NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|896559443|ref|WP_049458268|]
View 

MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Stenotrophomonas]

Protein Classification

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11493423)

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis

CATH:  3.40.50.150
EC:  2.1.1.222|2.1.1.64
Gene Ontology:  GO:0102208|GO:0008425|GO:0032259|GO:0006744
PubMed:  10419476|11583838

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 14-231 2.02e-125

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


:

Pssm-ID: 273910  Cd Length: 224  Bit Score: 354.29  E-value: 2.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   14 ELDKFAALANRWWDADGPQKPLHALNPVRLKYVADRV------PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPEL 87
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   88 VKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFAVA 167
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896559443  168 IVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQLVDVSGMAYEPWRNHARLSSRTDINYL 231
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 14-231 2.02e-125

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 354.29  E-value: 2.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   14 ELDKFAALANRWWDADGPQKPLHALNPVRLKYVADRV------PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPEL 87
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   88 VKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFAVA 167
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896559443  168 IVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQLVDVSGMAYEPWRNHARLSSRTDINYL 231
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 7-236 4.47e-70

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 217.68  E-value: 4.47e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   7 SSNFDQAELDKFAALANRWWDADGPQKPLHALNPVRLKYVADRV------------PLRGARVLDIGCGGGLLSEALAQA 74
Cdd:PLN02396  73 TTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLcrhfskdpssakPFEGLKFIDIGCGGGLLSEPLARM 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  75 GADVTAIDLAPELVKVARLHAL--ESGATVDYRVQAAEDLAAEQPgSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHL 152
Cdd:PLN02396 153 GATVTGVDAVDKNVKIARLHADmdPVTSTIEYLCTTAEKLADEGR-KFDAVLSLEVIEHVANPAEFCKSLSALTIPNGAT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443 153 FLSTINRTAAAFAVAIVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQLVDVSGMAYEPWRNHARLSSRTDINYLA 232
Cdd:PLN02396 232 VLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIA 311


                 ....
gi 896559443 233 YAVK 236
Cdd:PLN02396 312 YGTK 315
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 22-158 5.43e-44

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: 144.39  E-value: 5.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  22 ANRWWDAdgpqkplhalnpvRLKYVADRVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGat 101
Cdd:COG2227    6 ARDFWDR-------------RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELN-- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896559443 102 VDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTIN 158
Cdd:COG2227   71 VDFVQGDLEDLPLE-DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-150 5.21e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 104.95  E-value: 5.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   57 VLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDP 135
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 896559443  136 G--AIIEACKRLLKPGG 150
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-155 1.61e-17

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: 75.16  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  56 RVLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGA-TVDYRVQAAEDLAAEQPGSFDVVTCMEMLEH-V 132
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLAdNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 896559443 133 PDPGAIIEACKRLLKPGGHLFLS 155
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
56-155 4.04e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 43.17  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443    56 RVLDIGCGGG--LLSEALAQAGADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCMEMLEHVP 133
Cdd:smart00828   2 RVLDFGCGYGsdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIK 81

                           90       100
                   ....*....|....*....|..
gi 896559443   134 DPGAIIEACKRLLKPGGHLFLS 155
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHLVLA 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 14-231 2.02e-125

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 354.29  E-value: 2.02e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   14 ELDKFAALANRWWDADGPQKPLHALNPVRLKYVADRV------PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPEL 87
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   88 VKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFAVA 167
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896559443  168 IVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQLVDVSGMAYEPWRNHARLSSRTDINYL 231
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 7-236 4.47e-70

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 217.68  E-value: 4.47e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   7 SSNFDQAELDKFAALANRWWDADGPQKPLHALNPVRLKYVADRV------------PLRGARVLDIGCGGGLLSEALAQA 74
Cdd:PLN02396  73 TTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLcrhfskdpssakPFEGLKFIDIGCGGGLLSEPLARM 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  75 GADVTAIDLAPELVKVARLHAL--ESGATVDYRVQAAEDLAAEQPgSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHL 152
Cdd:PLN02396 153 GATVTGVDAVDKNVKIARLHADmdPVTSTIEYLCTTAEKLADEGR-KFDAVLSLEVIEHVANPAEFCKSLSALTIPNGAT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443 153 FLSTINRTAAAFAVAIVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQLVDVSGMAYEPWRNHARLSSRTDINYLA 232
Cdd:PLN02396 232 VLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIA 311


                 ....
gi 896559443 233 YAVK 236
Cdd:PLN02396 312 YGTK 315
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 22-158 5.43e-44

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: 144.39  E-value: 5.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  22 ANRWWDAdgpqkplhalnpvRLKYVADRVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGat 101
Cdd:COG2227    6 ARDFWDR-------------RLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELN-- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 896559443 102 VDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTIN 158
Cdd:COG2227   71 VDFVQGDLEDLPLE-DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 42-159 4.18e-31

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: 111.62  E-value: 4.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  42 RLKYVADRVPLR-GARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEqPGSF 120
Cdd:COG2226   10 GREALLAALGLRpGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896559443 121 DVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINR 159
Cdd:COG2226   89 DLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-150 5.21e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 104.95  E-value: 5.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   57 VLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDP 135
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 896559443  136 G--AIIEACKRLLKPGG 150
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-154 1.32e-28

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 103.51  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   58 LDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGatVDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDPGA 137
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 896559443  138 IIEACKRLLKPGGHLFL 154
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 7-156 4.21e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 101.93  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   7 SSNFDQAELDKFAALANRWWDAdgPQKPLHALNPVRLKYVADRVPLR-GARVLDIGCGGGLLSEALAQA-GADVTAIDLA 84
Cdd:COG2230    6 GNDFYRLFLDPTMTYSCAYFED--PDDTLEEAQEAKLDLILRKLGLKpGMRVLDIGCGWGGLALYLARRyGVRVTGVTLS 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896559443  85 PELVKVARLHALESGAT--VDYRVQAAEDLAAEqpGSFDVVTCMEMLEHVPDP--GAIIEACKRLLKPGGHLFLST 156
Cdd:COG2230   84 PEQLEYARERAAEAGLAdrVEVRLADYRDLPAD--GQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-206 4.87e-27

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 101.74  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   51 PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALesgatvdyRVQAAEDLAAEQPGSFDVVTCMEMLE 130
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVR--------FDQFDEQEAAVPAGKFDVIVAREVLE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896559443  131 HVPDPGAIIEACKRLLKPGGHLFLSTINRTAAafavAIVGAEYVARLLPKGTHHYqeFIKPAELARWLREADMQLV 206
Cdd:pfam13489  92 HVPDPPALLRQIAALLKPGGLLLLSTPLASDE----ADRLLLEWPYLRPRNGHIS--LFSARSLKRLLEEAGFEVV 161
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
16-178 3.73e-22

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 89.67  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  16 DKFAALANRWWDADGPQKplhalnpVRLKYVADRVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARlha 95
Cdd:COG4976   16 DSYDAALVEDLGYEAPAL-------LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  96 lESGATVDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTinRTAAAFAVAIVGAEYVA 175
Cdd:COG4976   86 -EKGVYDRLLVADLADLAEP-DGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV--EDADGSGRYAHSLDYVR 161


                 ...
gi 896559443 176 RLL 178
Cdd:COG4976  162 DLL 164
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
53-156 6.16e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 86.42  E-value: 6.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQA--GADVTAIDLAPELVKVARlhalESGATVDYRVQAAEDLAAEQPgsFDVVTCMEMLE 130
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR----ARLPNVRFVVADLRDLDPPEP--FDLVVSNAALH 74

                         90       100
                 ....*....|....*....|....*.
gi 896559443 131 HVPDPGAIIEACKRLLKPGGHLFLST 156
Cdd:COG4106   75 WLPDHAALLARLAAALAPGGVLAVQV 100
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 52-145 7.63e-21

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 87.20  E-value: 7.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  52 LRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESG--ATVDYRVQAAEDLAaeqpGSFDVVTCMEML 129
Cdd:PRK07580  62 LTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGlaGNITFEVGDLESLL----GRFDTVVCLDVL 137

                         90
                 ....*....|....*.
gi 896559443 130 EHVPDPGAiIEACKRL 145
Cdd:PRK07580 138 IHYPQEDA-ARMLAHL 152
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 53-201 1.98e-20

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 85.35  E-value: 1.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGAT-VDYRVQAAEDLAAEQPGSFDVVTCMEMLE 130
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDPLPAESFDLVVAFGVLH 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896559443 131 HVP--DPGAIIEACKRLLKPGGHLFLStINRTAAAFAVAIVGAEYVARLLPkGTHHYQEFIKPAELARWLREA 201
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGVLLLS-ASDAAAALSLARLLLLATASLLE-LLLLLRLLALELYLRALLAAA 176
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-152 3.77e-19

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 79.33  E-value: 3.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   58 LDIGCGGGLLSEALAQA--GADVTAIDLAPELVKVARLHALESGATVDYRVQA-AEDLAAEQPGSFDVVTCMEMLEHVPD 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRVELfQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 896559443  135 PGAIIEACKRLLKPGGHL 152
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 54-165 3.59e-18

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 78.23  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   54 GARVLDIGCGGGLLSEALAQ---AGADVTAIDLAPELVKVARLHALESGAT-VDYRVQAAEDLA-AEQPGSFDVVTCMEM 128
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPeLLEDDKFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 896559443  129 LEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFA 165
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPA 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-155 1.61e-17

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: 75.16  E-value: 1.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  56 RVLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGA-TVDYRVQAAEDLAAEQPGSFDVVTCMEMLEH-V 132
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLAdNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 896559443 133 PDPGAIIEACKRLLKPGGHLFLS 155
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 45-186 1.30e-15

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 72.99  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  45 YVADRVPLRGARVLDIGCGGGLLSEALAQAGA-DVTAIDLAPELVKVARLHALESGATVDYRVqaaEDLAAEQP-GSFDV 122
Cdd:COG3897   62 YLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRL---GDWRDPPAaGGFDL 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896559443 123 VTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAA----FAVAIVGAEYVARLLPKGTHHYQ 186
Cdd:COG3897  139 ILGGDVLYERDLAEPLLPFLDRLAAPGGEVLIGDPGRGYLPafreRLEALAGYEVVTRELEDTEKVKR 206
PRK08317 PRK08317
hypothetical protein; Provisional
 53-150 1.48e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 73.05  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQA---GADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQpGSFDVVTCMEML 129
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPD-GSFDAVRSDRVL 97

                         90       100
                 ....*....|....*....|.
gi 896559443 130 EHVPDPGAIIEACKRLLKPGG 150
Cdd:PRK08317  98 QHLEDPARALAEIARVLRPGG 118
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 53-154 3.60e-13

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: 66.71  E-value: 3.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQ--AGADVTAIDLAPELVKVARLHALESGatVDYRVQAAE-DL----AAEQPGSFDVVTC 125
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNG--LEDRITVIHgDLkefaAELPPGSFDLVVS 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 896559443 126 ----MEMLEHV--PDPG-------------AIIEACKRLLKPGGHLFL 154
Cdd:COG4123  115 nppyFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 43-157 1.95e-12

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: 64.62  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   43 LKYVADRVPLRGARVLDIGCGGGLLSEALAQ--AGADVTAIDLAPELVKVARLHaleSGATVDYRVQAAEDLAAEqPGSF 120
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKrfPQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLE-DSSF 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 896559443  121 DVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTI 157
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTF 136
PLN02244 PLN02244
tocopherol O-methyltransferase
 46-156 2.20e-12

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 65.54  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  46 VADRVPLRGARVLDIGCGGGLLSEALAQA-GADVTAIDLAPelVKVARLHALESGATVDYRVQAAEDLAAEQP---GSFD 121
Cdd:PLN02244 111 VPDDDEKRPKRIVDVGCGIGGSSRYLARKyGANVKGITLSP--VQAARANALAAAQGLSDKVSFQVADALNQPfedGQFD 188

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 896559443 122 VVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLST 156
Cdd:PLN02244 189 LVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVT 223
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 42-201 2.44e-12

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: 64.21  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   42 RLKYVADRVPLRGARVLDIGCGGGLLSEALAQAGAD---VTAIDLAPELVKVARLHAlESGATVDYRVQAAEDLAAEQpG 118
Cdd:TIGR01934  28 RRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDrgkVTGVDFSSEMLEVAKKKS-ELPLNIEFIQADAEALPFED-N 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  119 SFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHL----FLSTINRTAAAF-------AVAIVGaeyvaRLLPKGTHHY-- 185
Cdd:TIGR01934 106 SFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLvileFSKPANALLKKFykfylknVLPSIG-----GLISKNAEAYty 180

                         170       180
                  ....*....|....*....|.
gi 896559443  186 -----QEFIKPAELARWLREA 201
Cdd:TIGR01934 181 lpesiRAFPSQEELAAMLKEA 201
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
49-210 3.97e-12

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 63.83  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  49 RVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGATVDYR-VQ-AAEDLAAEQPGSFDVVTCM 126
Cdd:PRK11036  40 ELPPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQfIHcAAQDIAQHLETPVDLILFH 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443 127 EMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFAVAIVGA-EYVARLLPKG---THHYQEFIKPAELARWLREAD 202
Cdd:PRK11036 120 AVLEWVADPKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKRkkrTLSPDYPLDPEQVYQWLEEAG 199


                 ....*...
gi 896559443 203 MQLVDVSG 210
Cdd:PRK11036 200 WQIMGKTG 207
PRK06202 PRK06202
hypothetical protein; Provisional
 53-176 1.40e-11

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 61.94  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQAGA------DVTAIDLAPELVKVARLHALESGatVDYRVQAAEDLAAEqPGSFDVVTCM 126
Cdd:PRK06202  60 RPLTLLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARANPRRPG--VTFRQAVSDELVAE-GERFDVVTSN 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 896559443 127 EMLEHVPDPG--AIIEACKRLLKpgGHLFLSTINRTAAAFAVAIVGAEYVAR 176
Cdd:PRK06202 137 HFLHHLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYALFWAGTRLLSR 186
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
48-155 3.10e-11

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 61.73  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  48 DRVPLRGARVLDIGCGGGLLSEALAQAGA-DVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQpgsFDVVTC- 125
Cdd:COG2264  143 EKLLKPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDGP---YDLVVAn 219

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896559443 126 ------MEMLEHVpdpgaiieacKRLLKPGGHLFLS 155
Cdd:COG2264  220 ilanplIELAPDL----------AALLKPGGYLILS 245
PRK14967 PRK14967
putative methyltransferase; Provisional
 54-203 5.47e-11

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 60.45  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGGLLSEALAQAGAD-VTAIDLAPELVKVARLHALESGATVDyrVQAAEDLAAEQPGSFDVVTCM-----E 127
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGsVTAVDISRRAVRSARLNALLAGVDVD--VRRGDWARAVEFRPFDVVVSNppyvpA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443 128 MLEHVPDPGA----------------IIEACKRLLKPGGHLF-----LSTINRTAAAFAVAIVGAEYVAR-LLPKGthhy 185
Cdd:PRK14967 115 PPDAPPSRGParawdagpdgravldrLCDAAPALLAPGGSLLlvqseLSGVERTLTRLSEAGLDAEVVASqWIPFG---- 190

                        170       180
                 ....*....|....*....|
gi 896559443 186 qefikP--AELARWLREADM 203
Cdd:PRK14967 191 -----PvlRARAAWLERRGL 205
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 48-157 1.16e-10

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 59.97  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   48 DRVPLRGARVLDIGCGGGLLSEALAQAGAD-VTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQpgsFDVVTC- 125
Cdd:pfam06325 156 ERLVKPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPKEK---ADVVVAn 232

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 896559443  126 ------MEMLEHVpdpgaiieacKRLLKPGGHLFLSTI 157
Cdd:pfam06325 233 iladplIELAPDI----------YALVKPGGYLILSGI 260
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 51-152 1.29e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 59.40  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  51 PLRGARVLDIGCGGGLLSEALAQAG---ADVTAIDLAPELVKVA--RLHALESGATVDYrVQA-AEDLAAEQpGSFDVVT 124
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGreKLRDLGLSGNVEF-VQGdAEALPFPD-NSFDAVT 126

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896559443 125 cmeM---LEHVPD-PGAIIEACkRLLKPGGHL 152
Cdd:PRK00216 127 ---IafgLRNVPDiDKALREMY-RVLKPGGRL 154
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
48-157 1.52e-10

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 59.40  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  48 DRVPLRGARVLDIGCGGGLLSEALAQAGA-DVTAIDLAPELVKVARLHALESGatvdyrVQAAEDLAAEQPgSFDVVTC- 125
Cdd:PRK00517 114 EKLVLPGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQAVEAARENAELNG------VELNVYLPQGDL-KADVIVAn 186

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 896559443 126 ------MEMLEHVpdpgaiieacKRLLKPGGHLFLSTI 157
Cdd:PRK00517 187 ilanplLELAPDL----------ARLLKPGGRLILSGI 214
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 54-157 5.92e-10

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: 57.72  E-value: 5.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   54 GARVLDIGCG-GGLLSEALAQAGADVTAIDLAPELVKVA--RLHALESGATVDYRVQAAEDLaaeqPGSFDVVTCMEMLE 130
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLArkRVAAEGLARKVEVLLQDYRDF----DEPFDRIVSVGMFE 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 896559443  131 HVpdpG-----AIIEACKRLLKPGGHLFLSTI 157
Cdd:pfam02353 138 HV---GhenydTFFKKLYNLLPPGGLMLLHTI 166
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-123 6.23e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 56.84  E-value: 6.23e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896559443  52 LRGARVLDIGCGGGLLSEALAQAGA-DVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLaaEQPGSFDVV 123
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRI--PLGGSVDTV 114
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 43-134 6.74e-10

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 57.94  E-value: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  43 LKYVADRVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESGATVDYRVQA---AEDLaAEQPGS 119
Cdd:PLN02585 134 LLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKEALAALPPEVLPkfeANDL-ESLSGK 212

                         90
                 ....*....|....*
gi 896559443 120 FDVVTCMEMLEHVPD 134
Cdd:PLN02585 213 YDTVTCLDVLIHYPQ 227
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
48-209 1.18e-09

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 57.17  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  48 DRV-----PLRGARVLDIGCGGGLLSEALAQAGAD-VTAIDlaPELVKVARLHALESGATVDYRVQ----AAEDLAAEQp 117
Cdd:PRK15068 112 DRVlphlsPLKGRTVLDVGCGNGYHMWRMLGAGAKlVVGID--PSQLFLCQFEAVRKLLGNDQRAHllplGIEQLPALK- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443 118 gSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTInrtaaafavAIVGAEYVArLLPKGThhYQE-----FIkP- 191
Cdd:PRK15068 189 -AFDTVFSMGVLYHRRSPLDHLKQLKDQLVPGGELVLETL---------VIDGDENTV-LVPGDR--YAKmrnvyFI-Ps 254

                        170       180
                 ....*....|....*....|..
gi 896559443 192 -AELARWLREA---DMQLVDVS 209
Cdd:PRK15068 255 vPALKNWLERAgfkDVRIVDVS 276
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 54-154 1.84e-09

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: 55.58  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGGLLSEALAQA--GADVTAIDLAPELVKVARLHALESGATvDYRVQAAEDLAAEQPGSFDVVTC------ 125
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLE-NVEVLWSDGLSGVPDGSFDLILSnppfha 128

                         90       100       110
                 ....*....|....*....|....*....|....
gi 896559443 126 -----MEMLEhvpdpgAIIEACKRLLKPGGHLFL 154
Cdd:COG2813  129 gravdKEVAH------ALIADAARHLRPGGELWL 156
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
48-150 2.67e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 55.43  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  48 DRVPLRGARVLDIGCGGGLLSEALAQAGAD-VTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCm 126
Cdd:COG4076   30 ERVVKPGDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVIIS- 108

                         90       100
                 ....*....|....*....|....*...
gi 896559443 127 EMLEHV-PDPG--AIIE-ACKRLLKPGG 150
Cdd:COG4076  109 EMLDTAlLDEGqvPILNhARKRLLKPGG 136
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
44-152 6.83e-09

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 54.37  E-value: 6.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   44 KYVADRV-PLRGARVLDIGCGGGLLSEALAQ-AGA--DVTAIDLAPELVKVARLHALESG-ATVDYRVQAAEDLAAEQpG 118
Cdd:pfam01209  32 DFTMKCMgVKRGNKFLDVAGGTGDWTFGLSDsAGSsgKVVGLDINENMLKEGEKKAKEEGkYNIEFLQGNAEELPFED-D 110

                          90       100       110
                  ....*....|....*....|....*....|....
gi 896559443  119 SFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHL 152
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 54-158 9.13e-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: 54.01  E-value: 9.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGGLLSEALAQAGAD---VTAIDLAPELVKVAR--LHALESGATVDYRVQAAEDLAAEqpGSFDVVtcmeM 128
Cdd:COG2519   92 GARVLEAGTGSGALTLALARAVGPegkVYSYERREDFAEIARknLERFGLPDNVELKLGDIREGIDE--GDVDAV----F 165

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896559443 129 LEhVPDPGAIIEACKRLLKPGGHL--FLSTIN 158
Cdd:COG2519  166 LD-MPDPWEALEAVAKALKPGGVLvaYVPTVN 196
arsM PRK11873
arsenite methyltransferase;
54-178 2.69e-08

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 53.03  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGG---LLSEALAQAGADVTAIDLAPELVKVARLHALESGAT-VDYRVQAAEDLAAEQpGSFDVV--TCME 127
Cdd:PRK11873  78 GETVLDLGSGGGfdcFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEALPVAD-NSVDVIisNCVI 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896559443 128 MLehVPDPGAIIEACKRLLKPGGHLFLS----------TINRTAAAFAVAIVGAEYVARLL 178
Cdd:PRK11873 157 NL--SPDKERVFKEAFRVLKPGGRFAISdvvlrgelpeEIRNDAELYAGCVAGALQEEEYL 215
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
53-160 6.34e-08

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 52.16  E-value: 6.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCG-GGLLSEALAQAGADVTAIDLAPELVKVARlhALESGATVDYRVQAAEDLAaeqpGSFDVVTCMEMLEH 131
Cdd:PRK11705 167 PGMRVLDIGCGwGGLARYAAEHYGVSVVGVTISAEQQKLAQ--ERCAGLPVEIRLQDYRDLN----GQFDRIVSVGMFEH 240

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896559443 132 VpdpG-----AIIEACKRLLKPGGHLFLSTI--NRT 160
Cdd:PRK11705 241 V---GpknyrTYFEVVRRCLKPDGLFLLHTIgsNKT 273
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 53-178 2.66e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 49.32  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVAR--LHALE-SGATVDYRvQAAEDLAAEQPgsFDV--VTCme 127
Cdd:COG2518   66 PGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARerLAALGyDNVTVRVG-DGALGWPEHAP--FDRiiVTA-- 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896559443 128 MLEHVPDpgAIIEAckrlLKPGGHLflstinrtaaafaVAIVGAEYVARLL 178
Cdd:COG2518  141 AAPEVPE--ALLEQ----LAPGGRL-------------VAPVGEGGVQRLV 172
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 53-154 2.92e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.15  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQA--GADVTAIDLAPELVKVAR----LHALESGATVdyrVQAaeDLAA--EQPGSFDVVT 124
Cdd:COG2890  112 APPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARrnaeRLGLEDRVRF---LQG--DLFEplPGDGRFDLIV 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896559443 125 C---------MEML-----EHVP----DPGA--------IIEACKRLLKPGGHLFL 154
Cdd:COG2890  187 SnppyipedeIALLppevrDHEPrlalDGGEdgldfyrrIIAQAPRLLKPGGWLLL 242
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
54-151 4.31e-07

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 48.96  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGGLLSEALAQAGADVTAIDLAPelvkvARLHALEsgatvdyRVQAAEDLAAEQP-----------GSFDV 122
Cdd:PRK11207  31 PGKTLDLGCGNGRNSLYLAANGFDVTAWDKNP-----MSIANLE-------RIKAAENLDNLHTavvdlnnltfdGEYDF 98

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896559443 123 VTC---MEMLEHVPDPGaIIEACKRLLKPGGH 151
Cdd:PRK11207  99 ILStvvLMFLEAKTIPG-LIANMQRCTKPGGY 129
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 48-217 7.07e-07

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 48.94  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   48 DRV-----PLRGARVLDIGCGGGLLSEALAQAGAD-VTAIDlaPELVKVARLHALESGATVDYRVQ----AAEDLAAEQp 117
Cdd:pfam08003 105 DRVlphlsPLKGRTILDVGCGNGYHMWRMLGEGAAmVVGID--PSELFLCQFEAVRKLLGNDQRAHllplGIEQLPALA- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  118 gSFDVVTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTInrtaaafavAIVGAEYVArLLPKGTH---HYQEFIKPAE- 193
Cdd:pfam08003 182 -AFDTVFSMGVLYHRRSPLDHLLQLKDQLVKGGELVLETL---------VIDGDENTV-LVPGDRYaqmRNVYFIPSAAa 250

                         170       180
                  ....*....|....*....|....*..
gi 896559443  194 LARWLREA---DMQLVDVSGMAYEPWR 217
Cdd:pfam08003 251 LINWLEKCgfvDVRIVDVSVTTLEEQR 277
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 52-152 8.74e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 47.49  E-value: 8.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  52 LRGARVLDIGCGGGL----LSEALAqAGADVTAIDLAPELVKVARLHALESGAT--VDYRVQAAED-LAAEQPGSFDVVt 124
Cdd:COG4122   15 LGAKRILEIGTGTGYstlwLARALP-DDGRLTTIEIDPERAAIARENFARAGLAdrIRLILGDALEvLPRLADGPFDLV- 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 896559443 125 cmemL-----EHVPDpgaIIEACKRLLKPGGHL 152
Cdd:COG4122   93 ----FidadkSNYPD---YLELALPLLRPGGLI 118
PRK14968 PRK14968
putative methyltransferase; Provisional
 54-124 1.01e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 47.59  E-value: 1.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896559443  54 GARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARLHALESG-ATVDYRVQAAEDLAAEQPGSFDVVT 124
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNiRNNGVEVIRSDLFEPFRGDKFDVIL 95
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 51-159 1.15e-06

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: 47.20  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   51 PLRGARVLDIGCGGGLLSEALAQAGAD--VTAIDLAPELVKVAR----LHALESGatvdyRVQAAEDLAAEQPGSFDVVT 124
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKESPDaeLTMVDINARALESARenlaANGLENG-----EVVASDVYSGVEDGKFDLII 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 896559443  125 C----MEMLEHVPDPG-AIIEACKRLLKPGGHLFLsTINR 159
Cdd:pfam05175 104 SnppfHAGLATTYNVAqRFIADAKRHLRPGGELWI-VANR 142
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 49-152 1.68e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 47.76  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  49 RVP-LRGARVLDIGCGGGLLSEALAQ--AGADVTAIDLAPELVKVARlhalesGATVDYRVQAAEDLAAEQPgsFDVVTC 125
Cdd:PRK14103  24 RVGaERARRVVDLGCGPGNLTRYLARrwPGAVIEALDSSPEMVAAAR------ERGVDARTGDVRDWKPKPD--TDVVVS 95

                         90       100
                 ....*....|....*....|....*..
gi 896559443 126 MEMLEHVPDPGAIIEACKRLLKPGGHL 152
Cdd:PRK14103  96 NAALQWVPEHADLLVRWVDELAPGSWI 122
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
56-204 1.68e-06

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 46.78  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  56 RVLDIGCGGgllsealaQAGADVTAIDLAPelvkvarlhalesGATVDYRVQAAEDLAAEqPGSFDVVTCMEMLEHVPDP 135
Cdd:COG4627    5 LKLNIGCGP--------KRLPGWLNVDIVP-------------APGVDIVGDLTDPLPFP-DNSVDAIYSSHVLEHLDYE 62

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896559443 136 GAI--IEACKRLLKPGGHLFLST--INRTAAAFAVAIVGAEYVARLLPKGTHHYQEFIKPAELARWLREADMQ 204
Cdd:COG4627   63 EAPlaLKECYRVLKPGGILRIVVpdLEHVARLYLAEYDAALDVAELRLAGPIDPLGIILGERLAGLAARHSVL 135
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 53-154 3.66e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 46.69  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGGLLSEALAQA--GADVTAIDLAPELVKVARLHAlESGATVDYRVQAAEDLAAEQPGSFDVVTC----- 125
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARRNA-KHGLGARVEFLQGDWFEPLPGGRFDLIVSnppyi 186

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 896559443 126 ---------MEMLEHVP----DPGA--------IIEACKRLLKPGGHLFL 154
Cdd:PRK09328 187 peadihllqPEVRDHEPhlalFGGEdgldfyrrIIEQAPRYLKPGGWLLL 236
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
56-150 9.31e-06

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 44.82  E-value: 9.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  56 RVLDIGCG-GGLLSEALAQAG-ADVTAIDLAPELVKVARLH-ALESGATVDYRVQ-----AAEDLAaEQPGSFDVVtcme 127
Cdd:COG0421   40 RVLIIGGGdGGLARELLKHPPvERVDVVEIDPEVVELAREYfPLLAPAFDDPRLRvvigdGRAFLR-EAEESYDVI---- 114

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896559443 128 MLEhVPDPGAI---------IEACKRLLKPGG 150
Cdd:COG0421  115 IVD-LTDPVGPaeglftrefYEDCRRALKPGG 145
Methyltransf_18 pfam12847
Methyltransferase domain; Protein in this family function as methyltransferases.
 42-155 1.00e-05

Methyltransferase domain; Protein in this family function as methyltransferases.


Pssm-ID: 463730  Cd Length: 151  Bit Score: 43.96  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   42 RLKYVADRVPlRGARVLDIGCGGGLLSEALAQAGADVTAI--DLAPELVKVARLHALESGATVDYRVQAAEDLAAEQPGS 119
Cdd:pfam12847   4 RLQAIASLVP-PGSRVADIGTDHAYLPIYLVKNGIAPKAIasDINEGPLEKARENIEKYGLEDRIEVRLGDGLEVLEPGE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 896559443  120 FDVVTCMEMlehvpdpGA-----IIEACKRLLKPGGHLFLS 155
Cdd:pfam12847  83 VDTIVIAGM-------GGeliidILEAGPEVLKSVKRLILQ 116
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 54-155 1.77e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.13  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCGGGLLSEALAQA-GADVTAIDLAPELVKVARLHALESGATVDYRVqaAEDLAAEQP-GSFDVVTCMEMLEH 131
Cdd:PLN02336 267 GQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEFEV--ADCTKKTYPdNSFDVIYSRDTILH 344

                         90       100
                 ....*....|....*....|....
gi 896559443 132 VPDPGAIIEACKRLLKPGGHLFLS 155
Cdd:PLN02336 345 IQDKPALFRSFFKWLKPGGKVLIS 368
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 46-154 2.89e-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: 43.60  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  46 VADRVPLRGARVLDIGCGGGL----LseALAQAGADVTAID--------LApELVKVARLhaleSGATVdyrVQA-AEDL 112
Cdd:COG0357   60 LLPLLPKEGARVLDVGSGAGFpgipL--AIARPDLQVTLVDslgkkiafLR-EVVRELGL----KNVTV---VHGrAEEL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896559443 113 AAEQPgsFDVVTC-----MEMLehvpdpgaiIEACKRLLKPGGHLFL 154
Cdd:COG0357  130 APREK--FDVVTAravapLPDL---------LELALPLLKPGGRLLA 165
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
56-155 4.04e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 43.17  E-value: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443    56 RVLDIGCGGG--LLSEALAQAGADVTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQPGSFDVVTCMEMLEHVP 133
Cdd:smart00828   2 RVLDFGCGYGsdLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIK 81

                           90       100
                   ....*....|....*....|..
gi 896559443   134 DPGAIIEACKRLLKPGGHLFLS 155
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHLVLA 103
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 55-157 5.15e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 43.21  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  55 ARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARlhalESGATVDYRVQAAEDLAAEQpGSFDVVTCMEMLEHVPD 134
Cdd:PRK10258  44 THVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR----QKDAADHYLAGDIESLPLAT-ATFDLAWSNLAVQWCGN 118

                         90       100
                 ....*....|....*....|....
gi 896559443 135 -PGAIIEACkRLLKPGGHLFLSTI 157
Cdd:PRK10258 119 lSTALRELY-RVVRPGGVVAFTTL 141
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
54-154 6.10e-05

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 43.40  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  54 GARVLDIGCG-GGLLSEALAQAGADVTA--IDLAPELVKVARLHALESGATVDYRVQaaeDlaAEQP---GSFDVVTC-- 125
Cdd:COG0827  116 GLRILDPAVGtGNLLTTVLNQLKKKVNAygVEVDDLLIRLAAVLANLQGHPVELFHQ---D--ALQPlliDPVDVVISdl 190

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 896559443 126 -------------MEMLE-------HVPdpgaIIEACKRLLKPGGHLFL 154
Cdd:COG0827  191 pvgyypnderakrFKLKAdeghsyaHHL----FIEQSLNYLKPGGYLFF 235
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
43-92 1.31e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 41.81  E-value: 1.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896559443  43 LKYVADRVPLRGAR-VLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVAR 92
Cdd:PRK14896  18 VDRIVEYAEDTDGDpVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLR 68
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 51-150 1.67e-04

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. 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: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 41.84  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  51 PLRGARVLDIGCG--GGLLSEALAQAGA-DVTAIDLAPELVKVARlhalESGATVDYRVQAAEDLAAEQ-PGSFDVVtcm 126
Cdd:cd08232  163 DLAGKRVLVTGAGpiGALVVAAARRAGAaEIVATDLADAPLAVAR----AMGADETVNLARDPLAAYAAdKGDFDVV--- 235

                         90       100
                 ....*....|....*....|....
gi 896559443 127 emLEHVPDPGAiIEACKRLLKPGG 150
Cdd:cd08232  236 --FEASGAPAA-LASALRVVRPGG 256
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 51-92 1.84e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 41.65  E-value: 1.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 896559443  51 PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVAR 92
Cdd:COG0030   35 ITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILR 76
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 35-157 2.24e-04

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 41.26  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   35 LHALNPVRLKYVADRVPLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVARL------HALESGATVDYRVQA 108
Cdd:pfam05724  19 QEGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFFAeaglspPITELSGFKEYSSGN 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 896559443  109 AE-------DLAAEQPGSFDVVTCMEMLEHVPdPG---AIIEACKRLLKPGGHLFLSTI 157
Cdd:pfam05724  99 ISlycgdffTLPREELGKFDLIYDRAALCALP-PEmrpRYAKQMYELLPPGGRGLLITL 156
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 53-152 2.34e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 40.65  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   53 RGARVLDIGCGGGLLSEALAQAGAD-VTAIDLAPELVKVARLHALESGATVDYRVQAAEDLAAEQ-PGSFDVVTC----- 125
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGkVVGVDLGPMQLWKPRNDPGVTFIQGDIRDPETLDLLEELlGRKVDLVLSdgspf 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 896559443  126 MEMLEHVPDPGAI------IEACKRLLKPGGHL 152
Cdd:pfam01728 101 ISGNKVLDHLRSLdlvkaaLEVALELLRKGGNF 133
rADc smart00650
Ribosomal RNA adenine dimethylases;
51-92 2.70e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.19  E-value: 2.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 896559443    51 PLRGARVLDIGCGGGLLSEALAQAGADVTAIDLAPELVKVAR 92
Cdd:smart00650  11 LRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLR 52
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 43-150 3.94e-04

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 40.70  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  43 LKYVADRVPLrgARVLDIGCGGGLLSEALAQAGADVTAIDLAPelvkvARLHALESGATV-DYRVQAAE-DL-AAEQPGS 119
Cdd:PRK12335 112 VLEAVQTVKP--GKALDLGCGQGRNSLYLALLGFDVTAVDINQ-----QSLENLQEIAEKeNLNIRTGLyDInSASIQEE 184

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 896559443 120 FD-----VVTCMEMLEHVPDpgaIIEACKRLLKPGG 150
Cdd:PRK12335 185 YDfilstVVLMFLNRERIPA---IIKNMQEHTNPGG 217
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 46-114 7.00e-04

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. 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 has 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: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 39.89  E-value: 7.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896559443  46 VADRVPLR-GARVLDIGCGG-GLLSEALAQA-GADVTAIDLAPElvKVARLHALESGATVDYRvqAAEDLAA 114
Cdd:cd08260  157 LVHQARVKpGEWVAVHGCGGvGLSAVMIASAlGARVIAVDIDDD--KLELARELGAVATVNAS--EVEDVAA 224
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 55-155 7.05e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 7.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  55 ARVLDIGCG-GGLLSEALAQAGADVTAIDLAPELVKVARLHAlESGATVDYrvQAAEDLAAEQPGS-FDVVTCMEMLEHV 132
Cdd:PTZ00098  54 SKVLDIGSGlGGGCKYINEKYGAHVHGVDICEKMVNIAKLRN-SDKNKIEF--EANDILKKDFPENtFDMIYSRDAILHL 130

                         90       100
                 ....*....|....*....|....*
gi 896559443 133 P--DPGAIIEACKRLLKPGGHLFLS 155
Cdd:PTZ00098 131 SyaDKKKLFEKCYKWLKPNGILLIT 155
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 43-158 8.58e-04

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 39.27  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   43 LKYVADRVPlRGARVLDIGCGGGLLSEALA-QAGADVTAIDLAPELVkvarLHALESGATVdyrVQ--AAEDLAAEQPGS 119
Cdd:TIGR02081   4 LESILNLIP-PGSRVLDLGCGDGELLALLRdEKQVRGYGIEIDQDGV----LACVARGVNV---IQgdLDEGLEAFPDKS 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 896559443  120 FDVVTCMEMLEHVPDPGAIIeacKRLLKPGGHLFLSTIN 158
Cdd:TIGR02081  76 FDYVILSQTLQATRNPEEIL---DEMLRVGRHAIVSFPN 111
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 43-135 1.01e-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: 39.55  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  43 LKYVADRVPL-RGARVLDIGCGGGLLSEALAQA---GADVTAIDLAPELVKVAR-LHALESGATVDYRVQAAEDLAAEQP 117
Cdd:COG5459   69 LAELAEAGPDfAPLTVLDVGAGPGTAAWAAADAwpsLLDATLLERSAAALALGRrLARAAANPALETAEWRLADLAAALP 148

                         90
                 ....*....|....*....
gi 896559443 118 -GSFDVVTCMEMLEHVPDP 135
Cdd:COG5459  149 aPPADLVVASYVLNELADA 167
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 53-152 1.41e-03

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: 38.39  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCG-GGLLSEALAQaGADVTAIDLAPELVKVARL---HALESGATVdyRVQAAEDLaAEQPGSFD-VVT--- 124
Cdd:COG1041   26 EGDTVLDPFCGtGTILIEAGLL-GRRVIGSDIDPKMVEGAREnleHYGYEDADV--IRGDARDL-PLADESVDaIVTdpp 101

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896559443 125 -----------CMEMLEHVpdpgaiIEACKRLLKPGGHL 152
Cdd:COG1041  102 ygrsskisgeeLLELYEKA------LEEAARVLKPGGRV 134
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 48-152 2.20e-03

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 38.59  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  48 DRVPLR-GARVLDIGCGGG---LLSEALAQAGADVTAIDLAPElvKVARLHALesGA--TVDYRVQ--AAEDLAAEQPGS 119
Cdd:COG0604  133 DRGRLKpGETVLVHGAAGGvgsAAVQLAKALGARVIATASSPE--KAELLRAL--GAdhVIDYREEdfAERVRALTGGRG 208

                         90       100       110
                 ....*....|....*....|....*....|...
gi 896559443 120 FDVVtcmemLEHVPdpGAIIEACKRLLKPGGHL 152
Cdd:COG0604  209 VDVV-----LDTVG--GDTLARSLRALAPGGRL 234
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 43-145 2.99e-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: 37.43  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   43 LKYVADRVPlRGARVLDIGCGGGLLSEALAQA-GADVTAIDLAPELVkvarLHALESGATVdyrVQ--AAEDLAAEQPGS 119
Cdd:pfam07021   4 FRYILEWIP-PGSRVLDLGCGDGTLLYLLKEEkGVDGYGIELDAAGV----AECVAKGLYV---IQgdLDEGLEHFPDKS 75

                          90       100
                  ....*....|....*....|....*.
gi 896559443  120 FDVVTCMEMLEHVPDPGAIIEACKRL 145
Cdd:pfam07021  76 FDYVILSQTLQATRNPREVLDEMLRI 101
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 35-150 2.99e-03

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 38.28  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  35 LHALNPVRLKYvadrvplrGARVLDIGCG--GGLLSEALAQAGAdvTAIDLA-PELVKVARLHALESGATVDYRVQAAED 111
Cdd:cd08234  149 VHGLDLLGIKP--------GDSVLVFGAGpiGLLLAQLLKLNGA--SRVTVAePNEEKLELAKKLGATETVDPSREDPEA 218

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896559443 112 LAAEQPGSFDVVtcmemLEHVPDPgAIIEACKRLLKPGG 150
Cdd:cd08234  219 QKEDNPYGFDVV-----IEATGVP-KTLEQAIEYARRGG 251
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 53-168 5.25e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 37.18  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443  53 RGARVLDIGCGGG----LLSEALAQAGaDVTAIDLAPELVKVA--RLHALesgATVDYR-VQAAEDLAAEQP---GSFDV 122
Cdd:PLN02233  73 MGDRVLDLCCGSGdlafLLSEKVGSDG-KVMGLDFSSEQLAVAasRQELK---AKSCYKnIEWIEGDATDLPfddCYFDA 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 896559443 123 VTCMEMLEHVPDPGAIIEACKRLLKPGGHLFLSTINRTAAAFAVAI 168
Cdd:PLN02233 149 ITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSM 194
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 56-123 5.87e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 37.14  E-value: 5.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896559443  56 RVLDIGCG--GGLLSEALAQAGADVTAIDLAPELVKVARLHAL-ESGATVDYRVQAAEDlaAEQPGSFDVV 123
Cdd:PRK06522   2 KIAILGAGaiGGLFGAALAQAGHDVTLVARRGAHLDALNENGLrLEDGEITVPVLAADD--PAELGPQDLV 70
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 56-100 6.46e-03

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


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 36.95  E-value: 6.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 896559443   56 RVLDIGCGGGLLSEALAQAGAD--VTAIDLAPELVKVARLHALESGA 100
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNaeVIAVDISPDALAVAEENAEKNQL 163
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 60-139 6.50e-03

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 36.06  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896559443   60 IGCG--GGLLSEALAQAGADVTAIDLAPELVKVAR--LHALESGATVDYRVQAAEDlAAEQPGSFDV--VTC-------- 125
Cdd:pfam02558   4 LGAGaiGSLLGARLAKAGHDVTLILRGAELAAIKKngLRLTSPGGERIVPPPAVTS-ASESLGPIDLviVTVkayqteea 82

                          90
                  ....*....|....
gi 896559443  126 MEMLEHVPDPGAII 139
Cdd:pfam02558  83 LEDIAPLLGPNTVV 96
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH