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Conserved domains on  [gi|759893875|ref|WP_043580428|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Chromobacterium]

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

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List of domain hits

 Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 8-225 1.44e-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: 354.68  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875    8 EIDKFSQLAHKWWDKDSEFKPLHEINPLRLDFIDRHA------SLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKS 81
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   82 LKVAQLHSLESGVPIDYRCVAVEDLAAEMPGAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNRNAKAYLLA 161
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759893875  162 VVGAEYVLNMLPRGTHEYARFLKPSELGRMTRHAGLSLQTLSGMGYNPLTRIYSLNDDTAVNYL 225
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 8-225 1.44e-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: 354.68  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875    8 EIDKFSQLAHKWWDKDSEFKPLHEINPLRLDFIDRHA------SLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKS 81
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   82 LKVAQLHSLESGVPIDYRCVAVEDLAAEMPGAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNRNAKAYLLA 161
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759893875  162 VVGAEYVLNMLPRGTHEYARFLKPSELGRMTRHAGLSLQTLSGMGYNPLTRIYSLNDDTAVNYL 225
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-225 1.85e-70

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 218.45  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   2 SNVDELEIDKFSQLAHKWWDKDSEFKPLHEINPLRLDFID----RHAS--------LAGKKVLDVGCGGGILAESMAQKG 69
Cdd:PLN02396  74 TSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRstlcRHFSkdpssakpFEGLKFIDIGCGGGLLSEPLARMG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  70 AQVTGIDLAKKSLKVAQLHSLESGVP--IDYRCVAVEDLAAEMPgAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVF 147
Cdd:PLN02396 154 ATVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEKLADEGR-KFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATV 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759893875 148 FSTLNRNAKAYLLAVVGAEYVLNMLPRGTHEYARFLKPSELGRMTRHAGLSLQTLSGMGYNPLTRIYSLNDDTAVNYL 225
Cdd:PLN02396 233 LSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYI 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 13-152 4.89e-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: 144.00  E-value: 4.89e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  13 SQLAHKWWDKDsefkpLHEinplrldFIDRHAsLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLEs 92
Cdd:COG2227    3 DPDARDFWDRR-----LAA-------LLARLL-PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  93 gVPIDYRCVAVEDLAAEmPGAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLN 152
Cdd:COG2227   69 -LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-148 9.24e-27

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 98.89  E-value: 9.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   52 LDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSleSGVPIDYRCVAVEDLAAEmPGAFDVVTCMEMLEHVPDPQS 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 759893875  132 VVRACAQLVKPGGWVFF 148
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-149 3.48e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 69.00  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  50 KVLDVGCGGGILAESMAQ-KGAQVTGIDLAKKSLKVAQLHSLESGVP-IDYRCVAVEDLAAEMPGAFDVVTCMEMLEH-V 126
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 759893875 127 PDPQSVVRACAQLVKPGGWVFFS 149
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 8-225 1.44e-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: 354.68  E-value: 1.44e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875    8 EIDKFSQLAHKWWDKDSEFKPLHEINPLRLDFIDRHA------SLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKS 81
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIrknfknPLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   82 LKVAQLHSLESGVPIDYRCVAVEDLAAEMPGAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNRNAKAYLLA 161
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759893875  162 VVGAEYVLNMLPRGTHEYARFLKPSELGRMTRHAGLSLQTLSGMGYNPLTRIYSLNDDTAVNYL 225
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 2-225 1.85e-70

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 218.45  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   2 SNVDELEIDKFSQLAHKWWDKDSEFKPLHEINPLRLDFID----RHAS--------LAGKKVLDVGCGGGILAESMAQKG 69
Cdd:PLN02396  74 TSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRstlcRHFSkdpssakpFEGLKFIDIGCGGGLLSEPLARMG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  70 AQVTGIDLAKKSLKVAQLHSLESGVP--IDYRCVAVEDLAAEMPgAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVF 147
Cdd:PLN02396 154 ATVTGVDAVDKNVKIARLHADMDPVTstIEYLCTTAEKLADEGR-KFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATV 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759893875 148 FSTLNRNAKAYLLAVVGAEYVLNMLPRGTHEYARFLKPSELGRMTRHAGLSLQTLSGMGYNPLTRIYSLNDDTAVNYL 225
Cdd:PLN02396 233 LSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYI 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 13-152 4.89e-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: 144.00  E-value: 4.89e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  13 SQLAHKWWDKDsefkpLHEinplrldFIDRHAsLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLEs 92
Cdd:COG2227    3 DPDARDFWDRR-----LAA-------LLARLL-PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  93 gVPIDYRCVAVEDLAAEmPGAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLN 152
Cdd:COG2227   69 -LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-153 1.47e-28

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: 105.08  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  35 LRLDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLAAEmPGAF 114
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 759893875 115 DVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNR 153
Cdd:COG2226   89 DLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-148 9.24e-27

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 98.89  E-value: 9.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   52 LDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSleSGVPIDYRCVAVEDLAAEmPGAFDVVTCMEMLEHVPDPQS 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 759893875  132 VVRACAQLVKPGGWVFF 148
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-144 6.22e-26

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 96.86  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   51 VLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLAAEmPGAFDVVTCMEMLEHVPDP 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 759893875  130 Q--SVVRACAQLVKPGG 144
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-199 1.61e-24

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 95.19  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   47 AGKKVLDVGCGGGILAESMAQKGAQVTGIDLAkkslkvaqLHSLESGVPIDYRCVAVEDLAAEMPGAFDVVTCMEMLEHV 126
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPS--------PIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHV 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759893875  127 PDPQSVVRACAQLVKPGGWVFFSTLNRNAKAYLLavvgAEYVLNMLPRGTHeyARFLKPSELGRMTRHAGLSL 199
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH--ISLFSARSLKRLLEEAGFEV 160
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 19-150 1.13e-22

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 89.99  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  19 WWDKD---------SEFKPLHEINPLRLDFIDRHASL-AGKKVLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQL 87
Cdd:COG2230   13 FLDPTmtyscayfeDPDDTLEEAQEAKLDLILRKLGLkPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARE 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759893875  88 HSLESGVP--IDYRCVAVEDLAAEmpGAFDVVTCMEMLEHVPDPQ--SVVRACAQLVKPGGWVFFST 150
Cdd:COG2230   93 RAAEAGLAdrVEVRLADYRDLPAD--GQFDAIVSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
35-150 2.07e-22

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 90.06  E-value: 2.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  35 LRLDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQlhslESGVPIDYRCVAVEDLAAEmPGAF 114
Cdd:COG4976   34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLADLAEP-DGRF 108

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 759893875 115 DVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFST 150
Cdd:COG4976  109 DLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 19-149 4.43e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.89  E-value: 4.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  19 WWDKDSEFkplhEINPLRLDFIDRHASL-AGKKVLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQLHSLESGVP- 95
Cdd:COG0500    1 PWDSYYSD----ELLPGLAALLALLERLpKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGn 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 759893875  96 IDYRCVAVEDLAAEMPGAFDVVTCMEMLEHVP--DPQSVVRACAQLVKPGGWVFFS 149
Cdd:COG0500   77 VEFLVADLAELDPLPAESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLS 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
47-150 5.50e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 78.71  E-value: 5.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  47 AGKKVLDVGCGGGILAESMAQK--GAQVTGIDLAKKSLKVAQlhslESGVPIDYRCVAVEDLAAemPGAFDVVTCMEMLE 124
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR----ARLPNVRFVVADLRDLDP--PEPFDLVVSNAALH 74

                         90       100
                 ....*....|....*....|....*.
gi 759893875 125 HVPDPQSVVRACAQLVKPGGWVFFST 150
Cdd:COG4106   75 WLPDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 52-146 2.52e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 71.63  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   52 LDVGCGGGILAESMAQK--GAQVTGIDLAKKSLKVA--QLHSLESGVPIDYRcVAVEDLAAEMPGAFDVVTCMEMLEHVP 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAAreRLAALGLLNAVRVE-LFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 759893875  128 DPQSVVRACAQLVKPGGWV 146
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
PRK08317 PRK08317
hypothetical protein; Provisional
 47-146 3.18e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 72.28  E-value: 3.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  47 AGKKVLDVGCGGGILAESMAQ---KGAQVTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLAAEmPGAFDVVTCMEML 123
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFP-DGSFDAVRSDRVL 97

                         90       100
                 ....*....|....*....|...
gi 759893875 124 EHVPDPQSVVRACAQLVKPGGWV 146
Cdd:PRK08317  98 QHLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-149 3.48e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 69.00  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  50 KVLDVGCGGGILAESMAQ-KGAQVTGIDLAKKSLKVAQLHSLESGVP-IDYRCVAVEDLAAEMPGAFDVVTCMEMLEH-V 126
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90       100
                 ....*....|....*....|...
gi 759893875 127 PDPQSVVRACAQLVKPGGWVFFS 149
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
PLN02244 PLN02244
tocopherol O-methyltransferase
 37-150 5.35e-14

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 69.77  E-value: 5.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHASLAG---------KKVLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQLHSLESGVPiDYRCVAVEDl 106
Cdd:PLN02244  99 IRMIEESLAWAGvpdddekrpKRIVDVGCGIGGSSRYLARKyGANVKGITLSPVQAARANALAAAQGLS-DKVSFQVAD- 176

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 759893875 107 AAEMP---GAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFST 150
Cdd:PLN02244 177 ALNQPfedGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 37-139 2.03e-13

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 67.17  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVP--IDYRcvaVEDLAAEMpGAF 114
Cdd:PRK07580  53 LSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFE---VGDLESLL-GRF 128

                         90       100
                 ....*....|....*....|....*
gi 759893875 115 DVVTCMEMLEHVPDPQsVVRACAQL 139
Cdd:PRK07580 129 DTVVCLDVLIHYPQED-AARMLAHL 152
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
51-174 1.34e-11

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 62.29  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  51 VLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVPIDYRCV--AVEDLAAEMPGAFDVVTCMEMLEHVPD 128
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIhcAAQDIAQHLETPVDLILFHAVLEWVAD 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 759893875 129 PQSVVRACAQLVKPGGWVFFSTLNRNAKAYLLAVVGA-EYVLNMLPR 174
Cdd:PRK11036 128 PKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPK 174
PRK06202 PRK06202
hypothetical protein; Provisional
 51-165 4.39e-11

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 60.40  E-value: 4.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  51 VLDVGCGGGILAESMA----QKGAQ--VTGIDLAKKSLKVAQLHSLESGVpiDYRCVAVEDLAAEmPGAFDVVTCMEMLE 124
Cdd:PRK06202  64 LLDIGCGGGDLAIDLArwarRDGLRleVTAIDPDPRAVAFARANPRRPGV--TFRQAVSDELVAE-GERFDVVTSNHFLH 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759893875 125 HVPDPQ--SVVRACAQLVKpgGWVFFSTLNRNAKAYLLAVVGA 165
Cdd:PRK06202 141 HLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYALFWAGT 181
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 47-144 4.94e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.97  E-value: 4.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   47 AGKKVLDVGCGGGILAESMAQK---GAQVTGIDLAKKSLKVAQLHSLESGVpIDYRCVAVEDLAAEM---PGAFDVVTCM 120
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPElleDDKFDVVISN 81

                          90       100
                  ....*....|....*....|....
gi 759893875  121 EMLEHVPDPQSVVRACAQLVKPGG 144
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGG 105
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
44-151 6.60e-11

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 61.03  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  44 ASLAGKKVLDVGCGGGILAESMAQKGAQ-VTGIDLAKKSLkvAQLHSLE----SGVPIDYRCVAVEDLAAemPGAFDVVT 118
Cdd:PRK15068 119 SPLKGRTVLDVGCGNGYHMWRMLGAGAKlVVGIDPSQLFL--CQFEAVRkllgNDQRAHLLPLGIEQLPA--LKAFDTVF 194

                         90       100       110
                 ....*....|....*....|....*....|...
gi 759893875 119 CMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTL 151
Cdd:PRK15068 195 SMGVLYHRRSPLDHLKQLKDQLVPGGELVLETL 227
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 37-151 1.48e-10

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: 59.22  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   37 LDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGI--DLAKKSLKVAQLHsleSGVPIDYRCVAVEDLAAEmPGAF 114
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIalDISAGMLAQAKTK---LSENVQFICGDAEKLPLE-DSSF 99

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 759893875  115 DVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTL 151
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTF 136
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 16-119 6.04e-10

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: 57.20  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  16 AHKWWDKDSEFKPLHEINP----------LRL-DFIDRHASLAGKKVLDVGCGGGILAESMAQKGA-QVTGIDLAKKSLK 83
Cdd:COG3897   28 AHPLWDATEEALGESGAPPpfwaflwpsgQALaRYLLDHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALA 107

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 759893875  84 VAQLHSLESGVPIDYRCVAVEDLAAEmpGAFDVVTC 119
Cdd:COG3897  108 ALRLNAALNGVAITTRLGDWRDPPAA--GGFDLILG 141
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 36-198 8.49e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 57.09  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  36 RLDFIDRHASLAGKKVLDVGCGGGILAESMAQKG---AQVTGIDLAKKSLKVAQ--LHSLESGVPIDYrcvaVEDLAAEM 110
Cdd:PRK00216  40 RRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGRekLRDLGLSGNVEF----VQGDAEAL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875 111 P---GAFDVVTcmeM---LEHVPDPQSVVRACAQLVKPGGWVF---FSTlnrnAKAYLLAVVGAEYVLNMLPR------- 174
Cdd:PRK00216 116 PfpdNSFDAVT---IafgLRNVPDIDKALREMYRVLKPGGRLVileFSK----PTNPPLKKAYDFYLFKVLPLigklisk 188

                        170       180       190
                 ....*....|....*....|....*....|.
gi 759893875 175 GTHEYA-------RFLKPSELGRMTRHAGLS 198
Cdd:PRK00216 189 NAEAYSylaesirAFPDQEELAAMLEEAGFE 219
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
37-149 1.79e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 56.33  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHAsLAGKKVLDVGCGGGILAESMAQKGA-QVTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLAaemPGAFD 115
Cdd:COG2264  139 LEALEKLL-KPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLE---DGPYD 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 759893875 116 VVTC-------MEMLEHVpdpqsvvracAQLVKPGGWVFFS 149
Cdd:COG2264  215 LVVAnilanplIELAPDL----------AALLKPGGYLILS 245
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 37-128 4.09e-09

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 55.63  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGIDL-------AKKSLKVAQLHSLESGVPIDYrcvaVEDLaAE 109
Cdd:PLN02585 134 LLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDIsaamvaeAERRAKEALAALPPEVLPKFE----ANDL-ES 208

                         90
                 ....*....|....*....
gi 759893875 110 MPGAFDVVTCMEMLEHVPD 128
Cdd:PLN02585 209 LSGKYDTVTCLDVLIHYPQ 227
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 47-148 4.66e-09

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: 54.77  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  47 AGKKVLDVGCGGGILAESMAQK--GAQVTGI-------DLAKKSLKVAQLHSLesgvpIDYRCVAVEDLAAEM-PGAFDV 116
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQRspGARITGVeiqpeaaELARRNVALNGLEDR-----ITVIHGDLKEFAAELpPGSFDL 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 759893875 117 VTC----MEMLEHV--PDPQ-------------SVVRACAQLVKPGGWVFF 148
Cdd:COG4123  112 VVSnppyFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
37-117 6.30e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.14  E-value: 6.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQ-VTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLaaEMPGAFD 115
Cdd:COG2263   35 LHLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERLGVRVDFIRADVTRI--PLGGSVD 112


                 ..
gi 759893875 116 VV 117
Cdd:COG2263  113 TV 114
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 30-149 7.01e-09

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: 54.96  E-value: 7.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   30 HEINPLRLDFIDRHAsLAGKKVLDVGCGGGILAESMAQKGAQ-VTGIDLAKKSLKVAQLHSLESGVPIDYRCVAVEDLAA 108
Cdd:pfam06325 145 HPTTKLCLEALERLV-KPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPK 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 759893875  109 EmpgAFDVVTC-------MEMLEHVpdpqsvvracAQLVKPGGWVFFS 149
Cdd:pfam06325 224 E---KADVVVAniladplIELAPDI----------YALVKPGGYLILS 258
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-146 7.48e-09

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 54.37  E-value: 7.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   40 IDRHASLAGKKVLDVGCGGG----ILAESMAQKGaQVTGIDLAKKSLKVAQLHSLESGV-PIDYRCVAVEDLAAEmPGAF 114
Cdd:pfam01209  35 MKCMGVKRGNKFLDVAGGTGdwtfGLSDSAGSSG-KVVGLDINENMLKEGEKKAKEEGKyNIEFLQGNAEELPFE-DDSF 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 759893875  115 DVVTCMEMLEHVPDPQSVVRACAQLVKPGGWV 146
Cdd:pfam01209 113 DIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
37-149 1.55e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 53.62  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHAsLAGKKVLDVGCGGGILAESMAQKGA-QVTGIDLAKKSLKVAQLHSLESGVpidyrcvaveDLAAEMPGA-- 113
Cdd:PRK00517 110 LEALEKLV-LPGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDPQAVEAARENAELNGV----------ELNVYLPQGdl 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 759893875 114 -FDVVTC-------MEMLEHVpdpqsvvracAQLVKPGGWVFFS 149
Cdd:PRK00517 179 kADVIVAnilanplLELAPDL----------ARLLKPGGRLILS 212
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 30-149 4.41e-08

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 52.53  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   30 HEINPLRLDFIDRhASLAGKKVLDVGCGGGILAESMAQKGAQ-VTGIDLAKKSLKVAQLHSLESGVPIDYRcVAVEDLAA 108
Cdd:TIGR00406 143 HPTTSLCLEWLED-LDLKDKNVIDVGCGSGILSIAALKLGAAkVVGIDIDPLAVESARKNAELNQVSDRLQ-VKLIYLEQ 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 759893875  109 EMPGAFDVVTCMEMLEHVPD--PQSVvracaQLVKPGGWVFFS 149
Cdd:TIGR00406 221 PIEGKADVIVANILAEVIKElyPQFS-----RLVKPGGWLILS 258
PRK14968 PRK14968
putative methyltransferase; Provisional
 47-118 4.28e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.74  E-value: 4.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759893875  47 AGKKVLDVGCGGGILAESMAQKGAQVTGIDL-------AKKSLKVAQLHslESGVPIdYRCVAVEDLAAEmpgAFDVVT 118
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDInpyavecAKCNAKLNNIR--NNGVEV-IRSDLFEPFRGD---KFDVIL 95
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
48-126 4.58e-07

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 49.85  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  48 GKKVLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQLHSleSGVPI-----DYRcvavedlaaEMPGAFDVVTCME 121
Cdd:PRK11705 168 GMRVLDIGCGWGGLARYAAEHyGVSVVGVTISAEQQKLAQERC--AGLPVeirlqDYR---------DLNGQFDRIVSVG 236


                 ....*
gi 759893875 122 MLEHV 126
Cdd:PRK11705 237 MFEHV 241
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 40-148 5.92e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 48.99  E-value: 5.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  40 IDRHASLAGKKVLDVGCGGGILAESMAQ--KGAQVTGIDLAKKSLKVA----QLHSLESGVpidyrCVAVEDLAAEMPGA 113
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIALALAKerPDARVTAVDISPDALAVArrnaERLGLEDRV-----RFLQGDLFEPLPGD 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759893875 114 --FDVVTC---------MEMLEHV-------------PDPQSVVRACA----QLVKPGGWVFF 148
Cdd:COG2890  180 grFDLIVSnppyipedeIALLPPEvrdheprlaldggEDGLDFYRRIIaqapRLLKPGGWLLL 242
PRK14967 PRK14967
putative methyltransferase; Provisional
 48-119 1.23e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 47.74  E-value: 1.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759893875  48 GKKVLDVGCGGGILAESMAQKGA-QVTGIDLAKKSLKVAQLHSLESGVPIDyrcVAVEDLAAEMPGA-FDVVTC 119
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVDVD---VRRGDWARAVEFRpFDVVVS 107
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 29-126 2.44e-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: 47.32  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   29 LHEINPLRLDFIDRHASL-AGKKVLDVGCG-GGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVP-------IDYR 99
Cdd:pfam02353  42 LEEAQQAKLDLILDKLGLkPGMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLArkvevllQDYR 121

                          90       100
                  ....*....|....*....|....*..
gi 759893875  100 cvavedlaaEMPGAFDVVTCMEMLEHV 126
Cdd:pfam02353 122 ---------DFDEPFDRIVSVGMFEHV 139
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 38-156 2.48e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 47.82  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  38 DFIDRHASLAGKKVLDVGCGGGILAESMAQK-GAQVTGIDLAKKSLKVAQLHSlesgvpIDYRCvAVEDLAAEMP----- 111
Cdd:PLN02336 257 EFVDKLDLKPGQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERA------IGRKC-SVEFEVADCTkktyp 329

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 759893875 112 -GAFDVVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNRNAK 156
Cdd:PLN02336 330 dNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPG 375
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 29-151 2.71e-06

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: 46.65  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   29 LHEINPLRLDFIDRHASLAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSL-KVAQLHSLE------------SGVP 95
Cdd:pfam05724  19 QEGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISELAVeKFFAEAGLSppitelsgfkeySSGN 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 759893875   96 IDYRCVAVEDLAAEMPGAFDVVTCMEMLEHVP--DPQSVVRACAQLVKPGGWVFFSTL 151
Cdd:pfam05724  99 ISLYCGDFFTLPREELGKFDLIYDRAALCALPpeMRPRYAKQMYELLPPGGRGLLITL 156
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 46-151 2.83e-05

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: 44.32  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875   46 LAGKKVLDVGCGGGILAESMAQKGAQ-VTGIDlaKKSLKVAQLHSLESGVPIDYRC----VAVEDLAAEmpGAFDVVTCM 120
Cdd:pfam08003 114 LKGRTILDVGCGNGYHMWRMLGEGAAmVVGID--PSELFLCQFEAVRKLLGNDQRAhllpLGIEQLPAL--AAFDTVFSM 189

                          90       100       110
                  ....*....|....*....|....*....|.
gi 759893875  121 EMLEHVPDPQSVVRACAQLVKPGGWVFFSTL 151
Cdd:pfam08003 190 GVLYHRRSPLDHLLQLKDQLVKGGELVLETL 220
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 38-148 5.64e-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: 42.83  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  38 DFIDRHA--SLA--------GKKVLDVGCGGG----ILAesMAQKGAQVTGID-LAKKS--LK--VAQLHsLESGVPIDY 98
Cdd:COG0357   48 ELWERHIldSLAllpllpkeGARVLDVGSGAGfpgiPLA--IARPDLQVTLVDsLGKKIafLRevVRELG-LKNVTVVHG 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759893875  99 RcvaVEDLAAEmpGAFDVVTC-----MEMLehvpdpqsvVRACAQLVKPGGWVFF 148
Cdd:COG0357  125 R---AEELAPR--EKFDVVTAravapLPDL---------LELALPLLKPGGRLLA 165
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 48-119 5.87e-05

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: 42.19  E-value: 5.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759893875   48 GKKVLDVGCGGGILAESMAQKG--AQVTGIDLAKKSLKVAQLHSLESGVPiDYRCVAVEDLAAEMPGAFDVVTC 119
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLE-NGEVVASDVYSGVEDGKFDLIIS 104
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
42-144 6.51e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 42.72  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  42 RHASLAGKKVLDVGCGGGILAESMAQKGA-QVTGIDLAKKSLKVAQLHSLESGVpiDYRCVAVEDLAAE--MPGAFDVVT 118
Cdd:COG4076   30 ERVVKPGDVVLDIGTGSGLLSMLAARAGAkKVYAVEVNPDIAAVARRIIAANGL--SDRITVINADATDldLPEKADVII 107

                         90       100       110
                 ....*....|....*....|....*....|
gi 759893875 119 CmEMLEHV-PDPQSV---VRACAQLVKPGG 144
Cdd:COG4076  108 S-EMLDTAlLDEGQVpilNHARKRLLKPGG 136
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 38-148 6.67e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 42.75  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  38 DFIDRHASLAGKKVLDVGCGGGILAESMAQK--GAQVTGIDLAKKSLKVAQlhslESGVpiDYRCVAVEDLAAEMPgaFD 115
Cdd:PRK14103  20 DLLARVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR----ERGV--DARTGDVRDWKPKPD--TD 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 759893875 116 VVTCMEMLEHVPDPQSVVRACAQLVKPGGWVFF 148
Cdd:PRK14103  92 VVVSNAALQWVPEHADLLVRWVDELAPGSWIAV 124
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 40-86 1.33e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.07  E-value: 1.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 759893875  40 IDRHASLAGKKVLDVGCGGGILAESMAQ--KGAQVTGIDLAKKSLKVAQ 86
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALALAKerPDAEVTAVDISPEALAVAR 149
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 37-144 2.23e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding 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 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. 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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 41.43  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  37 LDFIDRHASL-AGKKVLDVGCGGGI------LAESMaqkGAQVTGIDLAKkslKVAQLHSLESGVPIDYRcvaVEDLAAE 109
Cdd:cd08267  132 LQALRDAGKVkPGQRVLINGASGGVgtfavqIAKAL---GAHVTGVCSTR---NAELVRSLGADEVIDYT---TEDFVAL 202

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 759893875 110 MPGA--FDVVtcmemLEHVPDPQSVVRACAQLVKPGG 144
Cdd:cd08267  203 TAGGekYDVI-----FDAVGNSPFSLYRASLALKPGG 234
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 47-119 5.48e-04

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: 39.79  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  47 AGKKVLDVGCGGGILAESMAQK--GAQVTGID-------LAKKSLKVAQLHslesgvpiDYRCVAVEDLAAEMPGAFDVV 117
Cdd:COG2813   49 LGGRVLDLGCGYGVIGLALAKRnpEARVTLVDvnaraveLARANAAANGLE--------NVEVLWSDGLSGVPDGSFDLI 120


                 ..
gi 759893875 118 TC 119
Cdd:COG2813  121 LS 122
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 50-128 1.21e-03

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 39.16  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  50 KVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVPIDyrcVAVEDL-AAEMPGAFD-----VVTCMEML 123
Cdd:PRK12335 123 KALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIR---TGLYDInSASIQEEYDfilstVVLMFLNR 199


                 ....*
gi 759893875 124 EHVPD 128
Cdd:PRK12335 200 ERIPA 204
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 46-117 1.48e-03

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: 39.00  E-value: 1.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759893875  46 LAGKKVLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQLHSLESGVP-IDYRCVAVEDLAAEMP--GAFDVV 117
Cdd:COG2265  232 TGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLEEVLPELLwgGRPDVV 306
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 43-151 2.10e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 38.20  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  43 HASLAGKK---VLDVGCGGGILAESMAQKGAQVTGIDLAKKSLKVAQlhslESGVPIDYRCVAVEDLAAEmPGAFDVVTC 119
Cdd:PRK10258  35 LAMLPQRKfthVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR----QKDAADHYLAGDIESLPLA-TATFDLAWS 109

                         90       100       110
                 ....*....|....*....|....*....|..
gi 759893875 120 MEMLEHVPDPQSVVRACAQLVKPGGWVFFSTL 151
Cdd:PRK10258 110 NLAVQWCGNLSTALRELYRVVRPGGVVAFTTL 141
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
46-145 2.83e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 37.41  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  46 LAGKKVLDVGCGGGILAESMAQKGAQVTGIDlaKKSLKVAQLHSLESGVPIDYRCVAVEDL-AAEMPGAFDVVTC---ME 121
Cdd:PRK11207  29 VKPGKTLDLGCGNGRNSLYLAANGFDVTAWD--KNPMSIANLERIKAAENLDNLHTAVVDLnNLTFDGEYDFILStvvLM 106

                         90       100
                 ....*....|....*....|....*.
gi 759893875 122 MLEHVPDPQSV--VRACaqlVKPGGW 145
Cdd:PRK11207 107 FLEAKTIPGLIanMQRC---TKPGGY 129
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 48-168 4.90e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 36.99  E-value: 4.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  48 GKKVLDVGCGGGILAESMAQKGAQVTGID-------LAKKSLKVAQLHSLEsgvpidyrcVAVEDLAAEMPGA--FDV-- 116
Cdd:COG2518   67 GDRVLEIGTGSGYQAAVLARLAGRVYSVErdpelaeRARERLAALGYDNVT---------VRVGDGALGWPEHapFDRii 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 759893875 117 VTCmeMLEHVPDPqsvvrACAQLvKPGGWvffstlnrnakayLLAVVGAEYV 168
Cdd:COG2518  138 VTA--AAPEVPEA-----LLEQL-APGGR-------------LVAPVGEGGV 168
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 48-158 6.27e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 36.79  E-value: 6.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759893875  48 GKKVLDVGCGGGILAESMAQK---GAQVTGIDLAKKSLKVAQLHSlESGVPIDYRCVA-VEDLAAEMP---GAFDVVTCM 120
Cdd:PLN02233  74 GDRVLDLCCGSGDLAFLLSEKvgsDGKVMGLDFSSEQLAVAASRQ-ELKAKSCYKNIEwIEGDATDLPfddCYFDAITMG 152

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 759893875 121 EMLEHVPDPQSVVRACAQLVKPGGWVFFSTLNRNAKAY 158
Cdd:PLN02233 153 YGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPF 190
 
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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