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Conserved domains on  [gi|16129413|ref|NP_415971|]
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putative glutathione S-transferase YncG [Escherichia coli str. K-12 substr. MG1655]

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

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List of domain hits

 Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-203 7.44e-30

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


:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 109.22  E-value: 7.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   1 MIKVYG-VPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLaLENDEIMTETAAIALMVLDRRP 79
Cdd:COG0625   1 MMKLYGsPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLA-LNPLGKVPVL-VDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413  80 D--LAPPvGRAERQLFQRLLVWLVANVYPTFTFADypERWAPDAPEQLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTL 157
Cdd:COG0625  79 EppLLPA-DPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16129413 158 VDCYLCTMRTWGPGHEWFQDNATNISAIADAVCQLPKLQEVLKRNE 203
Cdd:COG0625 156 ADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAE 201
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-203 7.44e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 109.22  E-value: 7.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   1 MIKVYG-VPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLaLENDEIMTETAAIALMVLDRRP 79
Cdd:COG0625   1 MMKLYGsPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLA-LNPLGKVPVL-VDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413  80 D--LAPPvGRAERQLFQRLLVWLVANVYPTFTFADypERWAPDAPEQLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTL 157
Cdd:COG0625  79 EppLLPA-DPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16129413 158 VDCYLCTMRTWGPGHEWFQDNATNISAIADAVCQLPKLQEVLKRNE 203
Cdd:COG0625 156 ADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAE 201
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 2-79 1.99e-24

GST_N family, Class Beta 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 91.44  E-value: 1.99e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129413   2 IKVYGVPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLALENDEIMTETAAIALMVLDRRP 79
Cdd:cd03057   1 MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLA-INPKGQVPALVLDDGEVLTESAAILQYLADLHP 77
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 46-200 3.30e-15

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 70.87  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   46 TLNPLCQVPTLALENDEIMTETAAIALMVLDRRPD--LAPPVGRAERQlfqRLLVWLvaNVYPTFTFADYPERWAPDAPE 123
Cdd:PRK10542  45 AINPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDrqLLAPVGSLSRY---HTIEWL--NYIATELHKGFTPLFRPDTPE 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129413  124 QLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTLVDCYLCTMRTWGPGHEWFQDNATNISAIADAVCQLPKLQEVLK 200
Cdd:PRK10542 120 EYKPTVRAQLEKKFQYVDEALADEQWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAYMQRVAERPAVAAALK 196
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 17-78 2.44e-06

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 43.77  E-value: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129413    17 LMLTLADIPYQ--FVDVSGFDHegasRELLKTLNPLCQVPTLALENDEIMTETAAIALMvLDRR 78
Cdd:pfam13409  10 LALEEKGLPYEieLVDLDPKDK----PPELLALNPLGTVPVLVLPDGTVLTDSLVILEY-LEEL 68
 
Name Accession Description Interval E-value
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-203 7.44e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 109.22  E-value: 7.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   1 MIKVYG-VPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLaLENDEIMTETAAIALMVLDRRP 79
Cdd:COG0625   1 MMKLYGsPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLA-LNPLGKVPVL-VDDGLVLTESLAILEYLAERYP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413  80 D--LAPPvGRAERQLFQRLLVWLVANVYPTFTFADypERWAPDAPEQLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTL 157
Cdd:COG0625  79 EppLLPA-DPAARARVRQWLAWADGDLHPALRNLL--ERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFSI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 16129413 158 VDCYLCTMRTWGPGHEWFQDNATNISAIADAVCQLPKLQEVLKRNE 203
Cdd:COG0625 156 ADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAE 201
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 2-79 1.99e-24

GST_N family, Class Beta 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 91.44  E-value: 1.99e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129413   2 IKVYGVPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLALENDEIMTETAAIALMVLDRRP 79
Cdd:cd03057   1 MKLYYSPGACSLAPHIALEELGLPFELVRVDLRTKTQKGADYLA-INPKGQVPALVLDDGEVLTESAAILQYLADLHP 77
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 88-199 5.46e-21

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 83.45  E-value: 5.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413  88 AERQLFQRLLVWLVANVYPTFTFADYPERWAPDA-PEQLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTLVDCYLCTMR 166
Cdd:cd03188   1 LERARLLEWLNFIASELHKAFGPLFYPARWADDAlAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVL 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 16129413 167 TWGPGHEWFQDNATNISAIADAVCQLPKLQEVL 199
Cdd:cd03188  81 RWARAVGLDLSDWPHLAAYLARVAARPAVQAAL 113
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 46-200 3.30e-15

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 70.87  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   46 TLNPLCQVPTLALENDEIMTETAAIALMVLDRRPD--LAPPVGRAERQlfqRLLVWLvaNVYPTFTFADYPERWAPDAPE 123
Cdd:PRK10542  45 AINPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDrqLLAPVGSLSRY---HTIEWL--NYIATELHKGFTPLFRPDTPE 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16129413  124 QLKKNVIEYRKSLYIWLNSQLTAEPYAFGEQLTLVDCYLCTMRTWGPGHEWFQDNATNISAIADAVCQLPKLQEVLK 200
Cdd:PRK10542 120 EYKPTVRAQLEKKFQYVDEALADEQWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAYMQRVAERPAVAAALK 196
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 2-71 2.73e-07

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: 46.41  E-value: 2.73e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129413   2 IKVYGVPGWG-STISELMLTLADIPYQFVDVSGFDHEgasRELLKTLNPLCQVPTLaLENDEIMTETAAIA 71
Cdd:cd00570   1 LKLYYFPGSPrSLRVRLALEEKGLPYELVPVDLGEGE---QEEFLALNPLGKVPVL-EDGGLVLTESLAIL 67
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 2-79 1.04e-06

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 44.80  E-value: 1.04e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16129413   2 IKVYGVPGWGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLAlENDEIMTETAAIALMVLDRRP 79
Cdd:cd03046   1 ITLYHLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLA-INPLGKVPVLV-DGDLVLTESAAIILYLAEKYG 76
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 17-78 2.44e-06

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 43.77  E-value: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129413    17 LMLTLADIPYQ--FVDVSGFDHegasRELLKTLNPLCQVPTLALENDEIMTETAAIALMvLDRR 78
Cdd:pfam13409  10 LALEEKGLPYEieLVDLDPKDK----PPELLALNPLGTVPVLVLPDGTVLTDSLVILEY-LEEL 68
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 16-70 2.81e-06

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: 43.72  E-value: 2.81e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129413  16 ELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLALEnDEIMTETAAI 70
Cdd:cd03056  16 RLLLALLGIPYEWVEVDILKGETRTPEFLA-LNPNGEVPVLELD-GRVLAESNAI 68
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
17-80 8.64e-05

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 39.52  E-value: 8.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16129413    17 LMLTLADIPYQFVDVSGFDHegasRELLKTLNPLCQVPTLALeNDEIMTETAAIALMVLDRRPD 80
Cdd:pfam13417  15 IALNEKGLPYEFVPIPPGDH----PPELLAKNPLGKVPVLED-DGGILCESLAIIDYLEELYPG 73
sspA PRK09481
stringent starvation protein A; Provisional
 29-163 2.85e-04

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 40.46  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413   29 VDVSGFDHEGASRELLKtLNPLCQVPTLAleNDEIMTETAAIALMVLDRR---PDLAP--PVGRAErqlfQRLLVWLVAN 103
Cdd:PRK09481  36 VEIEQVEKDNLPQDLID-LNPYQSVPTLV--DRELTLYESRIIMEYLDERfphPPLMPvyPVARGE----SRLMMHRIEK 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129413  104 VYptFTFADYPERWAPDAPEQLKKnviEYRKSLyIWLNSQLTAEPYAFGEQLTLVDCYLC 163
Cdd:PRK09481 109 DW--YSLMNKIVNGSASEADAARK---QLREEL-LAIAPVFGEKPYFMSEEFSLVDCYLA 162
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 2-71 3.85e-03

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: 34.97  E-value: 3.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129413     2 IKVYGVPG-WGSTISELMLTLADIPYQFVDVSGFDHEGASRELLKtLNPLCQVPTLaLENDEIMTETAAIA 71
Cdd:pfam02798   3 LTLYGIRGsPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLK-LNPLGKVPAL-EDGGKKLTESRAIL 71
 
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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