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Conserved domains on  [gi|767932643|ref|XP_011530551|]
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glutathione S-transferase C-terminal domain-containing protein isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 423-541 1.25e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam13679:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 138  Bit Score: 62.59  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932643  423 RKQQQLNNLVYVV------TNQAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLS-NIWF 495
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767932643  496 IQANMEYFTGMFN-----IGVALHACGVATDMVIEHCIKTRASFVTC-PCCY 541
Cdd:pfam13679  81 LEGTIAGSTPVELpdrvdVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
GstA super family cl33984
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
273-331 2.55e-04

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


The actual alignment was detected with superfamily member COG0625:

Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 42.58  E-value: 2.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932643 273 LEHVFAEGLY-----FTLADIVLLPCIHHFlviisRKFSEKLVEFPLLASWYQRIQEVPGVKTA 331
Cdd:COG0625  138 LEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLAAWLARLAARPAFQRA 196
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 423-541 1.25e-11

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 62.59  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932643  423 RKQQQLNNLVYVV------TNQAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLS-NIWF 495
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767932643  496 IQANMEYFTGMFN-----IGVALHACGVATDMVIEHCIKTRASFVTC-PCCY 541
Cdd:pfam13679  81 LEGTIAGSTPVELpdrvdVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 439-501 1.85e-05

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 44.98  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932643 439 AKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELGLsNIWFIQANME 501
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
273-331 2.55e-04

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 42.58  E-value: 2.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932643 273 LEHVFAEGLY-----FTLADIVLLPCIHHFlviisRKFSEKLVEFPLLASWYQRIQEVPGVKTA 331
Cdd:COG0625  138 LEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLAAWLARLAARPAFQRA 196
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 270-329 1.50e-03

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 38.31  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932643  270 LPPLEHVFA--EGLYF-----TLADIVLLPCIHHFLviiSRKFSEKLVEFPLLASWYQRIQEVPGVK 329
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLL---YPKAPDALDKYPKLKALHERVAARPNIK 98
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 442-501 3.18e-03

16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272928  Cd Length: 181  Bit Score: 39.16  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932643  442 GDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE--NKELSLIRAKKRsdELGLSNIWFIQANME 501
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAE 102
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 273-329 3.76e-03

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 37.93  E-value: 3.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932643 273 LEHVFAEGLYF------TLADIVLLPCIHHFLVIisRKFS-EKLV---EFPLLASWYQRIQEVPGVK 329
Cdd:cd03185   47 LEEELKGGKPFfggdtiGYLDIALGSFLGWFKAI--EEVGgVKLLdeeKFPLLAAWAERFLEREAVK 111
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 438-500 8.07e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.60  E-value: 8.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932643 438 QAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANM 500
Cdd:PRK09328 105 LLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW 167
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 423-541 1.25e-11

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 62.59  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932643  423 RKQQQLNNLVYVV------TNQAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLS-NIWF 495
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767932643  496 IQANMEYFTGMFN-----IGVALHACGVATDMVIEHCIKTRASFVTC-PCCY 541
Cdd:pfam13679  81 LEGTIAGSTPVELpdrvdVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 440-501 1.61e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 1.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932643  440 KPGDRIVDFCSGGGHVGIVLAH-MLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 501
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE 64
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 439-501 1.85e-05

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 44.98  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932643 439 AKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELGLsNIWFIQANME 501
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 440-498 2.17e-05

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 45.91  E-value: 2.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767932643 440 KPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIEnkelSLiraKKR-------SDELGLSNIWFIQA 498
Cdd:COG0357   66 KEGARVLDVGSGAGFPGIPLAIARPDLQVTLVD----SL---GKKiaflrevVRELGLKNVTVVHG 124
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
273-331 2.55e-04

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 42.58  E-value: 2.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932643 273 LEHVFAEGLY-----FTLADIVLLPCIHHFlviisRKFSEKLVEFPLLASWYQRIQEVPGVKTA 331
Cdd:COG0625  138 LEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLAAWLARLAARPAFQRA 196
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 440-503 3.53e-04

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.21  E-value: 3.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767932643 440 KPGDRIVDFCSGGGHVGIVLAHMLPScQVTLIENKELSLIRAKKRSDELGLSNIWFIQANMEYF 503
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL 87
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 431-526 3.73e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.77  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932643 431 LVYVVTNQAKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELglsNIWFIQANMEYF---TGMF 507
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLpleDGSF 88

                         90
                 ....*....|....*....
gi 767932643 508 NIGVALHacgvatdmVIEH 526
Cdd:COG2227   89 DLVICSE--------VLEH 99
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 439-472 9.46e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 41.28  E-value: 9.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 767932643 439 AKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE 472
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVE 68
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 270-329 1.50e-03

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 38.31  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932643  270 LPPLEHVFA--EGLYF-----TLADIVLLPCIHHFLviiSRKFSEKLVEFPLLASWYQRIQEVPGVK 329
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLL---YPKAPDALDKYPKLKALHERVAARPNIK 98
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 443-501 1.95e-03

rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited division proteins these are probably involved in the regulation of cell devision. GidB has been shown to be a methyltransferase G specific to the rRNA small subunit. Previously identified as a glucose-inhibited division protein B that appears to be present and in a single copy in all complete eubacterial genomes so far sequenced. GidB specifically methylates the N7 position of a guanosine in 16S rRNA.


Pssm-ID: 396880  Cd Length: 184  Bit Score: 39.57  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767932643  443 DRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 501
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHARAE 108
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 445-501 2.50e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.54  E-value: 2.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767932643  445 IVDFCSGGGHVGIVLAHMLpSCQVTLIENKELSLIRAKKRSDELGLsNIWFIQANME 501
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAE 55
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 442-501 3.18e-03

16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB (glucose-inhibited division protein B). It is present and a single copy in nearly all complete eubacterial genomes. It is missing only from some obligate intracellular species of various lineages (Chlamydiae, Ehrlichia, Wolbachia, Anaplasma, Buchnera, etc.). RsmG shows a methytransferase fold in its the crystal structure, and acts as a 7-methylguanosine (m(7)G) methyltransferase, apparently specific to 16S rRNA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272928  Cd Length: 181  Bit Score: 39.16  E-value: 3.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767932643  442 GDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE--NKELSLIRAKKRsdELGLSNIWFIQANME 501
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAE 102
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 273-329 3.76e-03

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 37.93  E-value: 3.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767932643 273 LEHVFAEGLYF------TLADIVLLPCIHHFLVIisRKFS-EKLV---EFPLLASWYQRIQEVPGVK 329
Cdd:cd03185   47 LEEELKGGKPFfggdtiGYLDIALGSFLGWFKAI--EEVGgVKLLdeeKFPLLAAWAERFLEREAVK 111
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 280-329 4.83e-03

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 37.25  E-value: 4.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767932643 280 GLYFTLADIVLLPCI--HHFLVIIsrkfsekLVEFPLLASWYQRIQEVPGVK 329
Cdd:cd10291   64 GDEYSIADIAIWPWVarHEWQGID-------LADFPNLKRWFERLAARPAVQ 108
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 274-327 5.33e-03

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; 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 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 36.87  E-value: 5.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767932643 274 EHVFAEGLYFTLADIVLLPCIHHFLVI-ISRkfseklVEFPLLASWYQRIQEVPG 327
Cdd:cd03180   61 RQAYLAGDRFTLADIALGCSVYRWLELpIER------PALPHLERWYARLSQRPA 109
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 441-499 5.64e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 39.26  E-value: 5.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767932643  441 PGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLS-NIWFIQAN 499
Cdd:TIGR00536 114 PILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSN 173
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 270-322 7.53e-03

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical 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). 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 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. 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, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 36.32  E-value: 7.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767932643 270 LPPLEHVFAEGLY-----FTLADIVLLPCIHHFLviISRKFSEKLVEFPLLASWYQRI 322
Cdd:cd00299   45 LAALEQLLAGRPYlagdqFSLADVALAPVLARLE--ALGPYYDLLDEYPRLKAWYDRL 100
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 438-500 8.07e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.60  E-value: 8.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767932643 438 QAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANM 500
Cdd:PRK09328 105 LLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW 167
 
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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