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Conserved domains on  [gi|6322360|ref|NP_012434|]
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glutamate--cysteine ligase [Saccharomyces cerevisiae S288C]

Protein Classification

GCS domain-containing protein (domain architecture ID 10503665)

GCS domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
253-645 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


:

Pssm-ID: 308610  Cd Length: 365  Bit Score: 641.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    253 IYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVA 332
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    333 PLLPKYNKngfggiakdvqdkvleIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDkapLDYDLAKHFAH 412
Cdd:pfam03074  81 PLKNNKFR----------------IPKSRYDSIDLYISGDPRNLEEYNDIDLPIDEDIYKRLLENG---IDELLAKHFAH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    413 LYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPtqqatPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYL 492
Cdd:pfam03074 142 LFIRDPLVIFSERIEQDDETSTDHFENIQSTNWQTVRFKPP-----PPNSDGIGWRVEFRPMEVQLTDFENAAFSVFIVL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    493 IVDSILTFsdNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDV-----ETEDYSISEIFHNPEnGIFPQFVT 567
Cdd:pfam03074 217 LTRAILSF--DLNFYIPISKVDENMKRAHKRDAVLNEKFWFRKNIFPNGSPtpvedEYEEMTIDEIFNGKE-GEFPGLIP 293
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322360    568 PILCQKGFVTKDWKElkhsskHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRL 645
Cdd:pfam03074 294 LIRSYLDSVNVDVET------RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
253-645 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


Pssm-ID: 308610  Cd Length: 365  Bit Score: 641.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    253 IYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVA 332
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    333 PLLPKYNKngfggiakdvqdkvleIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDkapLDYDLAKHFAH 412
Cdd:pfam03074  81 PLKNNKFR----------------IPKSRYDSIDLYISGDPRNLEEYNDIDLPIDEDIYKRLLENG---IDELLAKHFAH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    413 LYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPtqqatPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYL 492
Cdd:pfam03074 142 LFIRDPLVIFSERIEQDDETSTDHFENIQSTNWQTVRFKPP-----PPNSDGIGWRVEFRPMEVQLTDFENAAFSVFIVL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    493 IVDSILTFsdNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDV-----ETEDYSISEIFHNPEnGIFPQFVT 567
Cdd:pfam03074 217 LTRAILSF--DLNFYIPISKVDENMKRAHKRDAVLNEKFWFRKNIFPNGSPtpvedEYEEMTIDEIFNGKE-GEFPGLIP 293
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322360    568 PILCQKGFVTKDWKElkhsskHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRL 645
Cdd:pfam03074 294 LIRSYLDSVNVDVET------RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
253-645 0e+00

Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ligase (E.C. 6.3.2.2), also known as gamma-glutamylcysteine synthetase (GCS). This enzyme catalyzes the rate limiting step in the biosynthesis of glutathione. The eukaryotic enzyme is a dimer of a heavy chain and a light chain with all the catalytic activity exhibited by the heavy chain (this family).


Pssm-ID: 308610  Cd Length: 365  Bit Score: 641.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    253 IYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAPAFKGWLADQDVRWNVISGAVDDRTPKERGVA 332
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    333 PLLPKYNKngfggiakdvqdkvleIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDkapLDYDLAKHFAH 412
Cdd:pfam03074  81 PLKNNKFR----------------IPKSRYDSIDLYISGDPRNLEEYNDIDLPIDEDIYKRLLENG---IDELLAKHFAH 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    413 LYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFKPPtqqatPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYL 492
Cdd:pfam03074 142 LFIRDPLVIFSERIEQDDETSTDHFENIQSTNWQTVRFKPP-----PPNSDGIGWRVEFRPMEVQLTDFENAAFSVFIVL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322360    493 IVDSILTFsdNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDV-----ETEDYSISEIFHNPEnGIFPQFVT 567
Cdd:pfam03074 217 LTRAILSF--DLNFYIPISKVDENMKRAHKRDAVLNEKFWFRKNIFPNGSPtpvedEYEEMTIDEIFNGKE-GEFPGLIP 293
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322360    568 PILCQKGFVTKDWKElkhsskHERLYYYLKLISDRASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRL 645
Cdd:pfam03074 294 LIRSYLDSVNVDVET------RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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