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Conserved domains on  [gi|1569545716|gb|RYL55175|]
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bifunctional 3-demethylubiquinone 3-O-methyltransferase/2-octaprenyl-6-hydroxy phenol methylase [Klebsiella pneumoniae]

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 ...
 16-234 1.48e-134

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: 377.79  E-value: 1.48e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  91 LQVARLHALESGIQVDYVQETVEEHAAKHPQQYDVVTCMEMLEHVPDPQSVVHACARLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1569545716 171 VVGAEYVMKMVPKGTHDVKKFIKPAELLGWVDQTTLKEQHIIGLHYNPLTNTFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 1.48e-134

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: 377.79  E-value: 1.48e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  91 LQVARLHALESGIQVDYVQETVEEHAAKHPQQYDVVTCMEMLEHVPDPQSVVHACARLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1569545716 171 VVGAEYVMKMVPKGTHDVKKFIKPAELLGWVDQTTLKEQHIIGLHYNPLTNTFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 4-242 1.68e-62

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 198.42  E-value: 1.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716   4 EKTSVAPNVDHAEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGGLFGK-----------KVLDVGCGGGILAE 72
Cdd:PLN02396   68 RSTSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  73 SMAREGATVTGLDMGAEPLQVARLHAlesgiQVDYVQETVE------EHAAKHPQQYDVVTCMEMLEHVPDPQSVVHACA 146
Cdd:PLN02396  148 PLARMGATVTGVDAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLS 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716 147 RLVKPGGQVFFSTINRNGKAWLMAVVGAEYVMKMVPKGTHDVKKFIKPAELLGWVDQTTLKEQHIIGLHYNPLTNTFKLA 226
Cdd:PLN02396  223 ALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLS 302

                         250
                  ....*....|....*.
gi 1569545716 227 PGVDVNYMLHTTAKQD 242
Cdd:PLN02396  303 DDISVNYIAYGTKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 2.48e-40

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: 135.15  E-value: 2.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALEsgIQVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVP 136
Cdd:COG2227    25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|....*
gi 1569545716 137 DPQSVVHACARLVKPGGQVFFSTIN 161
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-153 6.47e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 91.86  E-value: 6.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  60 VLDVGCGGGILAESMARE-GATVTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVPDP 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1569545716 139 Q--SVVHACARLVKPGG 153
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 4.28e-14

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: 66.30  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVEEHAAKHPQQYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1569545716 136 PDPQSVVHACARLVKPGGQVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
58-166 7.64e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 36.63  E-value: 7.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716   58 KKVLDVGCGGGILAESMAREGA--TVTGLDMGAEPLQVARLHALESGiqvdyVQETVEEHAAK-----HPQQYDVVTCME 130
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALG-----LQGRIRIFYRDsakdpFPDTYDLVFGFE 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1569545716  131 MLEHVPDPQSVVHACARLVKPGGQVFFSTINRNGKA 166
Cdd:smart00828  76 VIHHIKDKMDLFSNISRHLKDGGHLVLADFIANLLS 111
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 1.48e-134

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: 377.79  E-value: 1.48e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  91 LQVARLHALESGIQVDYVQETVEEHAAKHPQQYDVVTCMEMLEHVPDPQSVVHACARLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1569545716 171 VVGAEYVMKMVPKGTHDVKKFIKPAELLGWVDQTTLKEQHIIGLHYNPLTNTFKLAPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 4-242 1.68e-62

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 198.42  E-value: 1.68e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716   4 EKTSVAPNVDHAEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERSGGLFGK-----------KVLDVGCGGGILAE 72
Cdd:PLN02396   68 RSTSTTTSLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  73 SMAREGATVTGLDMGAEPLQVARLHAlesgiQVDYVQETVE------EHAAKHPQQYDVVTCMEMLEHVPDPQSVVHACA 146
Cdd:PLN02396  148 PLARMGATVTGVDAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLS 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716 147 RLVKPGGQVFFSTINRNGKAWLMAVVGAEYVMKMVPKGTHDVKKFIKPAELLGWVDQTTLKEQHIIGLHYNPLTNTFKLA 226
Cdd:PLN02396  223 ALTIPNGATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLS 302

                         250
                  ....*....|....*.
gi 1569545716 227 PGVDVNYMLHTTAKQD 242
Cdd:PLN02396  303 DDISVNYIAYGTKRKD 318
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 2.48e-40

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: 135.15  E-value: 2.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALEsgIQVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVP 136
Cdd:COG2227    25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|....*
gi 1569545716 137 DPQSVVHACARLVKPGGQVFFSTIN 161
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 57-170 3.67e-27

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: 101.61  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVP 136
Cdd:COG2226    23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSFDLVISSFVLHHLP 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1569545716 137 DPQSVVHACARLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:COG2226   102 DPERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-153 6.47e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 91.86  E-value: 6.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  60 VLDVGCGGGILAESMARE-GATVTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVPDP 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1569545716 139 Q--SVVHACARLVKPGG 153
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-157 9.02e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 91.19  E-value: 9.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  61 LDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALESGiqVDYVQETVEEHAAKhPQQYDVVTCMEMLEHVPDPQS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 1569545716 141 VVHACARLVKPGGQVFF 157
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-170 1.86e-22

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 89.79  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLDmgaeplqvARLHALESGIQVDYVQETVEEHAAKHPQQYDVVTCMEMLEHVP 136
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVD--------PSPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1569545716 137 DPQSVVHACARLVKPGGQVFFSTINRNGKAWLMA 170
Cdd:pfam13489  95 DPPALLRQIAALLKPGGLLLLSTPLASDEADRLL 128
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 57-159 5.97e-20

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 83.06  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGAEPLQVARLHALESGI--QVDYVQETVEEHAAkhPQQYDVVTCMEMLE 133
Cdd:COG2230    52 GMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLadRVEVRLADYRDLPA--DGQFDAIVSIGMFE 129

                          90       100
                  ....*....|....*....|....*...
gi 1569545716 134 HVPDPQ--SVVHACARLVKPGGQVFFST 159
Cdd:COG2230   130 HVGPENypAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
48-159 1.40e-18

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 80.04  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  48 IAERSGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARlhalESGIQVDYVQETVEEhAAKHPQQYDVVT 127
Cdd:COG4976    38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLAD-LAEPDGRFDLIV 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1569545716 128 CMEMLEHVPDPQSVVHACARLVKPGGQVFFST 159
Cdd:COG4976   113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-159 1.05e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGAEPLQVARlhalESGIQVDYVQETVEEHAAkhPQQYDVVTCMEMLEH 134
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR----ARLPNVRFVVADLRDLDP--PEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1569545716 135 VPDPQSVVHACARLVKPGGQVFFST 159
Cdd:COG4106    76 LPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-158 1.01e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 75.72  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMA-REGATVTGLDMGAEPLQVARLHALESGI-QVDYVQETVEEHAAKHPQQYDVVTCMEMLEH 134
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLgNVEFLVADLAELDPLPAESFDLVVAFGVLHH 106

                          90       100
                  ....*....|....*....|....*.
gi 1569545716 135 VP--DPQSVVHACARLVKPGGQVFFS 158
Cdd:COG0500   107 LPpeEREALLRELARALKPGGVLLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-161 8.44e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 69.37  E-value: 8.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVEE-HAAKHPQQYDVVTCMEM 131
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEElPELLEDDKFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1569545716 132 LEHVPDPQSVVHACARLVKPGGQVFFSTIN 161
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-153 8.52e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 67.78  E-value: 8.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  61 LDVGCGGGILAESMARE--GATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVEEHAAKHPQQYDVVTCMEMLEHVPD 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLnAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*.
gi 1569545716 138 PQSVVHACARLVKPGG 153
Cdd:pfam08242  81 PRAVLRNIRRLLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 57-155 1.13e-14

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 70.74  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGAEPLQVARLHALESGIQVDYVQeTVEEHAAKHPQQYDVVTCMEMLE 133
Cdd:PRK08317   20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVR-GDADGLPFPDGSFDAVRSDRVLQ 98

                          90       100
                  ....*....|....*....|..
gi 1569545716 134 HVPDPQSVVHACARLVKPGGQV 155
Cdd:PRK08317   99 HLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 4.28e-14

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: 66.30  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVEEHAAKHPQQYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1569545716 136 PDPQSVVHACARLVKPGGQVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PLN02244 PLN02244
tocopherol O-methyltransferase
 58-159 5.34e-13

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 67.08  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  58 KKVLDVGCGGGILAESMARE-GATVTGLDMgaEPLQVARLHAL--ESGIqVDYVQETVEEhAAKHP---QQYDVVTCMEM 131
Cdd:PLN02244  120 KRIVDVGCGIGGSSRYLARKyGANVKGITL--SPVQAARANALaaAQGL-SDKVSFQVAD-ALNQPfedGQFDLVWSMES 195

                          90       100
                  ....*....|....*....|....*...
gi 1569545716 132 LEHVPDPQSVVHACARLVKPGGQVFFST 159
Cdd:PLN02244  196 GEHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
60-203 4.90e-11

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 60.75  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  60 VLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALESGI--QVDYVQETVEEHAAKHPQQYDVVTCMEMLEHVPD 137
Cdd:PRK11036   48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVsdNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVAD 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1569545716 138 PQSVVHACARLVKPGGQVFFSTINRNGKAWLMAVVGA-EYVMKMVPKGthdvKKF-------IKPAELLGWVDQ 203
Cdd:PRK11036  128 PKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKR----KKRtlspdypLDPEQVYQWLEE 197
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
20-155 1.06e-09

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 56.68  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  20 FEAVASRWwDLEGEFKPLhRINPLRLGYIAERSGGLFGKKVLDVGCGGGILAESM---AREGATVTGLDMGAEPLQVARL 96
Cdd:pfam01209   8 FSSVASKY-DLMNDVISF-GIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLsdsAGSSGKVVGLDINENMLKEGEK 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  97 HALESG-IQVDYVQETVEEhAAKHPQQYDVVTCMEMLEHVPDPQSVVHACARLVKPGGQV 155
Cdd:pfam01209  86 KAKEEGkYNIEFLQGNAEE-LPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
PRK06202 PRK06202
hypothetical protein; Provisional
 60-201 4.08e-09

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 55.01  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  60 VLDVGCGGGILAESMAREGA------TVTGLDMGAEPLQVARLHALESGIQVDYV--QETVEEhaakhPQQYDVVTCMEM 131
Cdd:PRK06202   64 LLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARANPRRPGVTFRQAvsDELVAE-----GERFDVVTSNHF 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716 132 LEHVPDPQ--SVVHACARLVKpgGQVFFSTINRNGKAWLMAVVGAEYVMK---MVPKGTHDVKKFIKPAELL-----GWV 201
Cdd:PRK06202  139 LHHLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYALFWAGTRLLSRssfVHTDGLLSVRRSYTPAELAalapqGWR 216
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 58-160 4.94e-09

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: 54.99  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  58 KKVLDVGCGGGILAESMAREG--ATVTGLDMGAEPLQVARLHaleSGIQVDYVQETVEeHAAKHPQQYDVVTCMEMLEHV 135
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTK---LSENVQFICGDAE-KLPLEDSSFDLIVSNLALQWC 111

                          90       100
                  ....*....|....*....|....*
gi 1569545716 136 PDPQSVVHACARLVKPGGQVFFSTI 160
Cdd:TIGR02072 112 DDLSQALSELARVLKPGGLLAFSTF 136
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 52-148 8.46e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.07  E-value: 8.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  52 SGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALESGI--QVDYVQETVEEHAAkhpqQYDVVTCM 129
Cdd:PRK07580   59 DGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLagNITFEVGDLESLLG----RFDTVVCL 134

                          90
                  ....*....|....*....
gi 1569545716 130 EMLEHVPDPQsVVHACARL 148
Cdd:PRK07580  135 DVLIHYPQED-AARMLAHL 152
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-183 9.89e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.00  E-value: 9.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  50 ERSGGLFGKKVLDVGCGGGILAESMAREG---ATVTGLDMGAEPLQVA--RLHALESGIQVDYVQETVEEhaakHP---Q 121
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGreKLRDLGLSGNVEFVQGDAEA----LPfpdN 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1569545716 122 QYDVVTcmeM---LEHVPDPQSVVHACARLVKPGGQVF---FSTINRNGkawlMAVVGAEYVMKMVPK 183
Cdd:PRK00216  121 SFDAVT---IafgLRNVPDIDKALREMYRVLKPGGRLVileFSKPTNPP----LKKAYDFYLFKVLPL 181
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-126 5.80e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.44  E-value: 5.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  47 YIAERSGGLFGKKVLDVGCGGGILAESMAREGAT-VTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAkhPQQYDV 125
Cdd:COG2263    36 HLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPL--GGSVDT 113


                  .
gi 1569545716 126 V 126
Cdd:COG2263   114 V 114
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 47-162 1.00e-07

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: 51.04  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  47 YIAERSGgLFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAKHpqQYDV 125
Cdd:COG3897    62 YLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAG--GFDL 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1569545716 126 VTC------MEMLEHvpdpqsVVHACARLVKPGGQVFFSTINR 162
Cdd:COG3897   139 ILGgdvlyeRDLAEP------LLPFLDRLAAPGGEVLIGDPGR 175
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 57-157 1.60e-07

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: 50.53  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAR--EGATVTGLDMGAEPLQVARLHALESGI--QVDYVQETVEEHAAK-HPQQYDVVTC--- 128
Cdd:COG4123    38 GGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNGLedRITVIHGDLKEFAAElPPGSFDLVVSnpp 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1569545716 129 -MEMLEHV--PDPQ-------------SVVHACARLVKPGGQVFF 157
Cdd:COG4123   118 yFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 45-137 1.78e-07

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 51.01  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  45 LGYIAErSGGLFGKKVLDVGCGGGILAESMAREGATVTGLD----MGAEPLQVAR--LHALESGIQVDYVQETVEEHAAK 118
Cdd:PLN02585  134 LLWLAE-DGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDisaaMVAEAERRAKeaLAALPPEVLPKFEANDLESLSGK 212

                          90
                  ....*....|....*....
gi 1569545716 119 hpqqYDVVTCMEMLEHVPD 137
Cdd:PLN02585  213 ----YDTVTCLDVLIHYPQ 227
PRK14967 PRK14967
putative methyltransferase; Provisional
 48-128 8.40e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 8.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  48 IAERSGGLFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGAEPLQVARLHALESGIQVDYVQETVEEHAAKHPqqYDVV 126
Cdd:PRK14967   28 ALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRP--FDVV 105


                  ..
gi 1569545716 127 TC 128
Cdd:PRK14967  106 VS 107
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-160 9.38e-07

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: 48.80  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGAEPLQVARLHAL----ESGIQVDYVQETVEEhaakhpqQYDVVTC--- 128
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAElngvEARLEVYLPGDLPKE-------KADVVVAnil 234

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1569545716 129 ----MEMLEHVpdpqsvvhacARLVKPGGQVFFSTI 160
Cdd:pfam06325 235 adplIELAPDI----------YALVKPGGYLILSGI 260
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 57-160 1.50e-06

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: 47.91  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGA-TVTGLDMGAEPLQVARLHALESGIQvDYVQETVEEHAAKHPQQYDVVTCMEMLEHV 135
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAaKVVGIDIDPLAVESARKNAELNQVS-DRLQVKLIYLEQPIEGKADVIVANILAEVI 238

                          90       100
                  ....*....|....*....|....*..
gi 1569545716 136 PD--PQSVvhacaRLVKPGGQVFFSTI 160
Cdd:TIGR00406 239 KElyPQFS-----RLVKPGGWLILSGI 260
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
57-160 1.78e-06

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 47.45  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGAEPLQVARLHALESGIQVDyvqetveEHAAKHPQQYDVVTC------- 128
Cdd:PRK00517  120 GKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAARENAELNGVELN-------VYLPQGDLKADVIVAnilanpl 192

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1569545716 129 MEMLEHVpdpqsvvhacARLVKPGGQVFFSTI 160
Cdd:PRK00517  193 LELAPDL----------ARLLKPGGRLILSGI 214
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
57-158 2.53e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 47.48  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGAEPLQVARLHALESGIQvDYVqeTVEEHAAKHPQQYDVVTC------- 128
Cdd:COG2264   149 GKTVLDVGCGSGILAIAAAKLGAKrVLAVDIDPVAVEAARENAELNGVE-DRI--EVVLGDLLEDGPYDLVVAnilanpl 225

                          90       100       110
                  ....*....|....*....|....*....|
gi 1569545716 129 MEMLEHVpdpqsvvhacARLVKPGGQVFFS 158
Cdd:COG2264   226 IELAPDL----------AALLKPGGYLILS 245
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 57-160 1.30e-05

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: 45.01  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCG-GGILAESMAREGATVTGLDMGAEPLQVA--RLHALESGIQV-----DYVQetveehaakHPQQYDVVTC 128
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLArkRVAAEGLARKVevllqDYRD---------FDEPFDRIVS 132

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1569545716 129 MEMLEHV-----PDPQSVVHacaRLVKPGGQVFFSTI 160
Cdd:pfam02353 133 VGMFEHVghenyDTFFKKLY---NLLPPGGLMLLHTI 166
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
57-156 1.91e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.26  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMGAEPLQVARLHALESGIQvDYVqETVEEHAAKH--PQQYDVVTCmEMLE 133
Cdd:COG4076    36 GDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRIIAANGLS-DRI-TVINADATDLdlPEKADVIIS-EMLD 112

                          90       100
                  ....*....|....*....|....*..
gi 1569545716 134 HV-PDPQSV---VHACARLVKPGGQVF 156
Cdd:COG4076   113 TAlLDEGQVpilNHARKRLLKPGGRII 139
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
57-163 3.72e-05

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 44.07  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGAEPLQVA--RLHALESGIQV-DYVQETveehaakhpQQYDVVTCMEML 132
Cdd:PRK11705  168 GMRVLDIGCGWGGLARYAAEHyGVSVVGVTISAEQQKLAqeRCAGLPVEIRLqDYRDLN---------GQFDRIVSVGMF 238

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1569545716 133 EHVpDPQ------SVVHacaRLVKPGGQVFFSTINRN 163
Cdd:PRK11705  239 EHV-GPKnyrtyfEVVR---RCLKPDGLFLLHTIGSN 271
PRK14968 PRK14968
putative methyltransferase; Provisional
 57-85 4.45e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 4.45e-05
                          10        20
                  ....*....|....*....|....*....
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLD 85
Cdd:PRK14968   24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVD 52
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 57-105 5.79e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.21  E-value: 5.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1569545716  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGAEPLQVAR----LHALESGIQV 105
Cdd:COG2890   113 PPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARrnaeRLGLEDRVRF 167
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 57-157 5.99e-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: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGG----ILAesMAREGATVTGLDmgaePL--------QVARLHALEsGIQVdyVQETVEEHAAKhpQQYD 124
Cdd:COG0357    68 GARVLDVGSGAGfpgiPLA--IARPDLQVTLVD----SLgkkiaflrEVVRELGLK-NVTV--VHGRAEELAPR--EKFD 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1569545716 125 VVTC-----MEMLehvpdpqsvVHACARLVKPGGQVFF 157
Cdd:COG0357   137 VVTAravapLPDL---------LELALPLLKPGGRLLA 165
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
55-210 7.48e-05

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.92  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  55 LFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGaePLQVARLHALE----SGIQVDYVQETVEEHAAkhPQQYDVVTCM 129
Cdd:PRK15068  121 LKGRTVLDVGCGNGYHMWRMLGAGAkLVVGIDPS--QLFLCQFEAVRkllgNDQRAHLLPLGIEQLPA--LKAFDTVFSM 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716 130 EMLEHVPDPQSVVHACARLVKPGGQVFFSTInrngkawlmaVVGAEYVMKMVPKGT----HDVkKFIkP--AELLGW--- 200
Cdd:PRK15068  197 GVLYHRRSPLDHLKQLKDQLVPGGELVLETL----------VIDGDENTVLVPGDRyakmRNV-YFI-PsvPALKNWler 264

                         170       180
                  ....*....|....*....|
gi 1569545716 201 ----------VDQTTLKEQH 210
Cdd:PRK15068  265 agfkdvrivdVSVTTTEEQR 284
arsM PRK11873
arsenite methyltransferase;
41-177 9.58e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 42.63  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  41 NPLRLGYIAErsgglfGKKVLDVGCGGGI---LAesmARE-GAT--VTGLDMGAEPLQVARLHALESGIQ-VDYVQETVE 113
Cdd:PRK11873   68 NPTALAELKP------GETVLDLGSGGGFdcfLA---ARRvGPTgkVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716 114 E-----HAAkhpqqyDVV--TCMEMLehVPDPQSVVHACARLVKPGGQVFFS----------TINRNGKAWLMAVVGAEY 176
Cdd:PRK11873  139 AlpvadNSV------DVIisNCVINL--SPDKERVFKEAFRVLKPGGRFAISdvvlrgelpeEIRNDAELYAGCVAGALQ 210


                  .
gi 1569545716 177 V 177
Cdd:PRK11873  211 E 211
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 60-160 1.06e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 42.44  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  60 VLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARlhalesgiqvdyvqetvEEHAAKHPQQYDVvtcmemlEHVPDPQ 139
Cdd:PRK10258   46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR-----------------QKDAADHYLAGDI-------ESLPLAT 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1569545716 140 SV---------VHACA----------RLVKPGGQVFFSTI 160
Cdd:PRK10258  102 ATfdlawsnlaVQWCGnlstalrelyRVVRPGGVVAFTTL 141
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-128 3.12e-04

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: 40.27  E-value: 3.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1569545716  56 FGKKVLDVGCGGGILAESMAREG--ATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVeeHAAKHPQQYDVVTC 128
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLEnGEVVASDV--YSGVEDGKFDLIIS 104
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 57-95 6.00e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 6.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1569545716  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGAEPLQVAR 95
Cdd:PRK09328  109 PLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVAR 149
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 40-155 1.02e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. 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 includes various 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.48  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  40 INPLRLGYIAERSGGLF-GKKVLDVGCGG-GILAESMAR-EGATVTGLDMGAEPLQVARLHALESGIQV--DYVQETVEE 114
Cdd:cd08261   142 VEPLAIGAHAVRRAGVTaGDTVLVVGAGPiGLGVIQVAKaRGARVIVVDIDDERLEFARELGADDTINVgdEDVAARLRE 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1569545716 115 HAAKHPqqYDVV---TCMemlehvpdPQSVVHACaRLVKPGGQV 155
Cdd:cd08261   222 LTDGEG--ADVVidaTGN--------PASMEEAV-ELVAHGGRV 254
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 57-191 1.46e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.35  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGAEPLQVARLHALESGIQVDYvqETVEEHAAKHPQQ-YDVVTCMEMLEH 134
Cdd:PLN02336  267 GQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEF--EVADCTKKTYPDNsFDVIYSRDTILH 344

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1569545716 135 VPDPQSVVHACARLVKPGGQVFFSTINRNGKAwlmavVGAEYVMKMVPKG--THDVKKF 191
Cdd:PLN02336  345 IQDKPALFRSFFKWLKPGGKVLISDYCRSPGT-----PSPEFAEYIKQRGydLHDVQAY 398
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 57-173 1.63e-03

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: 38.25  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGILAESMARE--GATVTGLDMGAEPLQVARLHALESGIQ-VDYVQETVEEHAAkhPQQYDVVTC----- 128
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLEnVEVLWSDGLSGVP--DGSFDLILSnppfh 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1569545716 129 ----------MEMLEhvpdpqsvvHACARLvKPGGQVFFsTINRNG--KAWLMAVVG 173
Cdd:COG2813   128 agravdkevaHALIA---------DAARHL-RPGGELWL-VANRHLpyERKLEELFG 173
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 51-136 2.30e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.13  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  51 RSGGLFGKKVLDVGCGGGILAESMARE--GATVTGLDMGAEPLQVARlhalESGiqVDYVQETVEEHAAKHPqqYDVVTC 128
Cdd:PRK14103   24 RVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR----ERG--VDARTGDVRDWKPKPD--TDVVVS 95


                  ....*...
gi 1569545716 129 MEMLEHVP 136
Cdd:PRK14103   96 NAALQWVP 103
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 49-155 2.67e-03

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: 38.37  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  49 AERSGGLFGKKVLDVGCGG-GILAESMAREG--ATVTGLDMGAEPLQVARlhALESGIQVDyVQETVEEHAAKHPQQYDV 125
Cdd:cd08232   158 VNRAGDLAGKRVLVTGAGPiGALVVAAARRAgaAEIVATDLADAPLAVAR--AMGADETVN-LARDPLAAYAADKGDFDV 234

                          90       100       110
                  ....*....|....*....|....*....|
gi 1569545716 126 VtcmemLEHVPDPQSvVHACARLVKPGGQV 155
Cdd:cd08232   235 V-----FEASGAPAA-LASALRVVRPGGTV 258
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 57-174 3.98e-03

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: 37.58  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCGGGI--LAESMAR-EGATVTG------LDMgaeplqVARLHALESgiqVDYVQETVEEHAAKHpQQYDVVt 127
Cdd:cd08267   144 GQRVLINGASGGVgtFAVQIAKaLGAHVTGvcstrnAEL------VRSLGADEV---IDYTTEDFVALTAGG-EKYDVI- 212

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1569545716 128 cmemLEHVPDPQSVVHACARLVKPGGQvfFSTINRNGKAWLMAVVGA 174
Cdd:cd08267   213 ----FDAVGNSPFSLYRASLALKPGGR--YVSVGGGPSGLLLVLLLL 253
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 57-126 7.29e-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: 37.08  E-value: 7.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1569545716  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGAEPLQVARLHALESGI-QVDYVQETVEEHAAKHP--QQYDVV 126
Cdd:COG2265   234 GERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLkNVEFVAGDLEEVLPELLwgGRPDVV 306
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
58-166 7.64e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 36.63  E-value: 7.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716   58 KKVLDVGCGGGILAESMAREGA--TVTGLDMGAEPLQVARLHALESGiqvdyVQETVEEHAAK-----HPQQYDVVTCME 130
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALG-----LQGRIRIFYRDsakdpFPDTYDLVFGFE 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1569545716  131 MLEHVPDPQSVVHACARLVKPGGQVFFSTINRNGKA 166
Cdd:smart00828  76 VIHHIKDKMDLFSNISRHLKDGGHLVLADFIANLLS 111
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 57-155 8.60e-03

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: 36.03  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569545716  57 GKKVLDVGCG-GG---ILAEsmaREGATVTGLDMGAEPLQVARLHALESGIQVD----YVQETVEEHaakHPQQYDVVTC 128
Cdd:pfam01728  22 GKTVLDLGAApGGwsqVALQ---RGAGKVVGVDLGPMQLWKPRNDPGVTFIQGDirdpETLDLLEEL---LGRKVDLVLS 95

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1569545716 129 -----MEMLEHVPDPQSV------VHACARLVKPGGQV 155
Cdd:pfam01728  96 dgspfISGNKVLDHLRSLdlvkaaLEVALELLRKGGNF 133
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 57-126 9.95e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 36.09  E-value: 9.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1569545716  57 GKKVLDVGCGGGI---LAESMAREGATVTGLDMGAEPLQVARLHAlesgIQVDYVQETveEHAAKHPQQYDVV 126
Cdd:PRK06550    5 TKTVLITGAASGIglaQARAFLAQGAQVYGVDKQDKPDLSGNFHF----LQLDLSDDL--EPLFDWVPSVDIL 71
 
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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