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Conserved domains on  [gi|193204635|ref|NP_001122615|]
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Glutathione gamma-glutamylcysteinyltransferase [Caenorhabditis elegans]

Protein Classification

phytochelatin synthase family protein( domain architecture ID 10523433)

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 ...
 17-224 3.46e-125

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: 360.71  E-value: 3.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   17 YRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESM 96
Cdd:pfam05023   1 YRRPLPPNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEEM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   97 LDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSpdFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSP 176
Cdd:pfam05023  81 LDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDS--SLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 193204635  177 LAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGL 224
Cdd:pfam05023 159 IGAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
 
Name Accession Description Interval E-value
Phytochelatin pfam05023
Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of ...
 17-224 3.46e-125

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: 360.71  E-value: 3.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   17 YRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESM 96
Cdd:pfam05023   1 YRRPLPPNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEEM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   97 LDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSpdFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSP 176
Cdd:pfam05023  81 LDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDS--SLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 193204635  177 LAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGL 224
Cdd:pfam05023 159 IGAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
 
Name Accession Description Interval E-value
Phytochelatin pfam05023
Phytochelatin synthase; Phytochelatin synthase is the enzyme responsible for the synthesis of ...
 17-224 3.46e-125

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: 360.71  E-value: 3.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   17 YRRPLPETCIEFSSELGKKLFTEALVRGSANIYFKLASQFRTQDEPAYCGLSTLVMVLNALEVDPEKVWKAPWRFYHESM 96
Cdd:pfam05023   1 YRRPLPPNLIAFSSPEGKKLFREALAEGTMEDYFPLASQFVTQSEPAYCGLATLVMVLNALAIDPGRVWKGPWRWFTEEM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193204635   97 LDCCVPLENIRKSGINLQQFSCLAKCNRLKSTVSYGDNSpdFLKKFRTSLVNSVRSDDQVLVASYDRSVLGQTGSGHFSP 176
Cdd:pfam05023  81 LDCCIPLEVVKRQGITLDEFACLAKCNGAKVQVYRASDS--SLEQFRKLVKANLSSPDNFVIVSYSRKVLGQTGGGHFSP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 193204635  177 LAAYHEDSDQVLIMDVARFKYPPHWVKLETLQKALCSVDVTTKLPRGL 224
Cdd:pfam05023 159 IGAYHEESDRVLILDVARFKYPPHWVPLELLWEAMNTIDPVTGKSRGY 206
 
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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