIDNIDTKVDLLEFAYNHGIKVISS 210
Cdd:cd00757 107 ELIAG---YDLVLDCTDNFATRYLINDACVKLGKPLVSG 142
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 109-213 1.30e-10

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 61.40  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   109 GCRKIRVVDFDQVSLSSLNR---HSCAilnDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTLGNgtpDFIVD 185
Cdd:PRK05690  55 GVGTLTLVDFDTVSLSNLQRqvlHDDA---TIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGH---DLVLD 128

                         90       100
                 ....*....|....*....|....*...
gi 6322825   186 CIDNIDTKVDLLEFAYNHGIKVISsmGA 213
Cdd:PRK05690 129 CTDNVATRNQLNRACFAAKKPLVS--GA 154
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 77-193 2.35e-08

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: 54.10  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825     77 GEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAIlNDVGTPKVECLRRHMREIAPWC 156
Cdd:TIGR02354  12 TPKIVQKLEQATVAICGLGGLGSNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYT 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 6322825    157 EIDPINELWTLQNGERLTlgnGTPDFIVDCIDNIDTK 193
Cdd:TIGR02354  91 EIEAYDEKITEENIDKFF---KDADIVCEAFDNAEAK 124
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 62-215 1.79e-07

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 52.69  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    62 EQFIRQSLknnveF--LGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDV-- 137
Cdd:PRK07688   3 ERYSRQEL-----FspIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVkn 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   138 GTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTLGNgtpDFIVDCIDNIDTKVDLLEFAYNHGIKVI-----SSMG 212
Cdd:PRK07688  78 NLPKAVAAKKRLEEINSDVRVEAIVQDVTAEELEELVTGV---DLIIDATDNFETRFIVNDAAQKYGIPWIygacvGSYG 154


                 ...
gi 6322825   213 ASA 215
Cdd:PRK07688 155 LSY 157
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 76-193 1.41e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 50.26  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    76 LGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNR---HSCAilnDVGTPKVECLRRHMREI 152
Cdd:PRK05597  18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRqviHSTA---GVGQPKAESAREAMLAL 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6322825   153 APWCEIDPINELWTLQNGerLTLGNGTpDFIVDCIDNIDTK 193
Cdd:PRK05597  95 NPDVKVTVSVRRLTWSNA--LDELRDA-DVILDGSDNFDTR 132
PRK07877 PRK07877
Rv1355c family protein;
109-208 4.51e-06

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 49.22  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   109 GCRKIRVVDFDQVSLSSLNRHScAILNDVGTPKVECLRRHMREIAPWCEIDPINELWTLQNGERLTLGngtPDFIVDCID 188
Cdd:PRK07877 130 LCGELRLADFDTLELSNLNRVP-AGVFDLGVNKAVVAARRIAELDPYLPVEVFTDGLTEDNVDAFLDG---LDVVVEECD 205

                         90       100
                 ....*....|....*....|
gi 6322825   189 NIDTKVDLLEFAYNHGIKVI 208
Cdd:PRK07877 206 SLDVKVLLREAARARRIPVL 225
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 82-193 1.50e-05

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 46.80  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    82 EKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPKVECLRRHMREIAPWCEIDPI 161
Cdd:PRK05600  37 ERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPDIRVNAL 116

                         90       100       110
                 ....*....|....*....|....*....|..
gi 6322825   162 NELWTLQNGERLTlgnGTPDFIVDCIDNIDTK 193
Cdd:PRK05600 117 RERLTAENAVELL---NGVDLVLDGSDSFATK 145
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 62-221 3.72e-05

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 45.49  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    62 EQFIRQSLKNNVeflGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGT-- 139
Cdd:PRK12475   3 ERYSRQILFSGI---GEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKQkk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825   140 PKVECLRRHMREIAPWCEIDPINELWTLQNGERLTlgnGTPDFIVDCIDNIDTKVDLLEFAYNHGI-----KVISSMGAS 214
Cdd:PRK12475  80 PKAIAAKEHLRKINSEVEIVPVVTDVTVEELEELV---KEVDLIIDATDNFDTRLLINDLSQKYNIpwiygGCVGSYGVT 156


                 ....*..
gi 6322825   215 AKSDPTK 221
Cdd:PRK12475 157 YTIIPGK 163
PRK14851 PRK14851
hypothetical protein; Provisional
 62-215 3.53e-04

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 42.93  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    62 EQFIRQSLKNNVEFLGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGTPK 141
Cdd:PRK14851  19 AEYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRPK 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322825   142 VECLRRHMREIAPWCEIDPINELWTLQNGERLTLGngtPDFIVDCID--NIDTKVDLLEFAYNHGIKVISS--MGASA 215
Cdd:PRK14851  99 LAVMKEQALSINPFLEITPFPAGINADNMDAFLDG---VDVVLDGLDffQFEIRRTLFNMAREKGIPVITAgpLGYSS 173
PRK08223 PRK08223
hypothetical protein; Validated
 60-199 4.17e-03

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 38.90  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322825    60 YDEQFIRqslknNVEFLGEDTIEKLSNQYVVVVGAGGVGSWVVNSLVRSGCRKIRVVDFDQVSLSSLNRHSCAILNDVGT 139
Cdd:PRK08223   6 YDEAFCR-----NLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322825   140 PKVECLRRHMREIAPWCEI----DPInelwtlqngerltlgngTPDFIVDCIDNIDTKVDLLEF 199
Cdd:PRK08223  81 PKAEVLAEMVRDINPELEIrafpEGI-----------------GKENADAFLDGVDVYVDGLDF 127
 
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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