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Conserved domains on  [gi|114607912|ref|XP_001155930|]
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PREDICTED: glutamate--cysteine ligase catalytic subunit [Pan troglodytes]

Protein Classification

RpsA and GCS domain-containing protein (domain architecture ID 11955177)

RpsA and 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 ...
236-608 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: 738.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  236 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 315
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  316 PLKNNNYRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 392
Cdd:pfam03074  81 PLKNNKFRIPKSRYDSIDLYISGdprNLEEYNDIDLPIDEDIYKRLLENGIDELLAKHFAHLFIRDPLVIFSERIEQDDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  393 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 471
Cdd:pfam03074 161 TSTDHFENIQSTNWQTVRFKPPPPNSDgIGWRVEFRPMEVQLTDFENAAFSVFIVLLTRAILSFDLNFYIPISKVDENMK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  472 VAQKRDAVLQGMFYFRKDIckggnavvdgcgKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 551
Cdd:pfam03074 241 RAHKRDAVLNEKFWFRKNI------------FPNGSPTPVEDEYEEMTIDEIFNGKEGEFPGLIPLIRSYLDSVNVDVET 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 114607912  552 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 608
Cdd:pfam03074 309 RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
RpsA super family cl28253
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis];
22-76 4.79e-03

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member PRK00087:

Pssm-ID: 333073  Cd Length: 647  Bit Score: 39.93  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114607912  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
236-608 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: 738.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  236 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 315
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  316 PLKNNNYRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 392
Cdd:pfam03074  81 PLKNNKFRIPKSRYDSIDLYISGdprNLEEYNDIDLPIDEDIYKRLLENGIDELLAKHFAHLFIRDPLVIFSERIEQDDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  393 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 471
Cdd:pfam03074 161 TSTDHFENIQSTNWQTVRFKPPPPNSDgIGWRVEFRPMEVQLTDFENAAFSVFIVLLTRAILSFDLNFYIPISKVDENMK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  472 VAQKRDAVLQGMFYFRKDIckggnavvdgcgKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 551
Cdd:pfam03074 241 RAHKRDAVLNEKFWFRKNI------------FPNGSPTPVEDEYEEMTIDEIFNGKEGEFPGLIPLIRSYLDSVNVDVET 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 114607912  552 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 608
Cdd:pfam03074 309 RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
PRK00087 PRK00087
4-hydroxy-3-methylbut-2-enyl diphosphate reductase/S1 RNA-binding domain protein; Reviewed
22-76 4.79e-03

4-hydroxy-3-methylbut-2-enyl diphosphate reductase/S1 RNA-binding domain protein; Reviewed


Pssm-ID: 234623  Cd Length: 647  Bit Score: 39.93  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114607912  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
 
Name Accession Description Interval E-value
GCS pfam03074
Glutamate-cysteine ligase; This family represents the catalytic subunit of glutamate-cysteine ...
236-608 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: 738.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  236 IYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLE 315
Cdd:pfam03074   1 IYMDAMGFGMGCCCLQVTFQAPNIDEARYLYDQLAPLAPIMLALTAASPIFKGYLADTDVRWNVISASVDDRTPEERGEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  316 PLKNNNYRISKSRYDSIDSYLSK---CGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDA 392
Cdd:pfam03074  81 PLKNNKFRIPKSRYDSIDLYISGdprNLEEYNDIDLPIDEDIYKRLLENGIDELLAKHFAHLFIRDPLVIFSERIEQDDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  393 NESDHFENIQSTNWQTMRFKPPPPNSD-IGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMK 471
Cdd:pfam03074 161 TSTDHFENIQSTNWQTVRFKPPPPNSDgIGWRVEFRPMEVQLTDFENAAFSVFIVLLTRAILSFDLNFYIPISKVDENMK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114607912  472 VAQKRDAVLQGMFYFRKDIckggnavvdgcgKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDT 551
Cdd:pfam03074 241 RAHKRDAVLNEKFWFRKNI------------FPNGSPTPVEDEYEEMTIDEIFNGKEGEFPGLIPLIRSYLDSVNVDVET 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 114607912  552 RCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQI 608
Cdd:pfam03074 309 RCRLYKYLKLISKRASGELPTTARWIRNFVLNHPDYKQDSVVSDEINYDLLKACDRI 365
PRK00087 PRK00087
4-hydroxy-3-methylbut-2-enyl diphosphate reductase/S1 RNA-binding domain protein; Reviewed
22-76 4.79e-03

4-hydroxy-3-methylbut-2-enyl diphosphate reductase/S1 RNA-binding domain protein; Reviewed


Pssm-ID: 234623  Cd Length: 647  Bit Score: 39.93  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114607912  22 VRRHGILQFLHI----YHAVKdRHKDVLKWGDEVEYMLVSFDHENKKVRlvLSGEKVLE 76
Cdd:PRK00087 495 VDIGGVDGLLHVseisWGRVE-KPSDVLKVGDEIKVYILDIDKENKKLS--LSLKKLLP 550
rpsA PRK06299
30S ribosomal protein S1; Reviewed
26-67 6.44e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775  Cd Length: 565  Bit Score: 39.38  E-value: 6.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 114607912  26 GILQFLHIYHAVKDRHKD---VLKWGDEVEYMLVSFDHENKKVRL 67
Cdd:PRK06299 483 GVEGLIRASELSRDRVEDateVLKVGDEVEAKVINIDRKNRRISL 527
 
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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