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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026920 271 LPPLEHVFA--EGLYF-----TLADIVLLPCIHHFLViicKKFSEKLEQFPLLTSWYQRIQEVPKVK 330
Cdd:pfam14497  35 LGYFEKVLNknGGGYLvgdklTYADLALFQVLDGLLY---PKAPDALDKYPKLKALHERVAARPNIK 98

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 1248026920 440 AKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELGLsNIWFIQANME 502
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026920 262 HIRKAKAADLPPLEHVFAEGLY-----FTLADIVLLPCIHHFLVIicKKFSEKLEQFPLLTSWYQRI 323
Cdd:cd00299    36 AAREELPALLAALEQLLAGRPYlagdqFSLADVALAPVLARLEAL--GPYYDLLDEYPRLKAWYDRL 100

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248026920 432 LVYLVLNQA--KPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANM 501
Cdd:PRK09328   96 LVEWALEALllKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDW 167

Methyltransferase domain; This family appears to have methyltransferase activity.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1248026920 441 KPGDRIVDFCSGGGHVGIVLAH-MLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 502
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE 64

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 1248026920 441 KPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIEnkelSLiraKKR-------SDELGLSNIWFIQA 499
Cdd:COG0357    66 KEGARVLDVGSGAGFPGIPLAIARPDLQVTLVD----SL---GKKiaflrevVRELGLKNVTVVHG 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026920 432 LVYLVLNQAKPGDRIVDFCSGGGHVGIVLAHMlpSCQVTLIENKELSLIRAKKRSDELglsNIWFIQANMEYF---TGMF 508
Cdd:COG2227    14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLpleDGSF 88

                          90
                  ....*....|....*....
gi 1248026920 509 NIGVALHacgvatdmVIEH 527
Cdd:COG2227    89 DLVICSE--------VLEH 99

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1248026920 262 HIRKAKAADLPPLEHVFAEGLY-----FTLADIVLLPCIHHFLVIicKKFSEKLEQFPLLTSWYQRI 323
Cdd:cd00299    36 AAREELPALLAALEQLLAGRPYlagdqFSLADVALAPVLARLEAL--GPYYDLLDEYPRLKAWYDRL 100

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026920 243 AFSKLTVQEDAAASNREPSHIRKAkaadLPPLEHVFAEGLY-----FTLADIVLLPCIHHFlviicKKFSEKLEQFPLLT 317
Cdd:COG0625   111 LLERLAPEKDPAAIARARAELARL----LAVLEARLAGGPYlagdrFSIADIALAPVLRRL-----DRLGLDLADYPNLA 181

                          90       100
                  ....*....|....*....|...
gi 1248026920 318 SWYQRIQEVPKVKTAASKCGIYF 340
Cdd:COG0625   182 AWLARLAARPAFQRALAAAEPDL 204

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 1248026920 444 DRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANME 502
Cdd:pfam02527  50 DHVLDVGSGAGFPGIPLAIARPDKKVTLLESLLKKINFLEEVKSELGLDNVTIVHARAE 108

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248026920 264 RKAKAADLPPLEHVFAEGLYF-----TLADIVLLPCIHHFLVIickKFSEKLEQFPLLTSWYQRIQEVP 327
Cdd:pfam00043  28 LEKVARVLSALEEVLKGQTYLvgdklTLADIALAPALLWLYEL---DPACLREKFPNLKAWFERVAARP 93

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 1248026920 443 GDRIVDFCSGGGHVGIVLAHMLPSCQVTLIE--NKELSLIRAKKRsdELGLSNIWFIQANME 502
Cdd:TIGR00138  43 GKRVIDIGSGAGFPGIPLAIARPELKLTLLEsnHKKVAFLREVKA--ELGLNNVEIVNGRAE 102

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]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248026920 442 PGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLS-NIWFIQAN 500
Cdd:TIGR00536 114 PILHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSN 173