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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154707916 186 LEHVFAEGLY-----FTLADIVLLPCIHHFlviisRKFSEKLVEFPLLASWYQRIQEVPGVKTA 244
Cdd:COG0625  138 LEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLAAWLARLAARPAFQRA 196

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154707916 353 KPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIEnkelSLiraKKR-------SDELGLSNIWFIQA 411
Cdd:COG0357   66 KEGARVLDVGSGAGFPGIPLAIARPDLQVTLVD----SL---GKKiaflrevVRELGLKNVTVVHG 124

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154707916  183 LPPLEHVFA--EGLYF-----TLADIVLLPCIHHFLviiSRKFSEKLVEFPLLASWYQRIQEVPGVK 242
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLL---YPKAPDALDKYPKLKALHERVAARPNIK 98

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154707916 186 LEHVFAEGLYF------TLADIVLLPCIHHFLVIisRKFS-EKLV---EFPLLASWYQRIQEVPGVK 242
Cdd:cd03185   47 LEEELKGGKPFfggdtiGYLDIALGSFLGWFKAI--EEVGgVKLLdeeKFPLLAAWAERFLEREAVK 111

Methyltransferase domain; This family appears to have methyltransferase activity.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154707916  353 KPGDRIVDFCSGGGHVGIVLAH-MLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 414
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE 64

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154707916 352 AKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELGLsNIWFIQANME 414
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154707916 353 KPGDRIVDFCSGGGHVGIVLAHMLPScQVTLIENKELSLIRAKKRSDELGLSNIWFIQANMEYF 416
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAEL 87

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

                         10        20        30
                 ....*....|....*....|....*....|....
gi 154707916 352 AKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE 385
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRSPGARITGVE 68

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 154707916  356 DRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 414
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHARAE 108

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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154707916  355 GDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE--NKELSLIRAKKRsdELGLSNIWFIQANME 414
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAE 102

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154707916 193 GLYFTLADIVLLPCI--HHFLVIIsrkfsekLVEFPLLASWYQRIQEVPGVK 242
Cdd:cd10291   64 GDEYSIADIAIWPWVarHEWQGID-------LADFPNLKRWFERLAARPAVQ 108

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 154707916 187 EHVFAEGLYFTLADIVLLPCIHHFLVI-ISRkfseklVEFPLLASWYQRIQEVPG 240
Cdd:cd03180   61 RQAYLAGDRFTLADIALGCSVYRWLELpIER------PALPHLERWYARLSQRPA 109

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154707916 351 QAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANM 413
Cdd:PRK09328 105 LLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW 167

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154707916 352 AKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQAN 412
Cdd:COG2813   47 EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSD 107