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Conserved domains on  [gi|17557472|ref|NP_503968|]
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Glutathione S-Transferase [Caenorhabditis elegans]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 10122574)

glutathione S-transferase (GST) family protein may catalyze the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress

CATH:  1.20.1050.10|3.40.30.10
PubMed:  15822171|15607001|11695986|15558583
SCOP:  4000976|4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-76 1.14e-31

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


:

Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 109.95  E-value: 1.14e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEenTLKNEMPFGQMPVLEVDGEKIPQSVAIARFVA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEL--DLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 87-195 2.87e-20

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


:

Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 81.90  E-value: 2.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  87 VEKAWADAFTDLYKDFLIDMKPWAmiafgYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLFF 166
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYF-----YEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLAL 75

                        90       100
                ....*....|....*....|....*....
gi 17557472 167 FETTTSLIELEKGFLGTDFPVVNAYFKRI 195
Cdd:cd03192  76 FDVLDYLLYLLPKDLLEKYPKLKALRERV 104
 
Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-76 1.14e-31

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 109.95  E-value: 1.14e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEenTLKNEMPFGQMPVLEVDGEKIPQSVAIARFVA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEL--DLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 87-195 2.87e-20

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 81.90  E-value: 2.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  87 VEKAWADAFTDLYKDFLIDMKPWAmiafgYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLFF 166
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYF-----YEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLAL 75

                        90       100
                ....*....|....*....|....*....
gi 17557472 167 FETTTSLIELEKGFLGTDFPVVNAYFKRI 195
Cdd:cd03192  76 FDVLDYLLYLLPKDLLEKYPKLKALRERV 104
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-199 2.63e-15

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 71.08  E-value: 2.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEID------DWIKEENtlknemPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeqksPEFLALN------PLGKVPVLVDDGLVLTESLAILEYLAE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  78 QLG---FAGQTPVEKAWADAFTdlykdFLIDMKPWAMIAFGYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLekSKSGFL 154
Cdd:COG0625  76 RYPeppLLPADPAARARVRQWL-----AWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL--AGGPYL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17557472 155 LDSGISFPDLFFFETTTSLIELekGFLGTDFPVVNAYFKRIAEHP 199
Cdd:COG0625 149 AGDRFSIADIALAPVLRRLDRL--GLDLADYPNLAAWLARLAARP 191
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 6-211 2.24e-12

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 63.46  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472    6 LHYFNARGYAEASRAMFHMAGVEFEDVRYEI--DDWIKEENTLK-NEMPFGQMPVLEVDGEKIPQSVAIARFVANQLGFA 82
Cdd:PTZ00057   7 LYYFDARGKAELIRLIFAYLGIEYTDKRFGEngDAFIEFKNFKKeKDTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKIC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   83 GQTPVEKAWADAFTDLYKDFLIDMKPWAMIafgypgaagdrDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFP 162
Cdd:PTZ00057  87 GESELNEFYADMIFCGVQDIHYKFNNTNLF-----------KQNETTFLNEELPKWSGYFENILKKNHCNYFVGDNLTYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17557472  163 DLFFFETTTSlIELEKGFLGTDFPVVNAYFKRIAEHPKLKPYLETRPYS 211
Cdd:PTZ00057 156 DLAVFNLYDD-IETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRKES 203
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 108-208 9.12e-12

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 59.49  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   108 PWAMIAFGYPGAagDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLFFFETTTSLIELEKGFLGTDFPV 187
Cdd:pfam14497   6 PIASSLYYEDEK--KKAKRRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDKYPK 83

                          90       100
                  ....*....|....*....|.
gi 17557472   188 VNAYFKRIAEHPKLKPYLETR 208
Cdd:pfam14497  84 LKALHERVAARPNIKAYLASR 104
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-77 4.93e-11

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 56.54  E-value: 4.93e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17557472     6 LHYFNARG--YAEASRAMFHMAGVEFEDVRYEIDDWIKEENTLKNEMPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:pfam02798   3 LTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
PLN02473 PLN02473
glutathione S-transferase
 22-84 3.27e-03

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 37.28  E-value: 3.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557472   22 FHMAGVEFEDVRYEID--DWIKEENTLKNemPFGQMPVLEvDGE-KIPQSVAIARFVANQlgFAGQ 84
Cdd:PLN02473  21 FLEKGIEFEVIHVDLDklEQKKPEHLLRQ--PFGQVPAIE-DGDlKLFESRAIARYYATK--YADQ 81
 
Name Accession Description Interval E-value
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 4-76 1.14e-31

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 109.95  E-value: 1.14e-31
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEenTLKNEMPFGQMPVLEVDGEKIPQSVAIARFVA 76
Cdd:cd03039   1 YKLTYFNIRGRGEPIRLLLADAGVEYEDVRITYEEWPEL--DLKPTLPFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 87-195 2.87e-20

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 81.90  E-value: 2.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  87 VEKAWADAFTDLYKDFLIDMKPWAmiafgYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLFF 166
Cdd:cd03192   1 EEEARVDAIVDTIADLRAEFAPYF-----YEPDGEEKKEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLAL 75

                        90       100
                ....*....|....*....|....*....
gi 17557472 167 FETTTSLIELEKGFLGTDFPVVNAYFKRI 195
Cdd:cd03192  76 FDVLDYLLYLLPKDLLEKYPKLKALRERV 104
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 4-76 2.59e-18

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 75.69  E-value: 2.59e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEENTLKNemPFGQMPVLEVDGEKIPQSVAIARFVA 76
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALN--PLGKVPVLEDGGLVLTESLAILEYLA 71
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-199 2.63e-15

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 71.08  E-value: 2.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEID------DWIKEENtlknemPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeqksPEFLALN------PLGKVPVLVDDGLVLTESLAILEYLAE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  78 QLG---FAGQTPVEKAWADAFTdlykdFLIDMKPWAMIAFGYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLekSKSGFL 154
Cdd:COG0625  76 RYPeppLLPADPAARARVRQWL-----AWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARL--AGGPYL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 17557472 155 LDSGISFPDLFFFETTTSLIELekGFLGTDFPVVNAYFKRIAEHP 199
Cdd:COG0625 149 AGDRFSIADIALAPVLRRLDRL--GLDLADYPNLAAWLARLAARP 191
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-77 3.67e-15

GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.


Pssm-ID: 239374 [Multi-domain]  Cd Length: 73  Bit Score: 67.34  E-value: 3.67e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557472   3 KYRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEentLKNEMPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:cd03076   1 PYTLTYFPVRGRAEAIRLLLADQGISWEEERVTYEEWQES---LKPKMLFGQLPCFKDGDLTLVQSNAILRHLGR 72
PTZ00057 PTZ00057
glutathione s-transferase; Provisional
 6-211 2.24e-12

glutathione s-transferase; Provisional


Pssm-ID: 173353 [Multi-domain]  Cd Length: 205  Bit Score: 63.46  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472    6 LHYFNARGYAEASRAMFHMAGVEFEDVRYEI--DDWIKEENTLK-NEMPFGQMPVLEVDGEKIPQSVAIARFVANQLGFA 82
Cdd:PTZ00057   7 LYYFDARGKAELIRLIFAYLGIEYTDKRFGEngDAFIEFKNFKKeKDTPFEQVPILEMDNIIFAQSQAIVRYLSKKYKIC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   83 GQTPVEKAWADAFTDLYKDFLIDMKPWAMIafgypgaagdrDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFP 162
Cdd:PTZ00057  87 GESELNEFYADMIFCGVQDIHYKFNNTNLF-----------KQNETTFLNEELPKWSGYFENILKKNHCNYFVGDNLTYA 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 17557472  163 DLFFFETTTSlIELEKGFLGTDFPVVNAYFKRIAEHPKLKPYLETRPYS 211
Cdd:PTZ00057 156 DLAVFNLYDD-IETKYPNSLKNFPLLKAHNEFISNLPNIKNYISNRKES 203
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 108-208 9.12e-12

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 59.49  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   108 PWAMIAFGYPGAagDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLFFFETTTSLIELEKGFLGTDFPV 187
Cdd:pfam14497   6 PIASSLYYEDEK--KKAKRRKEFREERLPKFLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDKYPK 83

                          90       100
                  ....*....|....*....|.
gi 17557472   188 VNAYFKRIAEHPKLKPYLETR 208
Cdd:pfam14497  84 LKALHERVAARPNIKAYLASR 104
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-77 4.93e-11

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 56.54  E-value: 4.93e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17557472     6 LHYFNARG--YAEASRAMFHMAGVEFEDVRYEIDDWIKEENTLKNEMPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:pfam02798   3 LTLYGIRGspRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-78 2.06e-10

GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 239375  Cd Length: 79  Bit Score: 55.23  E-value: 2.06e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17557472   3 KYRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWIKEentLKNE--MPFGQMPVLEVDGEKIPQSVAIARFVANQ 78
Cdd:cd03077   1 KPVLHYFNGRGRMESIRWLLAAAGVEFEEKFIESAEDLEK---LKKDgsLMFQQVPMVEIDGMKLVQTRAILNYIAGK 75
GST_N_Mu cd03075
GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 6-79 7.46e-10

GST_N family, Class Mu subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1), thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 239373 [Multi-domain]  Cd Length: 82  Bit Score: 53.54  E-value: 7.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   6 LHYFNARGYAEASRAMFHMAGVEFEDVRYEIDD--------WIKEENTLKneMPFGQMPVLEVDGEKIPQSVAIARFVAN 77
Cdd:cd03075   3 LGYWDIRGLAQPIRLLLEYTGEKYEEKRYELGDapdydrsqWLNEKFKLG--LDFPNLPYYIDGDVKLTQSNAILRYIAR 80


                ..
gi 17557472  78 QL 79
Cdd:cd03075  81 KH 82
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 86-210 7.66e-08

C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumors.


Pssm-ID: 198319 [Multi-domain]  Cd Length: 126  Bit Score: 49.24  E-value: 7.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  86 PVEKAWADAFTDLYKDflIDMKPWAMIAFGYpgAAGDRDELKktSLdPAKEKYF-KLLSKRlekSKSGFLLDSGISFPDL 164
Cdd:cd03210   1 EKEAALIDMVNDGVED--LRLKYVRMIYQNY--EAGKDDYIK--DL-PEQLKPFeKLLAKN---NGKGFIVGDKISFADY 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17557472 165 FFFETTTSLIELEKGFLgTDFPVVNAYFKRIAEHPKLKPYLETRPY 210
Cdd:cd03210  71 NLFDLLDIHLVLAPGCL-DAFPLLKAFVERLSARPKLKAYLESDAF 115
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 117-199 3.28e-07

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 46.90  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472   117 PGAAGDRDELKKtsLDPAKEKYFKLLSKRLEKSKsgFLLDSGISFPDLFFFETTTSLIELEKGFLGTDFPVVNAYFKRIA 196
Cdd:pfam00043  15 PPEEKKEPEVDE--ALEKVARVLSALEEVLKGQT--YLVGDKLTLADIALAPALLWLYELDPACLREKFPNLKAWFERVA 90


                  ...
gi 17557472   197 EHP 199
Cdd:pfam00043  91 ARP 93
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 4-76 1.26e-05

GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 41.79  E-value: 1.26e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17557472   4 YRLHYFNARGYAEASRAMFHMAGVEFEDVRYEIDDWI--KEENTLKNemPFGQMPVLEVDGEKIPQSVAIARFVA 76
Cdd:cd03056   1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGEtrTPEFLALN--PNGEVPVLELDGRVLAESNAILVYLA 73
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 22-78 8.14e-05

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 39.56  E-value: 8.14e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17557472  22 FHMAGVEFEDVRYEID--DWIKEENTLKNemPFGQMPVLEVDGEKIPQSVAIARFVANQ 78
Cdd:cd03053  20 LEEKGVDYELVPVDLTkgEHKSPEHLARN--PFGQIPALEDGDLKLFESRAITRYLAEK 76
GST_C_Alpha cd03208
C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione ...
 86-206 4.16e-04

C-terminal, alpha helical domain of Class Alpha Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Alpha subfamily is composed of vertebrate GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 198317 [Multi-domain]  Cd Length: 135  Bit Score: 38.85  E-value: 4.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17557472  86 PVEKAWADAFTDLYKDFLidmkpwAMIAFGYPGAAGDRDELKKTSLDPAKEKYFKLLSKRLEKSKSGFLLDSGISFPDLF 165
Cdd:cd03208   1 LKERALIDMYVEGTADLM------EMIMMLPFLPPEEKEAKLALIKEKAKNRYFPVFEKVLKDHGQDFLVGNKLSRADVQ 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17557472 166 FFETTTSLIELEKGFLgTDFPVVNAYFKRIAEHPKLKPYLE 206
Cdd:cd03208  75 LLEAILMVEELDPSIL-SDFPLLQAFKTRISNIPTIKKFLQ 114
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 27-75 8.75e-04

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 36.89  E-value: 8.75e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 17557472  27 VEFEDVRYEIDDWIKEENTLKNemPFGQMPVLEV-DGEKIPQSVAIARFV 75
Cdd:cd03051  26 VPLVTVDLAAGEQRSPEFLAKN--PAGTVPVLELdDGTVITESVAICRYL 73
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 14-78 9.43e-04

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 36.45  E-value: 9.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557472    14 YAEASRAMFHMAGVEFEDVRYEIDDWIKEEnTLKNEMPFGQMPVLEV-DGEKIPQSVAIARFVANQ 78
Cdd:pfam13409   4 FSHRVRLALEEKGLPYEIELVDLDPKDKPP-ELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEEL 68
PLN02473 PLN02473
glutathione S-transferase
 22-84 3.27e-03

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 37.28  E-value: 3.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17557472   22 FHMAGVEFEDVRYEID--DWIKEENTLKNemPFGQMPVLEvDGE-KIPQSVAIARFVANQlgFAGQ 84
Cdd:PLN02473  21 FLEKGIEFEVIHVDLDklEQKKPEHLLRQ--PFGQVPAIE-DGDlKLFESRAIARYYATK--YADQ 81
 
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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