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Conserved domains on  [gi|42568166|ref|NP_198569|]
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NAD(P)-binding Rossmann-fold superfamily protein [Arabidopsis thaliana]

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 ...
 83-317 9.16e-95

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: 285.27  E-value: 9.16e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  83 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 162
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 163 CHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSR 242
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42568166 243 SVRHRLrRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEdenPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVI 317
Cdd:cd00755 161 KVRKRL-RKRGIFFGVPVVYSTEPPDPPKADELVCGDE---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 ...
 83-317 9.16e-95

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: 285.27  E-value: 9.16e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  83 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 162
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 163 CHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSR 242
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42568166 243 SVRHRLrRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEdenPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVI 317
Cdd:cd00755 161 KVRKRL-RKRGIFFGVPVVYSTEPPDPPKADELVCGDE---VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 102-322 3.48e-62

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: 202.23  E-value: 3.48e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 102 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 181
Cdd:COG1179  33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 182 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLrRKHGIEGGIPVV 261
Cdd:COG1179 113 SEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRL-RKRGIPKGVKVV 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568166 262 FSLEKPKaKLLPFEGTNGEDENPLDYQvvpgfrvriipVLGTI---PAIFGQIMASYVITQLAG 322
Cdd:COG1179 192 YSTEQPR-KPQADGTVCDTGGTGLKCA-----------GPGSIsfvPAVFGLIAAGEVIRDLLG 243
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 79-322 4.10e-33

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: 125.06  E-value: 4.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166    79 NIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSS 158
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   159 IFPECHIEAKVMLYDSSSEEEILSgKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADirestiD 238
Cdd:pfam00899  86 INPDVEVEAYTERLTPENAEELIK-SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK------T 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   239 PLSRSvrhrlrrkhgieggipvVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIMASYVIT 318
Cdd:pfam00899 159 PCYRC-----------------LFP-EDPPPKLVPSCTVAG--------------------VLGPTTAVVAGLQALEALK 200


                  ....
gi 42568166   319 QLAG 322
Cdd:pfam00899 201 LLLG 204
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 102-265 4.33e-27

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 109.51  E-value: 4.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  102 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 181
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  182 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLRRKHGI----EG- 256
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDFGVvknsKGk 198

                        170
                 ....*....|
gi 42568166  257 -GIPVVFSLE 265
Cdd:PRK15116 199 lGVDCVFSTE 208
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 106-232 4.99e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 64.89  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATrADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSgKP 185
Cdd:TIGR02354  34 SNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYTEIEAYDEKITEENIDKFFK-DA 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42568166   186 DFVLDCIDNIDTKvGLLAACVKRGLK---VLSATGAGARADPTRIRVADI 232
Cdd:TIGR02354 112 DIVCEAFDNAEAK-AMLVNAVLEKYKdkyLIAASGLAGYDDANSIKTRKI 160
 
Name Accession Description Interval E-value
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 83-317 9.16e-95

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: 285.27  E-value: 9.16e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  83 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 162
Cdd:cd00755   1 YGEEGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 163 CHIEAKVMLYDSSSEEEILSGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSR 242
Cdd:cd00755  81 CEVDAVEEFLTPDNSEDLLGGDPDFVVDAIDSIRAKVALIAYCRKRKIPVISSMGAGGKLDPTRIRVADISKTSGDPLAR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42568166 243 SVRHRLrRKHGIEGGIPVVFSLEKPKAKLLPFEGTNGEdenPLDYQVVPGFRVRIIPVLGTIPAIFGQIMASYVI 317
Cdd:cd00755 161 KVRKRL-RKRGIFFGVPVVYSTEPPDPPKADELVCGDE---VGADAALQGLRRAGLGSASTVPAVFGLAIASEVI 231
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 102-322 3.48e-62

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: 202.23  E-value: 3.48e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 102 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 181
Cdd:COG1179  33 GGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEVMAERIRDINPDCEVTAIDEFVTPENADELL 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 182 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLrRKHGIEGGIPVV 261
Cdd:COG1179 113 SEDYDYVIDAIDSVSAKAALIAWCRRRGIPIISSMGAGGKLDPTKIRVADLSKTSNCPLAAKVRKRL-RKRGIPKGVKVV 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568166 262 FSLEKPKaKLLPFEGTNGEDENPLDYQvvpgfrvriipVLGTI---PAIFGQIMASYVITQLAG 322
Cdd:COG1179 192 YSTEQPR-KPQADGTVCDTGGTGLKCA-----------GPGSIsfvPAVFGLIAAGEVIRDLLG 243
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 79-322 4.10e-33

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: 125.06  E-value: 4.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166    79 NIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSS 158
Cdd:pfam00899   6 ALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAAERLRE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   159 IFPECHIEAKVMLYDSSSEEEILSgKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADirestiD 238
Cdd:pfam00899  86 INPDVEVEAYTERLTPENAEELIK-SFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGK------T 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   239 PLSRSvrhrlrrkhgieggipvVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIMASYVIT 318
Cdd:pfam00899 159 PCYRC-----------------LFP-EDPPPKLVPSCTVAG--------------------VLGPTTAVVAGLQALEALK 200


                  ....
gi 42568166   319 QLAG 322
Cdd:pfam00899 201 LLLG 204
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 102-265 4.33e-27

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 109.51  E-value: 4.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  102 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 181
Cdd:PRK15116  39 GGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFITPDNVAEYM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  182 SGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVADIRESTIDPLSRSVRHRLRRKHGI----EG- 256
Cdd:PRK15116 119 SAGFSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVVDLAKTIQDPLAAKLRERLKSDFGVvknsKGk 198

                        170
                 ....*....|
gi 42568166  257 -GIPVVFSLE 265
Cdd:PRK15116 199 lGVDCVFSTE 208
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 102-230 3.56e-25

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: 100.42  E-value: 3.56e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 102 GGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEIL 181
Cdd:cd01483   8 GGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISEDNLDDFL 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 42568166 182 sGKPDFVLDCIDNIDTKVGLLAACVKRGLKVLSATGAGARADPTRIRVA 230
Cdd:cd01483  88 -DGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQVIDIG 135
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 106-215 2.29e-24

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: 100.97  E-value: 2.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGkP 185
Cdd:COG0476  40 SPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGRPKVEAAAERLRALNPDVEVEAIPERLTEENALELLAG-A 118

                        90       100       110
                ....*....|....*....|....*....|
gi 42568166 186 DFVLDCIDNIDTKVGLLAACVKRGLKVLSA 215
Cdd:COG0476 119 DLVLDCTDNFATRYLLNDACVKLGIPLVSG 148
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 106-209 4.06e-24

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: 99.86  E-value: 4.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGkP 185
Cdd:cd00757  34 SPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAAAERLRAINPDVEIEAYNERLDAENAEELIAG-Y 112

                        90       100
                ....*....|....*....|....
gi 42568166 186 DFVLDCIDNIDTKVGLLAACVKRG 209
Cdd:cd00757 113 DLVLDCTDNFATRYLINDACVKLG 136
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 106-234 8.65e-18

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: 80.89  E-value: 8.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRaDVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILsGKP 185
Cdd:cd01487  12 SNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLS-QIGEPKVEALKENLREINPFVKIEAINIKIDENNLEGLF-GDC 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42568166 186 DFVLDCIDNIDTKVGLL-AACVKRGLKVLSATGAGARADPTRIRVADIRE 234
Cdd:cd01487  90 DIVVEAFDNAETKAMLAeSLLGNKNKPVVCASGMAGFGDSNNIKTKKISD 139
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
106-234 1.42e-17

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 81.06  E-value: 1.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVaTRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILsGKP 185
Cdd:PRK08644  41 SNIAVALARSGVGNLKLVDFDVVEPSNLNRQQY-FISQIGMPKVEALKENLLEINPFVEIEAHNEKIDEDNIEELF-KDC 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 42568166  186 DFVLDCIDNIDTKVGLLAACVKR-GLKVLSATGAGARADPTRIRVADIRE 234
Cdd:PRK08644 119 DIVVEAFDNAETKAMLVETVLEHpGKKLVAASGMAGYGDSNSIKTRRIGK 168
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 108-223 7.85e-14

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 71.03  E-value: 7.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  108 AASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDF 187
Cdd:PRK05690  47 ASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIGQPKVESARAALARINPHIAIETINARLDDDELAALIAGH-DL 125

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 42568166  188 VLDCIDNIDTKVGLLAACVKRGLKVLSatGAGARAD 223
Cdd:PRK05690 126 VLDCTDNVATRNQLNRACFAAKKPLVS--GAAIRME 159
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 109-210 2.77e-13

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


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 70.79  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  109 ASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADV--GIPKAMCLKKHFSSIFPECHIEAKVMlyDSSSE--EEILSGK 184
Cdd:PRK07688  40 AEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKAVAAKKRLEEINSDVRVEAIVQ--DVTAEelEELVTGV 117

                         90       100
                 ....*....|....*....|....*.
gi 42568166  185 pDFVLDCIDNIDTKVGLLAACVKRGL 210
Cdd:PRK07688 118 -DLIIDATDNFETRFIVNDAAQKYGI 142
thiF_fam2 TIGR02354
thiamine biosynthesis protein ThiF, family 2; Members of the HesA/MoeB/ThiF family of proteins ...
 106-232 4.99e-12

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


Pssm-ID: 162819  Cd Length: 200  Bit Score: 64.89  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   106 SHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATrADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSgKP 185
Cdd:TIGR02354  34 SNVAINLARAGIGKLILVDFDVVEPSNLNRQQYKA-SQVGEPKTEALKENISEINPYTEIEAYDEKITEENIDKFFK-DA 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 42568166   186 DFVLDCIDNIDTKvGLLAACVKRGLK---VLSATGAGARADPTRIRVADI 232
Cdd:TIGR02354 112 DIVCEAFDNAEAK-AMLVNAVLEKYKdkyLIAASGLAGYDDANSIKTRKI 160
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 74-198 9.22e-12

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 65.91  E-value: 9.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   74 EHLTRNIQF--FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVG--IPKA 149
Cdd:PRK12475   3 ERYSRQILFsgIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEEDAKqkKPKA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 42568166  150 MCLKKHFSSIFPECHIEAKVMlyDSSSEE-EILSGKPDFVLDCIDNIDTK 198
Cdd:PRK12475  83 IAAKEHLRKINSEVEIVPVVT--DVTVEElEELVKEVDLIIDATDNFDTR 130
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 83-198 4.30e-11

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 64.12  E-value: 4.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   83 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 162
Cdd:PRK05597  18 IGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKAESAREAMLALNPD 97

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 42568166  163 CHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTK 198
Cdd:PRK05597  98 VKVTVSVRRLTWSNALDELRDA-DVILDGSDNFDTR 132
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
47-215 2.84e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.57  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   47 AGNGIEsetRPDTVANGQDllkdEIVSEHLTrnIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFD 126
Cdd:PRK08762  98 AGLPLE---RPRLLTDEQD----ERYSRHLR--LPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  127 QVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTKVGLLAACV 206
Cdd:PRK08762 169 VVDRSNLQRQILHTEDRVGQPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDV-DVVVDGADNFPTRYLLNDACV 247


                 ....*....
gi 42568166  207 KRGLKVLSA 215
Cdd:PRK08762 248 KLGKPLVYG 256
PRK08328 PRK08328
hypothetical protein; Provisional
 74-198 6.01e-09

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 56.34  E-value: 6.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   74 EHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGI-PKAMCL 152
Cdd:PRK08328   8 ERYDRQIMIFGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLGKnPKPLSA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 42568166  153 KKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTK 198
Cdd:PRK08328  88 KWKLERFNSDIKIETFVGRLSEENIDEVLKGV-DVIVDCLDNFETR 132
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 83-334 1.71e-06

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 49.88  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   83 FGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPE 162
Cdd:PRK05600  31 FGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQILFGASDVGRPKVEVAAERLKEIQPD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  163 CHIEAKVMLYDSSSEEEILSGkPDFVLDCIDNIDTKvgllaacvkrglkvlsatgagaradptrIRVADIRESTIDPL-- 240
Cdd:PRK05600 111 IRVNALRERLTAENAVELLNG-VDLVLDGSDSFATK----------------------------FLVADAAEITGTPLvw 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  241 --------SRSVRHRLRRKHGIegGIPVVFSlEKPKAKLLPFEGTNGedenpldyqvvpgfrvriipVLGTIPAIFGQIM 312
Cdd:PRK05600 162 gtvlrfhgELAVFNSGPDHRGV--GLRDLFP-EQPSGDSIPDCATAG--------------------VLGATTAVIGALM 218

                        250       260
                 ....*....|....*....|...
gi 42568166  313 ASYVITQLAGV-QVQMEPIVNLD 334
Cdd:PRK05600 219 ATEAIKFLTGIgDVQPGTVLSYD 241
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 53-206 1.81e-06

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 50.09  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   53 SETRPDTVANGQDLLKDEIV--SEHLTrnIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSL 130
Cdd:PRK07878   2 STSLPPLVEPAAELTRDEVArySRHLI--IPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42568166  131 SSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCIDNIDTKVGLLAACV 206
Cdd:PRK07878  80 SNLQRQVIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQY-DLILDGTDNFATRYLVNDAAV 154
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
112-206 8.74e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 47.81  E-value: 8.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  112 LLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEakvmLYDS--SSEEEILSGKP-DFV 188
Cdd:PRK07411  57 LAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVGKPKIESAKNRILEINPYCQVD----LYETrlSSENALDILAPyDVV 132

                         90
                 ....*....|....*...
gi 42568166  189 LDCIDNIDTKVGLLAACV 206
Cdd:PRK07411 133 VDGTDNFPTRYLVNDACV 150
PRK07877 PRK07877
Rv1355c family protein;
118-216 7.81e-05

Rv1355c family protein;


Pssm-ID: 236122 [Multi-domain]  Cd Length: 722  Bit Score: 44.98  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  118 GKLLLVDFDQVSLSSLNRhAVATRADVGIPKAMCLKKHFSSIFPecHIEAKVML--YDSSSEEEILSGKpDFVLDCIDNI 195
Cdd:PRK07877 132 GELRLADFDTLELSNLNR-VPAGVFDLGVNKAVVAARRIAELDP--YLPVEVFTdgLTEDNVDAFLDGL-DVVVEECDSL 207

                         90       100
                 ....*....|....*....|.
gi 42568166  196 DTKVGLLAACVKRGLKVLSAT 216
Cdd:PRK07877 208 DVKVLLREAARARRIPVLMAT 228
PRK08223 PRK08223
hypothetical protein; Validated
 74-215 3.52e-04

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 42.36  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   74 EHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLK 153
Cdd:PRK08223   8 EAFCRNLGWITPTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLA 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42568166  154 KHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCID--NIDTKVGLLAACVKRGLKVLSA 215
Cdd:PRK08223  88 EMVRDINPELEIRAFPEGIGKENADAFLDGV-DVYVDGLDffEFDARRLVFAACQQRGIPALTA 150
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 118-206 1.43e-03

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: 40.74  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 118 GKLLLVDFDQVSLSSLNRHAVATRADVGIPKAMCLKKHFSSIFPECHIEAKVMLYDSSSEE---EILSGKPDFVLDCIDN 194
Cdd:cd01490  29 GEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQNRVGPETEHifnDEFWEKLDGVANALDN 108

                        90
                ....*....|..
gi 42568166 195 IDTKVGLLAACV 206
Cdd:cd01490 109 VDARMYVDRRCV 120
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 109-187 3.50e-03

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: 39.28  E-value: 3.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166 109 ASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADV--GIPKAMCLKKHFSSIFPECHIEAKV----MLYDSSSEEEILS 182
Cdd:cd01486  15 ARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTFEDCkgGKPKAEAAAERLKEIFPSIDATGIVlsipMPGHPISESEVPS 94


                ....*
gi 42568166 183 GKPDF 187
Cdd:cd01486  95 TLKDV 99
PRK14851 PRK14851
hypothetical protein; Provisional
 68-215 5.85e-03

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 39.07  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166   68 KDEIVSEHLTRNIQFFGLESQHKVTGSYVVVIGLGGVGSHAASMLLRSGVGKLLLVDFDQVSLSSLNRHAVATRADVGIP 147
Cdd:PRK14851  18 AAEYREAAFSRNIGLFTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEPVNVNRQFGARVPSFGRP 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42568166  148 KAMCLKKHFSSIFPECHIEAKVMLYDSSSEEEILSGKpDFVLDCID--NIDTKVGLLAACVKRGLKVLSA 215
Cdd:PRK14851  98 KLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGV-DVVLDGLDffQFEIRRTLFNMAREKGIPVITA 166
 
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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