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Conserved domains on  [gi|516289913|ref|WP_017693220|]
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MULTISPECIES: D-cysteine desulfhydrase [Enterobacter]

Protein Classification

D-cysteine desulfhydrase family protein( domain architecture ID 10012093)

D-cysteine desulfhydrase family protein such as D-cysteine desulfhydrase, which catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives.

EC:  4.4.1.-
Gene Ontology:  GO:0030170|GO:0016846

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


:

Pssm-ID: 179673  Cd Length: 331  Bit Score: 534.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   4 QNLTRFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  84 TAAVAAKLGLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDALTDPAAQLDELATRLEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 164 LGALGYVESALEIAQQCEGAVSLSSVVVASG-SAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLAEGGVDFDAVVVASgSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 243 ALQ---AKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 516289913 320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 534.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   4 QNLTRFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  84 TAAVAAKLGLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDALTDPAAQLDELATRLEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 164 LGALGYVESALEIAQQCEGAVSLSSVVVASG-SAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLAEGGVDFDAVVVASgSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 243 ALQ---AKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 516289913 320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 2.88e-180

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 500.88  E-value: 2.88e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   12 LEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   92 GLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQV--EMVDALTDPAAQLDELATRLEAQGFRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETriESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  170 VESALEIAQQCEGAVSLSSVVVASGSAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLALQAKAE 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516289913  250 ILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEgPILFVHTGGAPALFAYHPHV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 2.45e-140

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 399.10  E-value: 2.45e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  19 TPLEYLPRFSDYLG--RDIFIKRDDVTPM-AMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  96 VALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDAL--TDPAAQLDELATRLEAQGFRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 173 ALEIAQQCEGAVSL-SSVVVASGSAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLALQAKAE-I 250
Cdd:cd06449  161 VLEIAQQEEELGFKfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516289913 251 LLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 3.33e-140

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 399.17  E-value: 3.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   8 RFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAV 87
Cdd:COG2515    1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  88 AAKLGLHCVALLENPIGTQAenyltNGNRLLLDLFNVQVEMVDALT--DPAAQLDELATRLEAQGFRPYVIPVGGSNALG 165
Cdd:COG2515   81 AAKLGLKCVLVLRGEEPTPL-----NGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 166 ALGYVESALEIAQQCEGAVSLssvvva-sgsagTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLAL 244
Cdd:COG2515  156 ALGYVEAAAELAAQLAELGVDfdyivvasgsggTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 245 QAKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGGAPALFAY 324
Cdd:COG2515  236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                 ..
gi 516289913 325 HP 326
Cdd:COG2515  316 AE 317
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 7.46e-46

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 157.47  E-value: 7.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   12 LEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   91 LGLHCVALLenPIGTqaenylTNGNRLLLDLFNVQVEMVDALTDPAAqldELATRLEAQGFRPYVIPVGGsNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVV--PEDA------PPGKLLLMRALGAEVVLVGGDYDEAV---AAARELAAEGPGAYYINQYD-NPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  171 ESALEIAQQCEGAVSLSSVVVASGsaGTHAGLAVGLEQLMPEVELIGV------TVSRSVADQKPKVVTLQQAVAEQLAL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPDAVVVPVGGG--GLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516289913  245 QAKAEILLW---DDYFAPGYGTPNDEGMEAVKLLARLEGILLDPvYTGKAMAGLiDGIARKRFKDEGPILFVHTG 316
Cdd:pfam00291 223 GDEPGALALdllDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 534.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   4 QNLTRFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  84 TAAVAAKLGLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDALTDPAAQLDELATRLEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 164 LGALGYVESALEIAQQCEGAVSLSSVVVASG-SAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLAEGGVDFDAVVVASgSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 243 ALQ---AKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 516289913 320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 2.88e-180

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 500.88  E-value: 2.88e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   12 LEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   92 GLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQV--EMVDALTDPAAQLDELATRLEAQGFRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETriESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  170 VESALEIAQQCEGAVSLSSVVVASGSAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLALQAKAE 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516289913  250 ILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEgPILFVHTGGAPALFAYHPHV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 2.45e-140

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 399.10  E-value: 2.45e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  19 TPLEYLPRFSDYLG--RDIFIKRDDVTPM-AMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  96 VALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDAL--TDPAAQLDELATRLEAQGFRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 173 ALEIAQQCEGAVSL-SSVVVASGSAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLALQAKAE-I 250
Cdd:cd06449  161 VLEIAQQEEELGFKfDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516289913 251 LLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 3.33e-140

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 399.17  E-value: 3.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   8 RFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAV 87
Cdd:COG2515    1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  88 AAKLGLHCVALLENPIGTQAenyltNGNRLLLDLFNVQVEMVDALT--DPAAQLDELATRLEAQGFRPYVIPVGGSNALG 165
Cdd:COG2515   81 AAKLGLKCVLVLRGEEPTPL-----NGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 166 ALGYVESALEIAQQCEGAVSLssvvva-sgsagTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAEQLAL 244
Cdd:COG2515  156 ALGYVEAAAELAAQLAELGVDfdyivvasgsggTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 245 QAKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVHTGGAPALFAY 324
Cdd:COG2515  236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                 ..
gi 516289913 325 HP 326
Cdd:COG2515  316 AE 317
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 5-324 3.59e-78

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 242.24  E-value: 3.59e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   5 NLTRFPRLEFIGAPTPLEYLPRFSDYLGR--DIFIKRDDVTP-MAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHV 81
Cdd:PRK12390   2 NLQKFPRYPLTFGPTPIHPLKRLSAHLGGkvELYAKREDCNSgLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  82 RQTAAVAAKLGLHCVALLENPIGTQAENYLTNGNRLLLDLFNVQVEMVDALTDPAAQ--LDELATRLEAQGFRPYVIPVG 159
Cdd:PRK12390  82 RQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPDGFDIGIRksWEDALEDVRAAGGKPYAIPAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 160 GS-NALGALGYVESALEIAQQ-CEGAVSLSSVVVASGSAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQA 237
Cdd:PRK12390 162 ASdHPLGGLGFVGFAEEVRAQeAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIARN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 238 VAEQLALQ---AKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGIARKRFKDEGPILFVH 314
Cdd:PRK12390 242 TAELVELGrdiTEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAH 321

                        330
                 ....*....|
gi 516289913 315 TGGAPALFAY 324
Cdd:PRK12390 322 LGGVPALNAY 331
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 6-324 8.63e-71

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 222.84  E-value: 8.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   6 LTRFPRLEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTA 85
Cdd:PRK14045   9 LSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  86 AVAAKLGLHCVALLenpigtQAENYLtNGNRLLLDLFNVQVEMVDAltDPAAQL----DELATRLEAQGFRPYVIPVGGS 161
Cdd:PRK14045  89 LAAKKLGLDAVLVL------RGKEEL-KGNYLLDKIMGIETRVYEA--KDSFELmkyaEEVAEELKGEGRKPYIIPPGGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 162 NALGALGYVESALEIAQQCEGAVSLSSVVVASG-SAGTHAGLAVGLEQLMPEVELIGVTVSRSVADQKPKVVTLQQAVAE 240
Cdd:PRK14045 160 SPVGTLGYVRAVGEIATQVKKLGVRFDSIVVAVgSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 241 QLALQAKAEILLWDDYFAPGYGTPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDgIARKRFKDEgPILFVHTGGAPA 320
Cdd:PRK14045 240 LLGVKVKVQEPELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMD-LAKKGELGE-KILFIHTGGISG 317


                 ....
gi 516289913 321 LFAY 324
Cdd:PRK14045 318 TFHY 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 7.46e-46

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 157.47  E-value: 7.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   12 LEFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTPMamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   91 LGLHCVALLenPIGTqaenylTNGNRLLLDLFNVQVEMVDALTDPAAqldELATRLEAQGFRPYVIPVGGsNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVV--PEDA------PPGKLLLMRALGAEVVLVGGDYDEAV---AAARELAAEGPGAYYINQYD-NPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  171 ESALEIAQQCEGAVSLSSVVVASGsaGTHAGLAVGLEQLMPEVELIGV------TVSRSVADQKPKVVTLQQAVAEQLAL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPDAVVVPVGGG--GLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516289913  245 QAKAEILLW---DDYFAPGYGTPNDEGMEAVKLLARLEGILLDPvYTGKAMAGLiDGIARKRFKDEGPILFVHTG 316
Cdd:pfam00291 223 GDEPGALALdllDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 19-317 2.43e-28

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 109.91  E-value: 2.43e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  19 TPLEYLPRFSDYLGRDIFIKRDDVTPMamGGNKLRKLEFLAADALREG---ADTLITAGAiqSNHVRQTAAVAAKLGLHC 95
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPT--GSFKDRGALNLILLAEEEGklpKGVIIESTG--GNTGIALAAAAARLGLKC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  96 VALLenPIGTQAENyltngnRLLLDLFNVQVEMVDALTDpAAQldELATRLEAQGFRPYVIPvGGSNALGALGYVESALE 175
Cdd:cd00640   77 TIVM--PEGASPEK------VAQMRALGAEVVLVPGDFD-DAI--ALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGLE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 176 IAQQCEGAVSLSSVVVASgSAGTHAGLAVGLEQLMPEVELIGVTvsrsvadqkPKVVTLqqavaeqlalqakaeillwdd 255
Cdd:cd00640  145 ILEQLGGQKPDAVVVPVG-GGGNIAGIARALKELLPNVKVIGVE---------PEVVTV--------------------- 193

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516289913 256 yfapgygtPNDEGMEAVKLLARLEGILLDPVyTGKAMAGLIDGiaRKRFKDEGPILFVHTGG 317
Cdd:cd00640  194 --------SDEEALEAIRLLAREEGILVEPS-SAAALAAALKL--AKKLGKGKTVVVILTGG 244
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 6-123 3.91e-06

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 48.27  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913   6 LTRFPRL--EFIGAPTPLEYLPRFSDYLGRDIFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVR 82
Cdd:PRK13803 257 QKTFKRLlqNYAGRPTPLTEAKRLSDIYGARIYLKREDLN--HTGSHKINNALGQALLAKRMGKTRIIAeTGAGQ--HGV 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516289913  83 QTAAVAAKLGLHCVALL-ENPIGTQAENYL------------TNGNRLLLDLFN 123
Cdd:PRK13803 333 ATATACALFGLKCTIFMgEEDIKRQALNVErmkllganvipvLSGSKTLKDAVN 386
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 13-96 4.25e-06

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 47.92  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  13 EFIGAPTPLEYLPRFSDYLGR-DIFIKRDDVTPmaMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTAAVAAK 90
Cdd:cd06446   29 DYVGRPTPLYRAKRLSEYLGGaKIYLKREDLNH--TGAHKINNALGQALLAKRMGKKRVIAeTGAGQ--HGVATATACAL 104


                 ....*.
gi 516289913  91 LGLHCV 96
Cdd:cd06446  105 FGLECE 110
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 19-316 1.50e-05

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 46.35  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  19 TPLEYLPRFSDYLGRDIFIKRDDVTP--------MAMGGNKlrkleflaadALREGADTLITA--GaiqsNHVRQTAAVA 88
Cdd:COG0498   67 TPLVKAPRLADELGKNLYVKEEGHNPtgsfkdraMQVAVSL----------ALERGAKTIVCAssG----NGSAALAAYA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  89 AKLGLHCVALLenPigtqaENYLTNGNRLLLDLFNVQVEMVDALTDPAAQL-DELAT-------------RLEAQ---GF 151
Cdd:COG0498  133 ARAGIEVFVFV--P-----EGKVSPGQLAQMLTYGAHVIAVDGNFDDAQRLvKELAAdeglyavnsinpaRLEGQktyAF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 152 ----------RPYVIPVG-GSNALGA-LGYVESaleiaqqcegavslssvvvasgsagthagLAVGLEQLMPevELIGV- 218
Cdd:COG0498  206 eiaeqlgrvpDWVVVPTGnGGNILAGyKAFKEL-----------------------------KELGLIDRLP--RLIAVq 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913 219 ------------------------TVSRSVADQKPkvVTLQQAVAeqlALQAKAEIllwddyfapGYGTPNDEGMEAVKL 274
Cdd:COG0498  255 atgcnpiltafetgrdeyeperpeTIAPSMDIGNP--SNGERALF---ALRESGGT---------AVAVSDEEILEAIRL 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 516289913 275 LARLEGILLDPvYTGKAMAGLIDGIARKRFKDEGPILFVHTG 316
Cdd:COG0498  321 LARREGIFVEP-ATAVAVAGLRKLREEGEIDPDEPVVVLSTG 361
PRK13802 PRK13802
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
 13-95 8.18e-04

bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 184335 [Multi-domain]  Cd Length: 695  Bit Score: 41.17  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  13 EFIGAPTPLEYLPRFSDYL----GRD--IFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTA 85
Cdd:PRK13802 321 RYVGRPSPLTEAPRFAERVkektGLDarVFLKREDLN--HTGAHKINNALGQALLVKRMGKTRVIAeTGAGQ--HGVATA 396

                         90
                 ....*....|
gi 516289913  86 AVAAKLGLHC 95
Cdd:PRK13802 397 TVCAMLGLKC 406
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
19-93 1.27e-03

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 40.51  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516289913  19 TPLEYLPRFSDYLGRDIFIKRDDVTPMAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGL 93
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVF--SFKLRgaynKMAQLTEEQLARG---VITASA--GNHAQGVALSAARLGI 92
PRK12483 PRK12483
threonine dehydratase; Reviewed
 19-96 1.81e-03

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 39.78  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  19 TPLEYLPRFSDYLGRDIFIKRDDVTPMAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGLH 94
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVF--SFKIRgaynKMARLPAEQLARG---VITASA--GNHAQGVALAAARLGVK 110


                 ..
gi 516289913  95 CV 96
Cdd:PRK12483 111 AV 112
PLN02618 PLN02618
tryptophan synthase, beta chain
 13-96 2.04e-03

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 39.74  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516289913  13 EFIGAPTPLEYLPRFSDYLGR------DIFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLITA-GAIQsnHVRQTA 85
Cdd:PLN02618  61 DYVGRETPLYFAERLTEHYKRadgegpEIYLKREDLN--HTGAHKINNAVAQALLAKRLGKKRIIAEtGAGQ--HGVATA 136

                         90
                 ....*....|.
gi 516289913  86 AVAAKLGLHCV 96
Cdd:PLN02618 137 TVCARFGLECI 147
 
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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