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Conserved domains on  [gi|15240084|ref|NP_199220|]
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phytochelatin synthase 1 (PCS1) [Arabidopsis thaliana]

Protein Classification

phytochelatin synthase family protein( domain architecture ID 10523434)

phytochelatin synthase family protein similar to phytochelatin synthase, also called glutathione gamma-glutamylcysteinyltransferase, that catalyzes the production of glutathione-derived peptides (phytochelatins) that bind heavy-metal ions, and is a key enzyme for heavy-metal detoxification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Phytochelatin pfam05023
Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of ...
7-213 1.71e-137

Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols. The crystal structure of a member of this family shows it to possess a papain fold. The enzyme catalyzes the deglycination of a GSH donor molecule. The enzyme contains a catalytic triad of cysteine, histidine and aspartate residues.


:

Pssm-ID: 461526  Cd Length: 206  Bit Score: 394.22  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084     7 YRRSLPsPPAIDFSSAEGKLIFNEALQKGTMEGFFRLISYFQTQSEPAYCGLASLSVVLNALSIDPGRKWKGPWRWFDES 86
Cdd:pfam05023   1 YRRPLP-PNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084    87 MLDCCEPLEVVKEKGISFGKVVCLAHCSGAKVEAFRTSQSTIDDFRKFVVKCTSSENCHMISTYHRGVFKQTGTGHFSPI 166
Cdd:pfam05023  80 MLDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDSSLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSPI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15240084   167 GGYNAERDMALILDVARFKYPPHWVPLKLLWEAMDSIDQSTGKRRGF 213
Cdd:pfam05023 160 GAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
Phytochelatin_C super family cl07822
Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized ...
231-458 1.67e-96

Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized domains are found at the C-terminus of plant phytochelatin synthases.


The actual alignment was detected with superfamily member pfam09328:

Pssm-ID: 401316  Cd Length: 252  Bit Score: 291.64  E-value: 1.67e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   231 CKDESWIEIAKYLKEDVPRLVSSQHVDSVEKIISVVFKSLPSNFNQFIRWVAEIRITEDSNQNLSAEEKSRLKLKQLVLK 310
Cdd:pfam09328   1 CKHESWVSVAKYLMDDVPLLLKSEDVKDVQEVLSVVFKSLPAEAGEFIKWVAEVRRQEDGGSSLSEEEKGRLAIKEEVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   311 EVHETELFKHINKFLST---------VGYEDSLTYAAAKACCQGAEILSGSP--SKEFCCRETCVKCIKGPDDSEGTVVT 379
Cdd:pfam09328  81 QVQETGLFKHVTDWLSSanscckhpiSGEEDSLPEIAASVCCQGAELLTGKLgsSGGYCCRETCVKCLKANGDKPITVVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   380 GVVVRDGNEQKVDLLVPSTQTE---CECGPE---ATYPAGNDVFTALLLALPPQTWSGIKDQALMHEMKQLISMASLPTL 453
Cdd:pfam09328 161 GTVVSGGSEQGVDMLVPSSREKsscCGSGLSnciGMHPSGNDVLTVLLLALPPSTWSGIKDEKLLAEIHGLVSTENLPTL 240

                  ....*
gi 15240084   454 LQEEV 458
Cdd:pfam09328 241 LQEEV 245
 
Name Accession Description Interval E-value
Phytochelatin pfam05023
Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of ...
7-213 1.71e-137

Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols. The crystal structure of a member of this family shows it to possess a papain fold. The enzyme catalyzes the deglycination of a GSH donor molecule. The enzyme contains a catalytic triad of cysteine, histidine and aspartate residues.


Pssm-ID: 461526  Cd Length: 206  Bit Score: 394.22  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084     7 YRRSLPsPPAIDFSSAEGKLIFNEALQKGTMEGFFRLISYFQTQSEPAYCGLASLSVVLNALSIDPGRKWKGPWRWFDES 86
Cdd:pfam05023   1 YRRPLP-PNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084    87 MLDCCEPLEVVKEKGISFGKVVCLAHCSGAKVEAFRTSQSTIDDFRKFVVKCTSSENCHMISTYHRGVFKQTGTGHFSPI 166
Cdd:pfam05023  80 MLDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDSSLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSPI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15240084   167 GGYNAERDMALILDVARFKYPPHWVPLKLLWEAMDSIDQSTGKRRGF 213
Cdd:pfam05023 160 GAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
Phytochelatin_C pfam09328
Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized ...
231-458 1.67e-96

Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized domains are found at the C-terminus of plant phytochelatin synthases.


Pssm-ID: 401316  Cd Length: 252  Bit Score: 291.64  E-value: 1.67e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   231 CKDESWIEIAKYLKEDVPRLVSSQHVDSVEKIISVVFKSLPSNFNQFIRWVAEIRITEDSNQNLSAEEKSRLKLKQLVLK 310
Cdd:pfam09328   1 CKHESWVSVAKYLMDDVPLLLKSEDVKDVQEVLSVVFKSLPAEAGEFIKWVAEVRRQEDGGSSLSEEEKGRLAIKEEVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   311 EVHETELFKHINKFLST---------VGYEDSLTYAAAKACCQGAEILSGSP--SKEFCCRETCVKCIKGPDDSEGTVVT 379
Cdd:pfam09328  81 QVQETGLFKHVTDWLSSanscckhpiSGEEDSLPEIAASVCCQGAELLTGKLgsSGGYCCRETCVKCLKANGDKPITVVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   380 GVVVRDGNEQKVDLLVPSTQTE---CECGPE---ATYPAGNDVFTALLLALPPQTWSGIKDQALMHEMKQLISMASLPTL 453
Cdd:pfam09328 161 GTVVSGGSEQGVDMLVPSSREKsscCGSGLSnciGMHPSGNDVLTVLLLALPPSTWSGIKDEKLLAEIHGLVSTENLPTL 240

                  ....*
gi 15240084   454 LQEEV 458
Cdd:pfam09328 241 LQEEV 245
 
Name Accession Description Interval E-value
Phytochelatin pfam05023
Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of ...
7-213 1.71e-137

Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols. The crystal structure of a member of this family shows it to possess a papain fold. The enzyme catalyzes the deglycination of a GSH donor molecule. The enzyme contains a catalytic triad of cysteine, histidine and aspartate residues.


Pssm-ID: 461526  Cd Length: 206  Bit Score: 394.22  E-value: 1.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084     7 YRRSLPsPPAIDFSSAEGKLIFNEALQKGTMEGFFRLISYFQTQSEPAYCGLASLSVVLNALSIDPGRKWKGPWRWFDES 86
Cdd:pfam05023   1 YRRPLP-PNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084    87 MLDCCEPLEVVKEKGISFGKVVCLAHCSGAKVEAFRTSQSTIDDFRKFVVKCTSSENCHMISTYHRGVFKQTGTGHFSPI 166
Cdd:pfam05023  80 MLDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDSSLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSPI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15240084   167 GGYNAERDMALILDVARFKYPPHWVPLKLLWEAMDSIDQSTGKRRGF 213
Cdd:pfam05023 160 GAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
Phytochelatin_C pfam09328
Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized ...
231-458 1.67e-96

Domain of unknown function (DUF1984); Members of this family of functionally uncharacterized domains are found at the C-terminus of plant phytochelatin synthases.


Pssm-ID: 401316  Cd Length: 252  Bit Score: 291.64  E-value: 1.67e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   231 CKDESWIEIAKYLKEDVPRLVSSQHVDSVEKIISVVFKSLPSNFNQFIRWVAEIRITEDSNQNLSAEEKSRLKLKQLVLK 310
Cdd:pfam09328   1 CKHESWVSVAKYLMDDVPLLLKSEDVKDVQEVLSVVFKSLPAEAGEFIKWVAEVRRQEDGGSSLSEEEKGRLAIKEEVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   311 EVHETELFKHINKFLST---------VGYEDSLTYAAAKACCQGAEILSGSP--SKEFCCRETCVKCIKGPDDSEGTVVT 379
Cdd:pfam09328  81 QVQETGLFKHVTDWLSSanscckhpiSGEEDSLPEIAASVCCQGAELLTGKLgsSGGYCCRETCVKCLKANGDKPITVVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240084   380 GVVVRDGNEQKVDLLVPSTQTE---CECGPE---ATYPAGNDVFTALLLALPPQTWSGIKDQALMHEMKQLISMASLPTL 453
Cdd:pfam09328 161 GTVVSGGSEQGVDMLVPSSREKsscCGSGLSnciGMHPSGNDVLTVLLLALPPSTWSGIKDEKLLAEIHGLVSTENLPTL 240

                  ....*
gi 15240084   454 LQEEV 458
Cdd:pfam09328 241 LQEEV 245
 
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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