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Conserved domains on  [gi|1994267228|ref|WP_205229406|]
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class I SAM-dependent methyltransferase [Desulfobulbus rhabdoformis]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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; ...
 28-203 1.16e-34

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 PRK00216:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 239  Bit Score: 125.27  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETAR-KFADKESLASIEWHFGDVAFIPV 106
Cdd:PRK00216   38 VWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGReKLRDLGLSGNVEFVQGDAEALPF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 107 ETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLA---LS--VWRSIDRC---------PFFATLaeIIGN-----Y 167
Cdd:PRK00216  118 PDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVileFSkpTNPPLKKAydfylfkvlPLIGKL--ISKNaeaysY 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1994267228 168 IgAESTRAFYsscslsDREELRKLLSNAGFNNIEIR 203
Cdd:PRK00216  196 L-AESIRAFP------DQEELAAMLEEAGFERVRYR 224
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 28-203 1.16e-34

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 125.27  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETAR-KFADKESLASIEWHFGDVAFIPV 106
Cdd:PRK00216   38 VWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGReKLRDLGLSGNVEFVQGDAEALPF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 107 ETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLA---LS--VWRSIDRC---------PFFATLaeIIGN-----Y 167
Cdd:PRK00216  118 PDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVileFSkpTNPPLKKAydfylfkvlPLIGKL--ISKNaeaysY 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1994267228 168 IgAESTRAFYsscslsDREELRKLLSNAGFNNIEIR 203
Cdd:PRK00216  196 L-AESIRAFP------DQEELAAMLEEAGFERVRYR 224
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 31-162 3.52e-34

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: 120.87  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTGVVARRAAQlvgASGSVMGFDADRNMLETARKFADKESLaSIEWHFGDVAFIPVETER 110
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1994267228 111 CDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVWRSIDRCPFFATLAE 162
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 28-203 1.43e-29

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 111.59  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKEslASIEWHFGDVAFIPVE 107
Cdd:TIGR01934  26 LWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVAKKKSELP--LNIEFIQADAEALPFE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 108 TERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLAL--------SVWRSIDRCPFFATL---AEIIGNYIGA-----E 171
Cdd:TIGR01934 104 DNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVIlefskpanALLKKFYKFYLKNVLpsiGGLISKNAEAytylpE 183

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1994267228 172 STRAFysscslSDREELRKLLSNAGFNNIEIR 203
Cdd:TIGR01934 184 SIRAF------PSQEELAAMLKEAGFEEVRYR 209
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-141 2.87e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.09  E-value: 2.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  45 ILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLaSIEWHFGDVAFIPVETERCDVVICQQGLQFF- 123
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGA--RVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLp 77

                          90
                  ....*....|....*....
gi 1994267228 124 -PEKQKALEEMSRVLVPGG 141
Cdd:pfam13649  78 dPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-149 3.42e-16

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 72.46  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  44 RILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLASIEWHFGDV-AFIPVETERCDVVICQQGLQF 122
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELARKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*...
gi 1994267228 123 FPEKQKA-LEEMSRVLVPGGRLALSVWR 149
Cdd:cd02440    79 LVEDLARfLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 28-203 1.16e-34

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 125.27  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETAR-KFADKESLASIEWHFGDVAFIPV 106
Cdd:PRK00216   38 VWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGReKLRDLGLSGNVEFVQGDAEALPF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 107 ETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLA---LS--VWRSIDRC---------PFFATLaeIIGN-----Y 167
Cdd:PRK00216  118 PDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVileFSkpTNPPLKKAydfylfkvlPLIGKL--ISKNaeaysY 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1994267228 168 IgAESTRAFYsscslsDREELRKLLSNAGFNNIEIR 203
Cdd:PRK00216  196 L-AESIRAFP------DQEELAAMLEEAGFERVRYR 224
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 31-162 3.52e-34

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: 120.87  E-value: 3.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTGVVARRAAQlvgASGSVMGFDADRNMLETARKFADKESLaSIEWHFGDVAFIPVETER 110
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1994267228 111 CDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVWRSIDRCPFFATLAE 162
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 28-203 1.43e-29

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 111.59  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKEslASIEWHFGDVAFIPVE 107
Cdd:TIGR01934  26 LWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVAKKKSELP--LNIEFIQADAEALPFE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 108 TERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLAL--------SVWRSIDRCPFFATL---AEIIGNYIGA-----E 171
Cdd:TIGR01934 104 DNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVIlefskpanALLKKFYKFYLKNVLpsiGGLISKNAEAytylpE 183

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1994267228 172 STRAFysscslSDREELRKLLSNAGFNNIEIR 203
Cdd:TIGR01934 184 SIRAF------PSQEELAAMLKEAGFEEVRYR 209
PRK08317 PRK08317
hypothetical protein; Provisional
 35-202 1.10e-27

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 106.94  E-value: 1.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  35 ERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKfADKESLASIEWHFGDVAFIPVETERCDVV 114
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE-RAAGLGPNVEFVRGDADGLPFPDGSFDAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 115 ICQQGLQFFPEKQKALEEMSRVLVPGGRLALS-------VWRSIDRcpffATLAEIIgnyigaestRAFYSSC--SLSDR 185
Cdd:PRK08317   92 RSDRVLQHLEDPARALAEIARVLRPGGRVVVLdtdwdtlVWHSGDR----ALMRKIL---------NFWSDHFadPWLGR 158

                         170
                  ....*....|....*..
gi 1994267228 186 eELRKLLSNAGFNNIEI 202
Cdd:PRK08317  159 -RLPGLFREAGLTDIEV 174
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-141 2.87e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.09  E-value: 2.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  45 ILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLaSIEWHFGDVAFIPVETERCDVVICQQGLQFF- 123
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGA--RVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLp 77

                          90
                  ....*....|....*....
gi 1994267228 124 -PEKQKALEEMSRVLVPGG 141
Cdd:pfam13649  78 dPDLEAALREIARVLKPGG 96
arsM PRK11873
arsenite methyltransferase;
37-220 3.58e-25

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 100.79  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  37 AGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASIEWHFGDVAFIPVETERCDVVIC 116
Cdd:PRK11873   73 AELKPGETVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVIIS 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 117 QQGLQFFPEKQKALEEMSRVLVPGGRLALS--VWRsidrcpffATLAEIIGNyigaesTRAFYSSC--SLSDREELRKLL 192
Cdd:PRK11873  153 NCVINLSPDKERVFKEAFRVLKPGGRFAISdvVLR--------GELPEEIRN------DAELYAGCvaGALQEEEYLAML 218

                         170       180
                  ....*....|....*....|....*...
gi 1994267228 193 SNAGFNNIEIRLEvQMARFPSLDEFLPG 220
Cdd:PRK11873  219 AEAGFVDITIQPK-REYRIPDAREFLED 245
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-201 2.22e-24

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 97.90  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  29 WTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASIEWHFGDVAFIPVET 108
Cdd:pfam01209  30 WKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFED 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 109 ERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRL---------------ALSVWrSIDRCPFFATL-AEIIGNY-IGAE 171
Cdd:pfam01209 110 DSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVvclefskpenpllsqAYELY-FKYVMPFMGKMfAKSYKSYqYLQE 188

                         170       180       190
                  ....*....|....*....|....*....|
gi 1994267228 172 STRAFysscslSDREELRKLLSNAGFNNIE 201
Cdd:pfam01209 189 SIRDF------PDQKTLASMFEKAGFKSVG 212
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-147 1.08e-22

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: 90.46  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  28 AWTDTLIE--RAGIRPGDRILDVACGTGVVARRAAQLvGASgsVMGFDADRNMLETARKFADKeslASIEWHFGDVAFIP 105
Cdd:COG2227     9 FWDRRLAAllARLLPAGGRVLDVGCGTGRLALALARR-GAD--VTGVDISPEALEIARERAAE---LNVDFVQGDLEDLP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1994267228 106 VETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSV 147
Cdd:COG2227    83 LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 39-146 9.82e-21

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 85.93  E-value: 9.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  39 IRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASIEWHFGDVAFIP--VETERCDVVIC 116
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1994267228 117 QQGLQFFPEKQKALEEMSRVLVPGGRLALS 146
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIIS 110
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-147 2.27e-20

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 83.33  E-value: 2.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  41 PGDRILDVACGTGVVARR-AAQLVGASgsVMGFDADRNMLETARkfadkESLASIEWHFGDVAFIPVEtERCDVVICQQG 119
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALlAERFPGAR--VTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLDPP-EPFDLVVSNAA 72

                          90       100
                  ....*....|....*....|....*...
gi 1994267228 120 LQFFPEKQKALEEMSRVLVPGGRLALSV 147
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-198 3.80e-20

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 85.44  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  19 QYIVPAWMgawTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGasgSVMGFDADRNMLETARkfadkESLASIEWHF 98
Cdd:COG4976    27 GYEAPALL---AEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEEMLAKAR-----EKGVYDRLLV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  99 GDVAFIPVETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVWRsidrcpffatlaeiignyiGAESTRAFYS 178
Cdd:COG4976    96 ADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVED-------------------ADGSGRYAHS 156

                         170       180
                  ....*....|....*....|
gi 1994267228 179 scslsdREELRKLLSNAGFN 198
Cdd:COG4976   157 ------LDYVRDLLAAAGFE 170
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 46-145 8.34e-20

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 81.94  E-value: 8.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  46 LDVACGTGVVARRAAQLVGasgSVMGFDADRNMLETARKFADKESLASIEwhfGDVAFIPVETERCDVVICQQGLQFFPE 125
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREGLTFVV---GDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1994267228 126 KQKALEEMSRVLVPGGRLAL 145
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 31-147 1.15e-19

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 83.44  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLA-SIEWHFGDVAFIPvETE 109
Cdd:COG2230    41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGV--RVTGVTLSPEQLEYARERAAEAGLAdRVEVRLADYRDLP-ADG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1994267228 110 RCDVVICQQGLQFFPEKQKA--LEEMSRVLVPGGRLALSV 147
Cdd:COG2230   118 QFDAIVSIGMFEHVGPENYPayFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 17-154 1.79e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.12  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  17 YEQYIVPAWMGAWTDTlierAGIRPGDRILDVACGTGVVARRAAQLVGasGSVMGFDADRNMLETARKFADKESLASIEW 96
Cdd:COG0500     6 YSDELLPGLAALLALL----ERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGLGNVEF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1994267228  97 HFGDVA-FIPVETERCDVVICQQGLQFFPEK--QKALEEMSRVLVPGGRLALSVWRSIDRC 154
Cdd:COG0500    80 LVADLAeLDPLPAESFDLVVAFGVLHHLPPEerEALLRELARALKPGGVLLLSASDAAAAL 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 44-149 3.42e-16

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 72.46  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  44 RILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLASIEWHFGDV-AFIPVETERCDVVICQQGLQF 122
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGA--RVTGVDISPVALELARKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*...
gi 1994267228 123 FPEKQKA-LEEMSRVLVPGGRLALSVWR 149
Cdd:cd02440    79 LVEDLARfLEEARRLLKPGGVLVLTLVL 106
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 33-153 2.33e-15

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 71.90  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTGVVArRAAQLVGAsgSVMGFDADRNMLETARKFADKESLASIEWHFGDVAFIPVETERCD 112
Cdd:COG1041    18 LVNLAGAKEGDTVLDPFCGTGTIL-IEAGLLGR--RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLADESVD 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1994267228 113 VVICQ----QGLQFFPEKQ-----KALEEMSRVLVPGGRLALSVWRSIDR 153
Cdd:COG1041    95 AIVTDppygRSSKISGEELlelyeKALEEAARVLKPGGRVVIVTPRDIDE 144
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 29-199 2.55e-14

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 71.08  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  29 WTDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETA---RKFADKESLASIEWHFGDVAFIP 105
Cdd:PLN02233   61 WKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasrQELKAKSCYKNIEWIEGDATDLP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 106 VETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVWRSIDRcPFFATLAE-IIGNYI---------GAESTRA 175
Cdd:PLN02233  141 FDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQ-PFTTSMQEwMIDNVVvpvatgyglAKEYEYL 219

                         170       180
                  ....*....|....*....|....
gi 1994267228 176 FYSSCSLSDREELRKLLSNAGFNN 199
Cdd:PLN02233  220 KSSINEYLTGEELEKLALEAGFSS 243
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
18-115 3.67e-13

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 66.47  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  18 EQYIVPAWMGAWTDTLIERAGIRPGDRILDVACGTGVVArRAAQLVGASgSVMGFDADRNMLETARKFADKESlASIEWH 97
Cdd:COG2263    22 EQYPTPAELAAELLHLAYLRGDIEGKTVLDLGCGTGMLA-IGAALLGAK-KVVGVDIDPEALEIARENAERLG-VRVDFI 98

                          90
                  ....*....|....*...
gi 1994267228  98 FGDVAFIPVEtERCDVVI 115
Cdd:COG2263    99 RADVTRIPLG-GSVDTVV 115
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 33-218 8.91e-11

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 60.38  E-value: 8.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTGVVARRAAQLvGASGSVMGFDADRNMLETARKfadKESlASIEWHFGDVAFIPVETERCD 112
Cdd:TIGR02072  26 LLKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKT---KLS-ENVQFICGDAEKLPLEDSSFD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 113 VVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVwrsidrcpfFA--TLAEIignyigAESTRAfYSSCSLSdREELRK 190
Cdd:TIGR02072 101 LIVSNLALQWCDDLSQALSELARVLKPGGLLAFST---------FGpgTLHEL------RQSFGQ-HGLRYLS-LDELKA 163

                         170       180
                  ....*....|....*....|....*...
gi 1994267228 191 LLSNAgFNNIEIRLEVQMARFPSLDEFL 218
Cdd:TIGR02072 164 LLKNS-FELLTLEEELITLSFDDPLDVL 190
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 30-167 1.91e-10

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 58.66  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  30 TDTLIERAGIRPGDRILDVACGTGVVARRAAQLvGASGSVMGFDADRNMLETARKFADKESLASIEWHFGDvAFIPVETE 109
Cdd:COG2813    38 TRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGLENVEVLWSD-GLSGVPDG 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1994267228 110 RCDVVIC----QQGLQFFPEkqkALEEM----SRVLVPGGRLALSVWRSIdrcPFFATLAEIIGNY 167
Cdd:COG2813   116 SFDLILSnppfHAGRAVDKE---VAHALiadaARHLRPGGELWLVANRHL---PYERKLEELFGNV 175
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 46-143 3.67e-10

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.84  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  46 LDVACGTGVVARRAAQLVGASGSVmGFDADRNMLETAR-KFADKESLASIEWHFGDVAFIPVETERCDVVICQQGLQFFP 124
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYT-GLDISPAALEAAReRLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 1994267228 125 EKQKALEEMSRVLVPGGRL 143
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-201 2.49e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.13  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAG--IRPGDRILDVACGTGVVArRAAQLVGAsgSVMGFDADRNMLETARKFADKESLASIEWhfgdvafiPVETER 110
Cdd:pfam13489  12 LLLRLLpkLPSPGRVLDFGCGTGIFL-RLLRAQGF--SVTGVDPSPIAIERALLNVRFDQFDEQEA--------AVPAGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 111 CDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSVWRSIDRcpfFATLAEIIGnYIGAESTRafyssCSLSDREELRK 190
Cdd:pfam13489  81 FDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDE---ADRLLLEWP-YLRPRNGH-----ISLFSARSLKR 151

                         170
                  ....*....|.
gi 1994267228 191 LLSNAGFNNIE 201
Cdd:pfam13489 152 LLEEAGFEVVS 162
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 36-144 3.64e-09

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 55.94  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  36 RAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASiEWHF--GDVAFiPVETERCDV 113
Cdd:COG2519    86 RLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPD-NVELklGDIRE-GIDEGDVDA 163

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1994267228 114 VIcqqgLqFFPEKQKALEEMSRVLVPGGRLA 144
Cdd:COG2519   164 VF----L-DMPDPWEALEAVAKALKPGGVLV 189
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 33-145 3.72e-09

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 55.05  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTGVVARRAAQLV----------GASGSVMGFDADRNMLETARKFADKESLA-SIEWHFGDV 101
Cdd:pfam01170  20 MVNLAGWKPGDPLLDPMCGSGTILIEAALMGaniapgkfdaRVRAPLYGSDIDRRMVQGARLNAENAGVGdLIEFVQADA 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1994267228 102 AFIPVETERCDVVIC-----------QQGLQFFPEkqkALEEMSRVLVPGGRLAL 145
Cdd:pfam01170 100 ADLPLLEGSVDVIVTnppygirlgskGALEALYPE---FLREAKRVLRGGGWLVL 151
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 30-177 7.47e-08

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 51.05  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  30 TDTLIERAGIRPGDRILDVACGTGVVARRAAQLVGaSGSVMGFDADRNMLETARKFADKESLASIEWHFGDVaFIPVETE 109
Cdd:pfam05175  20 SRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESP-DAELTMVDINARALESARENLAANGLENGEVVASDV-YSGVEDG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1994267228 110 RCDVVIC----QQGLQFFPE-KQKALEEMSRVLVPGGRLALsVWRSidRCPFFATLAEIIGNYIGAESTRAFY 177
Cdd:pfam05175  98 KFDLIISnppfHAGLATTYNvAQRFIADAKRHLRPGGELWI-VANR--FLGYPPLLEELFGNVEVVAKTNGFK 167
PRK14967 PRK14967
putative methyltransferase; Provisional
 35-116 3.23e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 50.05  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  35 ERAGIRPGDRILDVACGTGVVARRAAQLvGAsGSVMGFDADRNMLETARkfadKESLAS---IEWHFGDVAFIpVETERC 111
Cdd:PRK14967   30 AAEGLGPGRRVLDLCTGSGALAVAAAAA-GA-GSVTAVDISRRAVRSAR----LNALLAgvdVDVRRGDWARA-VEFRPF 102


                  ....*
gi 1994267228 112 DVVIC 116
Cdd:PRK14967  103 DVVVS 107
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 34-88 4.05e-07

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.41  E-value: 4.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1994267228  34 IERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADK 88
Cdd:PRK00377   33 LSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEK 87
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 11-174 4.83e-07

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 49.76  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  11 GTAPETYEQYIVPAWMGAwtDTLIERAGIRPGDRILDVACGTGVVAR--RAAqlvgasGS-VMGFDADRNMLETARkfad 87
Cdd:PRK10258   14 GRAAAHYEQHAELQRQSA--DALLAMLPQRKFTHVLDAGCGPGWMSRywRER------GSqVTALDLSPPMLAQAR---- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  88 kESLASIEWHFGDVAFIPVETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLALSV------------WRSIDRCP 155
Cdd:PRK10258   82 -QKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTlvqgslpelhqaWQAVDERP 160

                         170       180
                  ....*....|....*....|..
gi 1994267228 156 F---FATLAEIIGNYIGAESTR 174
Cdd:PRK10258  161 HanrFLPPDAIEQALNGWRYQH 182
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
17-100 5.68e-07

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 48.90  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  17 YEQYIVPAWMGAwtdTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASIEW 96
Cdd:pfam01135  52 YGQTISAPHMHA---MMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIV 128


                  ....
gi 1994267228  97 HFGD 100
Cdd:pfam01135 129 VVGD 132
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 31-92 1.01e-06

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 48.86  E-value: 1.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLA 92
Cdd:pfam02353  51 DLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDV--NVVGLTLSKNQYKLARKRVAAEGLA 110
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 33-143 2.10e-06

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 47.39  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTG----VVARRAAQLVgasgSVmgfDADRNMLETARKFADKESLASIEWHFGDVAFIPVET 108
Cdd:COG2518    58 MLEALDLKPGDRVLEIGTGSGyqaaVLARLAGRVY----SV---ERDPELAERARERLAALGYDNVTVRVGDGALGWPEH 130

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1994267228 109 ERCDVVICQQGLQFFPEkqkALEEMsrvLVPGGRL 143
Cdd:COG2518   131 APFDRIIVTAAAPEVPE---ALLEQ---LAPGGRL 159
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 26-164 9.71e-06

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: 45.52  E-value: 9.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  26 MGAWTDtlieragIRPGDRILDVACGTGVVARRAAQLVGASgSVMGFDADRNMLETARK------FADKeslasIEWHFG 99
Cdd:COG4123    29 LAAFAP-------VKKGGRVLDLGTGTGVIALMLAQRSPGA-RITGVEIQPEAAELARRnvalngLEDR-----ITVIHG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 100 DVAFIP--VETERCDVVIC-------QQGLQfFPEKQKA---------LEE----MSRVLVPGGRLALsVWRSiDRcpff 157
Cdd:COG4123    96 DLKEFAaeLPPGSFDLVVSnppyfkaGSGRK-SPDEARAiarhedaltLEDliraAARLLKPGGRFAL-IHPA-ER---- 168


                  ....*..
gi 1994267228 158 atLAEII 164
Cdd:COG4123   169 --LAEIL 173
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 17-158 1.01e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 46.04  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  17 YEQYIVPawmGAWTDTLIERAgIRPGD------RILDVACGTGVVARRAAQLVGAsGSVMGFDADRNMLETARKfadKES 90
Cdd:PLN02490   87 YDHIINP---GHWTEDMRDDA-LEPADlsdrnlKVVDVGGGTGFTTLGIVKHVDA-KNVTILDQSPHQLAKAKQ---KEP 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1994267228  91 LASIEWHFGDVAFIPVETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRLAL------SVWRSidrcPFFA 158
Cdd:PLN02490  159 LKECKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDPQRGIKEAYRVLKIGGKACLigpvhpTFWLS----RFFA 228
PRK14968 PRK14968
putative methyltransferase; Provisional
 14-205 1.14e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  14 PETYEqyivPAwmgawTDT--LIERAGIRPGDRILDVACGTGVVarrAAQLVGASGSVMGFDADRNMLETARKFA--DKE 89
Cdd:PRK14968    3 DEVYE----PA-----EDSflLAENAVDKKGDRVLEVGTGSGIV---AIVAAKNGKKVVGVDINPYAVECAKCNAklNNI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  90 SLASIEWHFGDVaFIPVETERCDVVIcqqglqFFP------EKQKALEEMSRVLVPG--GRlalsvwRSIDRcpFFATLa 161
Cdd:PRK14968   71 RNNGVEVIRSDL-FEPFRGDKFDVIL------FNPpylpteEEEEWDDWLNYALSGGkdGR------EVIDR--FLDEV- 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1994267228 162 eiiGNYIgAESTRAF--YSscSLSDREELRKLLSNAGFnNIEIRLE 205
Cdd:PRK14968  135 ---GRYL-KPGGRILllQS--SLTGEDEVLEYLEKLGF-EAEVVAE 173
PLN02244 PLN02244
tocopherol O-methyltransferase
 43-148 1.22e-05

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 45.89  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  43 DRILDVACGTGVVARRAAQLVGASgsVMG-----FDADR-NMLETARKFADKESLasiewHFGDVAFIPVETERCDVVIC 116
Cdd:PLN02244  120 KRIVDVGCGIGGSSRYLARKYGAN--VKGitlspVQAARaNALAAAQGLSDKVSF-----QVADALNQPFEDGQFDLVWS 192

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1994267228 117 QQGLQFFPEKQKALEEMSRVLVPGGRLALSVW 148
Cdd:PLN02244  193 MESGEHMPDKRKFVQELARVAAPGGRIIIVTW 224
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
29-143 3.49e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.51  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  29 WTDTL--IERAGIRPGDRILDVACGTGVVARRAAQLvGASgSVMGFDADRNMLETA------RKFADKeslaSIEWHFGD 100
Cdd:COG2521   118 LEDARrkVKLVGVRRGDRVLDTCTGLGYTAIEALKR-GAR-EVITVEKDPNVLELAelnpwsRELANE----RIKIILGD 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1994267228 101 VA-FIP-VETERCDVVI----------CQQGLQFFpekqkalEEMSRVLVPGGRL 143
Cdd:COG2521   192 ASeVIKtFPDESFDAIIhdpprfslagELYSLEFY-------RELYRVLKPGGRL 239
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
19-143 3.60e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.87  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  19 QYIVPAW----------MGAWtDTLIERAgIRPGDRILDVACGTGVVARRAAQLvGAsGSVMGFDADRNMLETARKFADK 88
Cdd:COG4076     5 QFFVPRWhhpmlndverNDAF-KAAIERV-VKPGDVVLDIGTGSGLLSMLAARA-GA-KKVYAVEVNPDIAAVARRIIAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1994267228  89 ESLAS-IEWHFGDVAFIPVEtERCDVVICQQ-GLQFFPEKQ-KALEE-MSRVLVPGGRL 143
Cdd:COG4076    81 NGLSDrITVINADATDLDLP-EKADVIISEMlDTALLDEGQvPILNHaRKRLLKPGGRI 138
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 30-116 2.19e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 41.69  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  30 TDTLIERA----GIRPGDRILDVACGTGVVA------RRAAQlvgasgsVMGFDADRNMLETARKFADKESLASIEWHFG 99
Cdd:PRK09328   93 TEELVEWAlealLLKEPLRVLDLGTGSGAIAlalakeRPDAE-------VTAVDISPEALAVARRNAKHGLGARVEFLQG 165

                          90
                  ....*....|....*..
gi 1994267228 100 DVaFIPVETERCDVVIC 116
Cdd:PRK09328  166 DW-FEPLPGGRFDLIVS 181
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 70-145 2.68e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 40.44  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  70 MGFDADRNMLETArkfADKESLAS------IEWHFGDVAFIPVETERCDVVICQQGLQFFPEKQKALEEMSRVLVPGGRL 143
Cdd:PLN02232    1 MGLDFSSEQLAVA---ATRQSLKArscykcIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRV 77


                  ..
gi 1994267228 144 AL 145
Cdd:PLN02232   78 SI 79
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
33-146 3.05e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 41.31  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAgIRPGDRILDVACGTGVVArRAAQLVGAsGSVMGFDADRNMLETARKFADKESLAS-IEWHFGDVafipVETERC 111
Cdd:COG2264   141 ALEKL-LKPGKTVLDVGCGSGILA-IAAAKLGA-KRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDL----LEDGPY 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1994267228 112 DVVIcqqglqffpekqkA----------LEEMSRVLVPGGRLALS 146
Cdd:COG2264   214 DLVV-------------AnilanplielAPDLAALLKPGGYLILS 245
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 31-115 5.66e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 40.93  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTG----VVARRAAQlvgasgsVMGFDADRNMLETARKFADKESLASIEWHFGDVA-FIP 105
Cdd:COG2265   223 AAALEWLDLTGGERVLDLYCGVGtfalPLARRAKK-------VIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEeVLP 295

                          90
                  ....*....|..
gi 1994267228 106 --VETERCDVVI 115
Cdd:COG2265   296 elLWGGRPDVVV 307
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
33-147 6.61e-04

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 40.70  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLaSIEWHFGDvAFIPVETERCD 112
Cdd:COG0827   107 LVEKFTKKEGLRILDPAVGTGNLLTTVLNQLKKKVNAYGVEVDDLLIRLAAVLANLQGH-PVELFHQD-ALQPLLIDPVD 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1994267228 113 VVIC----------QQGLQFfpeKQKALEEMS-----------RVLVPGGRLALSV 147
Cdd:COG0827   185 VVISdlpvgyypndERAKRF---KLKADEGHSyahhlfieqslNYLKPGGYLFFLV 237
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 33-206 8.68e-04

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 40.21  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASIEWHFGDVAFIPVETERCD 112
Cdd:PRK13943   72 FMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDGYYGVPEFAPYD 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 113 VVICQQGLQFFPEKQ-KALEEMSRVLVPggrLALSVwrsIDRCPFFatLAEIIGNYIGAE---STRAFYSSCSLSD-REE 187
Cdd:PRK13943  152 VIFVTVGVDEVPETWfTQLKEGGRVIVP---INLKL---SRRQPAF--LFKKKDPYLVGNyklETRFIKAGGNLGNlLER 223

                         170       180
                  ....*....|....*....|.
gi 1994267228 188 LRKLLSNAGFN--NIEIRLEV 206
Cdd:PRK13943  224 NRKLLREFPFNreILVVRSHI 244
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 44-144 1.13e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 39.54  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  44 RILDVACGTG-----VVAR-RAAQlvgasgsVMGFDADRNMLETARkfadkESLASIEWHFGDVA-FIPveTERCDVVIC 116
Cdd:PRK01683   34 YVVDLGCGPGnstelLVERwPAAR-------ITGIDSSPAMLAEAR-----SRLPDCQFVEADIAsWQP--PQALDLIFA 99

                          90       100
                  ....*....|....*....|....*...
gi 1994267228 117 QQGLQFFPEKQKALEEMSRVLVPGGRLA 144
Cdd:PRK01683  100 NASLQWLPDHLELFPRLVSLLAPGGVLA 127
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 33-145 1.52e-03

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 39.22  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRIldVACGTGVVARRAAQLV---GASGSVMGFDADRNMLETARKFADKESLASIEwhfgDVAFIPVE-- 107
Cdd:cd08258   156 VAERSGIRPGDTV--VVFGPGPIGLLAAQVAklqGATVVVVGTEKDEVRLDVAKELGADAVNGGEE----DLAELVNEit 229

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1994267228 108 -TERCDVVICQQGlqffpeKQKALEEMSRVLVPGGRLAL 145
Cdd:cd08258   230 dGDGADVVIECSG------AVPALEQALELLRKGGRIVQ 262
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 34-116 1.96e-03

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.79  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  34 IERAGIRPGDRILDVacGTGVVARRAAQLVGASG--SVMGFDADRNMLETARKF--ADKESLASIEWHFGDvafipvete 109
Cdd:cd08255    90 VRDAEPRLGERVAVV--GLGLVGLLAAQLAKAAGarEVVGVDPDAARRELAEALgpADPVAADTADEIGGR--------- 158


                  ....*..
gi 1994267228 110 RCDVVIC 116
Cdd:cd08255   159 GADVVIE 165
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 24-197 2.22e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  24 AWMGAWTDTlieragirPGDRILDVACGTGVVARRAAQLvGAsgSVMGFDADRNMLETARKFADKESLA-SIEWHFGDVA 102
Cdd:PRK07580   54 SWLPADGDL--------TGLRILDAGCGVGSLSIPLARR-GA--KVVASDISPQMVEEARERAPEAGLAgNITFEVGDLE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 103 fiPVeTERCDVVICQQGLQFFPekQKALEEMSRVLVP--GGRLALSVwrsIDRCPFFATLAEIIGNYIGAE-STRAFyss 179
Cdd:PRK07580  123 --SL-LGRFDTVVCLDVLIHYP--QEDAARMLAHLASltRGSLIFTF---APYTPLLALLHWIGGLFPGPSrTTRIY--- 191

                         170
                  ....*....|....*...
gi 1994267228 180 cSLSDrEELRKLLSNAGF 197
Cdd:PRK07580  192 -PHRE-KGIRRALAAAGF 207
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 33-222 2.33e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 38.77  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  33 LIERAGIRPGDRILDVAC-GTGVVARRAAQLVGAsgSVMGFDADRNMLETARKFADKESLASIEwHFGDVAFIPVETERC 111
Cdd:cd08254   157 VVRAGEVKPGETVLVIGLgGLGLNAVQIAKAMGA--AVIAVDIKEEKLELAKELGADEVLNSLD-DSPKDKKAAGLGGGF 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228 112 DVVICQQGLQF-FPEKQKALEEMSRVLVPG-GRLALSVwrsidRCPFFATL-AEIIGNYigaestrafysSCSLSDREEL 188
Cdd:cd08254   234 DVIFDFVGTQPtFEDAQKAVKPGGRIVVVGlGRDKLTV-----DLSDLIAReLRIIGSF-----------GGTPEDLPEV 297

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1994267228 189 RKLLSnagfnniEIRLEVQMARFPsLDEFlPGYI 222
Cdd:cd08254   298 LDLIA-------KGKLDPQVETRP-LDEI-PEVL 322
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 39-136 2.91e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 37.82  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  39 IRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADrNMLETARKfadkeSLASIEW-------HFGDVAFipveterc 111
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAA-GVAECVAK-----GLYVIQGdldegleHFPDKSF-------- 76

                          90       100
                  ....*....|....*....|....*
gi 1994267228 112 DVVICQQGLQFFPEKQKALEEMSRV 136
Cdd:pfam07021  77 DYVILSQTLQATRNPREVLDEMLRI 101
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 31-130 9.78e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 36.86  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1994267228  31 DTLIERAGIRPGDRILDVACGTGVVARRAAQLVGASGSVMGFDADRNMLETARKFADKESLASI---EWHFGDVAfIPVE 107
Cdd:COG5459    70 AELAEAGPDFAPLTVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRRLARAAANPALetaEWRLADLA-AALP 148

                          90       100
                  ....*....|....*....|....
gi 1994267228 108 TERCDVVICQQGL-QFFPEKQKAL 130
Cdd:COG5459   149 APPADLVVASYVLnELADAARAAL 172
 
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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