NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|779928464|ref|WP_045388243|]
View 

MULTISPECIES: glutathione S-transferase family protein [Klebsiella]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 11427749)

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
EC:  2.5.1.-
Gene Ontology:  GO:0006749|GO:0005515
PubMed:  11035031
SCOP:  4000976|4000472

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-197 8.57e-22

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 88.03  E-value: 8.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFS---TFDAFSQINPVVKAPTAVlDNGLLLMDSTLILQYFEMQAePR 77
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYLAERY-PE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464  78 RKLLAKNPHRLAEDMQLLGFILAASEKAVQNIYEhRLRPAekQHQPWIERVTQQLLAACHEWDARLAGRT--TAQQLDQV 155
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLE-RLAPE--KDPAAIARARAELARLLAVLEARLAGGPylAGDRFSIA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 779928464 156 MITSTVVWSFIQAMiptTIPPHDFKHIHGLAEACEALVAFKK 197
Cdd:COG0625  157 DIALAPVLRRLDRL---GLDLADYPNLAAWLARLAARPAFQR 195
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-197 8.57e-22

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 88.03  E-value: 8.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFS---TFDAFSQINPVVKAPTAVlDNGLLLMDSTLILQYFEMQAePR 77
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYLAERY-PE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464  78 RKLLAKNPHRLAEDMQLLGFILAASEKAVQNIYEhRLRPAekQHQPWIERVTQQLLAACHEWDARLAGRT--TAQQLDQV 155
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLE-RLAPE--KDPAAIARARAELARLLAVLEARLAGGPylAGDRFSIA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 779928464 156 MITSTVVWSFIQAMiptTIPPHDFKHIHGLAEACEALVAFKK 197
Cdd:COG0625  157 DIALAPVLRRLDRL---GLDLADYPNLAAWLARLAARPAFQR 195
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
3-78 1.01e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 79.19  E-value: 1.01e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779928464    3 LIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVlDNGLLLMDSTLILQYFEMQAEPRR 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 93-199 6.63e-18

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 75.32  E-value: 6.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464  93 QLLGFILAASEKAVQNIYEHRLRPAEKQHQPWIERVTQQLLAACHEWDARLAGRTTAqQLDQVMITSTVVWSFIQAMIPT 172
Cdd:cd03205    3 RLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGG-RLTLGDIAVACALGYLDFRFPE 81

                         90       100
                 ....*....|....*....|....*..
gi 779928464 173 TIPPHDFKHIHGLAEACEALVAFKKYP 199
Cdd:cd03205   82 LDWRAGHPALAAWFARFEARPSFQATP 108
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 1-127 2.30e-11

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 60.12  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVLDNGLLLMDSTLILQYFE-MQAEPRrk 79
Cdd:PRK10357   1 MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIElLNVAPA-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 779928464  80 LLAKNPHRLAEDMQLLGFILAASEKAVQNIYEHRlRPAEKQHQPWIER 127
Cdd:PRK10357  79 MLPRDPLAALRVRQLEALADGIMDAALVSVREQA-RPAAQQSEDELLR 125
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-197 8.57e-22

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 88.03  E-value: 8.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFS---TFDAFSQINPVVKAPTAVlDNGLLLMDSTLILQYFEMQAePR 77
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKgeqKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYLAERY-PE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464  78 RKLLAKNPHRLAEDMQLLGFILAASEKAVQNIYEhRLRPAekQHQPWIERVTQQLLAACHEWDARLAGRT--TAQQLDQV 155
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLE-RLAPE--KDPAAIARARAELARLLAVLEARLAGGPylAGDRFSIA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 779928464 156 MITSTVVWSFIQAMiptTIPPHDFKHIHGLAEACEALVAFKK 197
Cdd:COG0625  157 DIALAPVLRRLDRL---GLDLADYPNLAAWLARLAARPAFQR 195
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
3-78 1.01e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 79.19  E-value: 1.01e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779928464    3 LIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVlDNGLLLMDSTLILQYFEMQAEPRR 78
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEELYPGPP 75
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 93-199 6.63e-18

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 75.32  E-value: 6.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464  93 QLLGFILAASEKAVQNIYEHRLRPAEKQHQPWIERVTQQLLAACHEWDARLAGRTTAqQLDQVMITSTVVWSFIQAMIPT 172
Cdd:cd03205    3 RLEALADGICDAAVLIVYERRLRPEEKQHQPWIERQWGKIERALDALEAELGDLPGG-RLTLGDIAVACALGYLDFRFPE 81

                         90       100
                 ....*....|....*....|....*..
gi 779928464 173 TIPPHDFKHIHGLAEACEALVAFKKYP 199
Cdd:cd03205   82 LDWRAGHPALAAWFARFEARPSFQATP 108
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 9-71 6.23e-12

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 58.41  E-value: 6.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779928464    9 SPYVRRVAISLELYGIQF--VSVPLSVFSTFDAFSQINPVVKAPTAVLDNGLLLMDSTLILQYFE 71
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYeiELVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLE 66
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 1-127 2.30e-11

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 60.12  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVLDNGLLLMDSTLILQYFE-MQAEPRrk 79
Cdd:PRK10357   1 MKLIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIElLNVAPA-- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 779928464  80 LLAKNPHRLAEDMQLLGFILAASEKAVQNIYEHRlRPAEKQHQPWIER 127
Cdd:PRK10357  79 MLPRDPLAALRVRQLEALADGIMDAALVSVREQA-RPAAQQSEDELLR 125
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 1-71 8.97e-08

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: 47.57  E-value: 8.97e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTF-DAFSQINPVVKAPtAVLDNGLLLMDSTLILQYFE 71
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEqEEFLALNPLGKVP-VLEDGGLVLTESLAILEYLA 71
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 1-71 8.30e-07

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 44.96  E-value: 8.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVLDNGLLLMDSTLILQYFE 71
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYID 71
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 1-69 2.23e-06

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: 43.79  E-value: 2.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFS---TFDAFSQINPVVKAPtAVLDNGLLLMDSTLILQY 69
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKgehKSPEHLARNPFGQIP-ALEDGDLKLFESRAITRY 72
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 1-69 2.44e-06

GST_N family, unknown subfamily 3; 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: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 43.79  E-value: 2.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 779928464   1 MKLIGMMDSPYVR--RVAISLELYGIQFVSVPLSVFSTFDAFSQINPVVKAPTAVLDNGLLLMDSTLILQY 69
Cdd:cd03049    1 MKLLYSPTSPYVRkvRVAAHETGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEY 71
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 1-71 5.41e-06

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: 42.67  E-value: 5.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779928464   1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSV-----FStfDAFSQINPVVKAPTAVLDNGLLLMDSTLILQYFE 71
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLaageqRS--PEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 1-69 4.01e-04

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: 37.67  E-value: 4.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779928464    1 MKLIGMMDSPYVRRVAISLELYGIQFVSVPLSVFSTFDA---FSQINPVVKAPtAVLDNGLLLMDSTLILQY 69
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKspeLLKLNPLGKVP-ALEDGGKKLTESRAILEY 73
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH