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Conserved domains on  [gi|2045151094|ref|NP_001381941|]
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glutathione S-transferase C-terminal domain-containing protein [Rattus norvegicus]

Protein Classification

glutathione S-transferase C-terminal domain-containing protein( domain architecture ID 118528)

glutathione S-transferase C-terminal domain-containing protein that also contains a class I SAM-dependent methyltransferase domain

CATH:  2.20.25.110|1.20.1050.10
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12504684|12826405|21455499
SCOP:  3000118|4000976

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; ...
 420-538 1.78e-15

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: 73.37  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 420 RKQQQLNNLAYLV------LDRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLS-NIWF 492
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2045151094 493 IQANMEYFTGV-----FDIGVALHACGVATDMVIQRCIQTRASFITC-PCCY 538
Cdd:pfam13679  81 LEGTIAGSTPVelpdrVDVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
GST_C_3 super family cl48253
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 267-326 5.25e-05

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


The actual alignment was detected with superfamily member pfam14497:

Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 42.54  E-value: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045151094 267 LPPLEHVFA--EGLYF-----TLADIVLLPCVHHFLVMickKFSEKLEQFPLLTSWYQRIQEVPKVK 326
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLLYP---KAPDALDKYPKLKALHERVAARPNIK 98
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 420-538 1.78e-15

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 73.37  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 420 RKQQQLNNLAYLV------LDRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLS-NIWF 492
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2045151094 493 IQANMEYFTGV-----FDIGVALHACGVATDMVIQRCIQTRASFITC-PCCY 538
Cdd:pfam13679  81 LEGTIAGSTPVelpdrVDVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 267-326 5.25e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 42.54  E-value: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045151094 267 LPPLEHVFA--EGLYF-----TLADIVLLPCVHHFLVMickKFSEKLEQFPLLTSWYQRIQEVPKVK 326
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLLYP---KAPDALDKYPKLKALHERVAARPNIK 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 436-512 6.10e-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: 43.44  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 436 AKPGDRIVDFCSGGGHVGIVLAHvlPLCQVTLIENKEISLIRAKKRSDELGLsNIWFIQANME---YFTGVFDIGVALHA 512
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEdlpFPDGSFDLVISSFV 96
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 258-319 6.99e-05

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: 42.10  E-value: 6.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045151094 258 HIRKATASELPPLEHVFAEGLY-----FTLADIVLLPCVHHFLVMicKKFSEKLEQFPLLTSWYQRI 319
Cdd:cd00299    36 AAREELPALLAALEQLLAGRPYlagdqFSLADVALAPVLARLEAL--GPYYDLLDEYPRLKAWYDRL 100
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
239-328 2.25e-04

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 42.96  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 239 AFSKLTVQEDAEATNRepshIRKATASELPPLEHVFAEGLY-----FTLADIVLLPCVHHFlvmicKKFSEKLEQFPLLT 313
Cdd:COG0625   111 LLERLAPEKDPAAIAR----ARAELARLLAVLEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLA 181

                          90
                  ....*....|....*
gi 2045151094 314 SWYQRIQEVPKVKTA 328
Cdd:COG0625   182 AWLARLAARPAFQRA 196
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 439-509 1.16e-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: 40.32  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045151094 439 GDRIVDFCSGGGHVGIVLAHVLPLCQVTLIE--NKEISLIRAKKRsdELGLSNIWFIQANMEYF--TGVFDIGVA 509
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAEDYqhEEQFDIITS 115
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 431-506 1.59e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.92  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 431 LVLDRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLSNIWFIQANMeyFTGV----FDI 506
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW--FEPLpggrFDL 178
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 420-538 1.78e-15

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 73.37  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 420 RKQQQLNNLAYLV------LDRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLS-NIWF 492
Cdd:pfam13679   1 KKLHQVEHLAEFIapllkeLLDENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNkRMSF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2045151094 493 IQANMEYFTGV-----FDIGVALHACGVATDMVIQRCIQTRASFITC-PCCY 538
Cdd:pfam13679  81 LEGTIAGSTPVelpdrVDVVTALHACDTATDDALRFALAKQARAIVLvPCCY 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 437-498 1.46e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 1.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045151094 437 KPGDRIVDFCSGGGHVGIVLAH-VLPLCQVTLIENKEISLIRAKKRSDELGLSNIWFIQANME 498
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE 64
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 267-326 5.25e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 42.54  E-value: 5.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045151094 267 LPPLEHVFA--EGLYF-----TLADIVLLPCVHHFLVMickKFSEKLEQFPLLTSWYQRIQEVPKVK 326
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLLYP---KAPDALDKYPKLKALHERVAARPNIK 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 436-512 6.10e-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: 43.44  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 436 AKPGDRIVDFCSGGGHVGIVLAHvlPLCQVTLIENKEISLIRAKKRSDELGLsNIWFIQANME---YFTGVFDIGVALHA 512
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEdlpFPDGSFDLVISSFV 96
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 258-319 6.99e-05

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: 42.10  E-value: 6.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045151094 258 HIRKATASELPPLEHVFAEGLY-----FTLADIVLLPCVHHFLVMicKKFSEKLEQFPLLTSWYQRI 319
Cdd:cd00299    36 AAREELPALLAALEQLLAGRPYlagdqFSLADVALAPVLARLEAL--GPYYDLLDEYPRLKAWYDRL 100
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 437-509 9.82e-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: 43.99  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 437 KPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIEnkeiSLiraKKR-------SDELGLSNIWFIQANMEYFTGV--FDIG 507
Cdd:COG0357    66 KEGARVLDVGSGAGFPGIPLAIARPDLQVTLVD----SL---GKKiaflrevVRELGLKNVTVVHGRAEELAPRekFDVV 138


                  ..
gi 2045151094 508 VA 509
Cdd:COG0357   139 TA 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 430-511 1.21e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.37  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 430 YLVLDRAKPGDRIVDFCSGGGHVGIVLAHvLPLCQVTLIENKEISLIRAKKRSDELGLSNIWFIQANM--------EYFT 501
Cdd:COG0500    18 LALLERLPKGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLaeldplpaESFD 96

                          90
                  ....*....|
gi 2045151094 502 GVFDIGVaLH 511
Cdd:COG0500    97 LVVAFGV-LH 105
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
239-328 2.25e-04

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 42.96  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 239 AFSKLTVQEDAEATNRepshIRKATASELPPLEHVFAEGLY-----FTLADIVLLPCVHHFlvmicKKFSEKLEQFPLLT 313
Cdd:COG0625   111 LLERLAPEKDPAAIAR----ARAELARLLAVLEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLA 181

                          90
                  ....*....|....*
gi 2045151094 314 SWYQRIQEVPKVKTA 328
Cdd:COG0625   182 AWLARLAARPAFQRA 196
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 428-511 2.40e-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: 41.16  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 428 LAYLVLDRAKPGDRIVDFCSGGGHVGIVLAHVlpLCQVTLIENKEISLIRAKKRSDELglsNIWFIQANMEYF---TGVF 504
Cdd:COG2227    14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLpleDGSF 88


                  ....*..
gi 2045151094 505 DIGVALH 511
Cdd:COG2227    89 DLVICSE 95
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 440-498 3.88e-04

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: 41.88  E-value: 3.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045151094 440 DRIVDFCSGGGHVGIVLAHVLPLCQVTLIE--NKEISLIRakKRSDELGLSNIWFIQANME 498
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLEslLKKINFLE--EVKSELGLDNVTIVHARAE 108
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 442-526 7.29e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 7.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 442 IVDFCSGGGHVGIVLAHVLPlCQVTLIENKEISLIRAKKRSDELGLsNIWFIQANME---YFTGVFDIGVALHACGVATD 518
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEdlpFPDGSFDLVVSSGVLHHLPD 78


                  ....*...
gi 2045151094 519 MVIQRCIQ 526
Cdd:pfam13649  79 PDLEAALR 86
rsmG_gidB TIGR00138
16S rRNA (guanine(527)-N(7))-methyltransferase RsmG; RsmG was previously called GidB ...
 439-509 1.16e-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: 40.32  E-value: 1.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045151094 439 GDRIVDFCSGGGHVGIVLAHVLPLCQVTLIE--NKEISLIRAKKRsdELGLSNIWFIQANMEYF--TGVFDIGVA 509
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAEDYqhEEQFDIITS 115
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 431-506 1.59e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.92  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 431 LVLDRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLSNIWFIQANMeyFTGV----FDI 506
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW--FEPLpggrFDL 178
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 428-469 1.90e-03

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: 40.13  E-value: 1.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2045151094 428 LAYLVldRAKPGDRIVDFCSGGGHVGIVLAHVLPLCQVTLIE 469
Cdd:COG4123    29 LAAFA--PVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVE 68
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 428-506 4.08e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.75  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045151094 428 LAYLVLDRAKPGD--RIVDFCSGGGHVGIVLAHVLPLCQVTLIENKEISLIRAKKRSDELGLSN-IWFIQANMeyFTGV- 503
Cdd:COG2890   100 LVELALALLPAGAppRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDL--FEPLp 177


                  ....*..
gi 2045151094 504 ----FDI 506
Cdd:COG2890   178 gdgrFDL 184
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 260-323 7.55e-03

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: 36.11  E-value: 7.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045151094 260 RKATASELPPLEHVFAEGLYF-----TLADIVLLPCVHHFLVmicKKFSEKLEQFPLLTSWYQRIQEVP 323
Cdd:pfam00043  28 LEKVARVLSALEEVLKGQTYLvgdklTLADIALAPALLWLYE---LDPACLREKFPNLKAWFERVAARP 93
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 277-326 9.11e-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: 36.48  E-value: 9.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2045151094 277 GLYFTLADIVLLPCV--HHFLvmickkfSEKLEQFPLLTSWYQRIQEVPKVK 326
Cdd:cd10291    64 GDEYSIADIAIWPWVarHEWQ-------GIDLADFPNLKRWFERLAARPAVQ 108
 
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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