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Conserved domains on  [gi|1487550534|gb|AYG18744|]
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bifunctional 3-demethylubiquinone 3-O-methyltransferase/2-octaprenyl-6-hydroxy phenol methylase [Escherichia coli str. K-12 substr. MG1655]

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 1.25e-139

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: 390.50  E-value: 1.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  91 LQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487550534 171 VVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYM 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 1.25e-139

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: 390.50  E-value: 1.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  91 LQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487550534 171 VVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 11-234 5.92e-61

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 194.18  E-value: 5.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  11 NVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGK-----------KVLDVGCGGGILAESMAREGA 79
Cdd:PLN02396   75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  80 TVTGLDMGFEPLQVAKLHAlesgiQVDYVQETVE------EHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGG 153
Cdd:PLN02396  155 TVTGVDAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534 154 DVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNY 233
Cdd:PLN02396  230 ATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNY 309


                  .
gi 1487550534 234 M 234
Cdd:PLN02396  310 I 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 24-161 4.25e-39

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: 131.68  E-value: 4.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  24 ASRWWDLEgefkpLHRinplrlgYIAERAGGlfGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALEsgI 103
Cdd:COG2227     6 ARDFWDRR-----LAA-------LLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--L 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487550534 104 QVDYVQETVEEHAAKHaGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLN 161
Cdd:COG2227    70 NVDFVQGDLEDLPLED-GSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-186 6.41e-24

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 93.65  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALEsgiqvdyvQETVEEHAAKHAGQYDVVTCMEMLEHVP 136
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF--------DQFDEQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1487550534 137 DPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMavvgAEYILRMVPKGTH 186
Cdd:pfam13489  95 DPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 2.26e-12

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: 61.68  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGFEPLQVAKLHALESGIQ-VDYVQETVEEHAAKHAGQYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1487550534 136 PDPQSVVRACAQLVKPGGDVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 16-234 1.25e-139

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: 390.50  E-value: 1.25e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  16 EIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGG-----LFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  91 LQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487550534 171 VVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 11-234 5.92e-61

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 194.18  E-value: 5.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  11 NVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGK-----------KVLDVGCGGGILAESMAREGA 79
Cdd:PLN02396   75 SLNEDELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  80 TVTGLDMGFEPLQVAKLHAlesgiQVDYVQETVE------EHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGG 153
Cdd:PLN02396  155 TVTGVDAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534 154 DVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNY 233
Cdd:PLN02396  230 ATVLSTINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNY 309


                  .
gi 1487550534 234 M 234
Cdd:PLN02396  310 I 310
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 24-161 4.25e-39

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: 131.68  E-value: 4.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  24 ASRWWDLEgefkpLHRinplrlgYIAERAGGlfGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALEsgI 103
Cdd:COG2227     6 ARDFWDRR-----LAA-------LLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--L 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487550534 104 QVDYVQETVEEHAAKHaGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLN 161
Cdd:COG2227    70 NVDFVQGDLEDLPLED-GSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 48-162 4.67e-25

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: 96.22  E-value: 4.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  48 IAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKhAGQYDVVT 127
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1487550534 128 CMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNR 162
Cdd:COG2226    93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-186 6.41e-24

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 93.65  E-value: 6.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALEsgiqvdyvQETVEEHAAKHAGQYDVVTCMEMLEHVP 136
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF--------DQFDEQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1487550534 137 DPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMavvgAEYILRMVPKGTH 186
Cdd:pfam13489  95 DPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-157 4.59e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 89.26  E-value: 4.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  61 LDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGiqVDYVQETVEEHAAKhAGQYDVVTCMEMLEHVPDPQS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 1487550534 141 VVRACAQLVKPGGDVFF 157
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-153 1.83e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 88.00  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  60 VLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKhAGQYDVVTCMEMLEHVPDP 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1487550534 139 Q--SVVRACAQLVKPGG 153
Cdd:pfam13649  80 DleAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-153 5.18e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 80.74  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  47 YIAERAGGLFGKKVLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVAKLHALESGI--QVDYVQETVEEHAAKhaGQY 123
Cdd:COG2230    42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLadRVEVRLADYRDLPAD--GQF 119

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1487550534 124 DVVTCMEMLEHVPDPQ--SVVRACAQLVKPGG 153
Cdd:COG2230   120 DAIVSIGMFEHVGPENypAYFAKVARLLKPGG 151
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
48-159 2.05e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 76.96  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  48 IAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKlhalESGIQVDYVQETVEEhAAKHAGQYDVVT 127
Cdd:COG4976    38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLAD-LAEPDGRFDLIV 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1487550534 128 CMEMLEHVPDPQSVVRACAQLVKPGGDVFFST 159
Cdd:COG4976   113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-159 4.22e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 4.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMARE--GATVTGLDmgFEPLQVAKlhALESGIQVDYVQETVEEHAAkhAGQYDVVTCMEMLEH 134
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERfpGARVTGVD--LSPEMLAR--ARARLPNVRFVVADLRDLDP--PEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1487550534 135 VPDPQSVVRACAQLVKPGGDVFFST 159
Cdd:COG4106    76 LPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-158 8.77e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.33  E-value: 8.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMA-REGATVTGLDMGFEPLQVAKLHALESGI-QVDYVQETVEEHAAKHAGQYDVVTCMEMLEH 134
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLgNVEFLVADLAELDPLPAESFDLVVAFGVLHH 106

                          90       100
                  ....*....|....*....|....*.
gi 1487550534 135 VP--DPQSVVRACAQLVKPGGDVFFS 158
Cdd:COG0500   107 LPpeEREALLRELARALKPGGVLLLS 132
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-153 4.42e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 63.16  E-value: 4.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  61 LDVGCGGGILAESMARE--GATVTGLDMGFEPLQVAKLHALESGIQ-VDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPD 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLnAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*.
gi 1487550534 138 PQSVVRACAQLVKPGG 153
Cdd:pfam08242  81 PRAVLRNIRRLLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-153 1.39e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 63.20  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGFEPLQVAKLHALESGIQ-VDYVQETVEE-HAAKHAGQYDVVTCMEM 131
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEElPELLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|..
gi 1487550534 132 LEHVPDPQSVVRACAQLVKPGG 153
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGG 105
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 2.26e-12

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: 61.68  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  59 KVLDVGCGGGILAESMAR-EGATVTGLDMGFEPLQVAKLHALESGIQ-VDYVQETVEEHAAKHAGQYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1487550534 136 PDPQSVVRACAQLVKPGGDVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 57-153 6.17e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.03  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMARE---GATVTGLDMGFEPLQVAKLHALESGIQVDYVQeTVEEHAAKHAGQYDVVTCMEMLE 133
Cdd:PRK08317   20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVR-GDADGLPFPDGSFDAVRSDRVLQ 98

                          90       100
                  ....*....|....*....|
gi 1487550534 134 HVPDPQSVVRACAQLVKPGG 153
Cdd:PRK08317   99 HLEDPARALAEIARVLRPGG 118
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
60-213 1.51e-11

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 62.29  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  60 VLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGI--QVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPD 137
Cdd:PRK11036   48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVsdNMQFIHCAAQDIAQHLETPVDLILFHAVLEWVAD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534 138 PQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGA-EYILRMVPKGthdvKKF-------IKPAELLGWVDQTSLKER 209
Cdd:PRK11036  128 PKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKR----KKRtlspdypLDPEQVYQWLEEAGWQIM 203


                  ....
gi 1487550534 210 HITG 213
Cdd:PRK11036  204 GKTG 207
PLN02244 PLN02244
tocopherol O-methyltransferase
 58-159 1.89e-10

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 59.76  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  58 KKVLDVGCGGGILAESMARE-GATVTGLDMgfEPLQVAKLHAL--ESGI------QV-DYVQETVEEhaakhaGQYDVVT 127
Cdd:PLN02244  120 KRIVDVGCGIGGSSRYLARKyGANVKGITL--SPVQAARANALaaAQGLsdkvsfQVaDALNQPFED------GQFDLVW 191

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1487550534 128 CMEMLEHVPDPQSVVRACAQLVKPGGDVFFST 159
Cdd:PLN02244  192 SMESGEHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 57-148 4.45e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGI--QVDYVQETVEEhaakHAGQYDVVTCMEMLEH 134
Cdd:PRK07580   64 GLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLagNITFEVGDLES----LLGRFDTVVCLDVLIH 139

                          90
                  ....*....|....
gi 1487550534 135 VPDPQsVVRACAQL 148
Cdd:PRK07580  140 YPQED-AARMLAHL 152
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 58-160 1.48e-08

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: 53.44  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  58 KKVLDVGCGGGILAESMAREG--ATVTGLDMGFEPLQVAKLHaleSGIQVDYVQETVEEHA-AKHagQYDVVTCMEMLEH 134
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPlEDS--SFDLIVSNLALQW 110

                          90       100
                  ....*....|....*....|....*.
gi 1487550534 135 VPDPQSVVRACAQLVKPGGDVFFSTL 160
Cdd:TIGR02072 111 CDDLSQALSELARVLKPGGLLAFSTF 136
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
20-155 2.99e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 52.44  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  20 FEAVASRWwDLEGEFKPLhRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESM---AREGATVTGLDMGFEPLQVAKL 96
Cdd:pfam01209   8 FSSVASKY-DLMNDVISF-GIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLsdsAGSSGKVVGLDINENMLKEGEK 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  97 HALESG-IQVDYVQETVEEhAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDV 155
Cdd:pfam01209  86 KAKEEGkYNIEFLQGNAEE-LPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
47-126 7.23e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.06  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  47 YIAERAGGLFGKKVLDVGCGGGILAESMAREGAT-VTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAkhAGQYDV 125
Cdd:COG2263    36 HLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPL--GGSVDT 113


                  .
gi 1487550534 126 V 126
Cdd:COG2263   114 V 114
PRK06202 PRK06202
hypothetical protein; Provisional
 43-210 5.31e-07

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 48.84  E-value: 5.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  43 LRLGYIAERAgglfgKKVLDVGCGGGILAESMAREGA------TVTGLDMGFEPLQVAKLHALESGIQVDYV--QETVEE 114
Cdd:PRK06202   52 LRPALSADRP-----LTLLDIGCGGGDLAIDLARWARrdglrlEVTAIDPDPRAVAFARANPRRPGVTFRQAvsDELVAE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534 115 HAakhagQYDVVTCMEMLEHVPDPQ--SVVRACAQLVKpgGDVFFSTLNRNGKSWLMAVVGAEYILR---MVPKGTHDVK 189
Cdd:PRK06202  127 GE-----RFDVVTSNHFLHHLDDAEvvRLLADSAALAR--RLVLHNDLIRSRLAYALFWAGTRLLSRssfVHTDGLLSVR 199

                         170       180
                  ....*....|....*....|....*.
gi 1487550534 190 KFIKPAELL-----GWVDQTSLKERH 210
Cdd:PRK06202  200 RSYTPAELAalapqGWRVERQWPFRY 225
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 45-137 9.22e-07

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 48.70  E-value: 9.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  45 LGYIAERaGGLFGKKVLDVGCGGGILAESMAREGATVTGLD----MGFEPLQVAK--LHALESGIQVDYVQETVEEhaak 118
Cdd:PLN02585  134 LLWLAED-GSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDisaaMVAEAERRAKeaLAALPPEVLPKFEANDLES---- 208

                          90
                  ....*....|....*....
gi 1487550534 119 HAGQYDVVTCMEMLEHVPD 137
Cdd:PLN02585  209 LSGKYDTVTCLDVLIHYPQ 227
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
55-160 9.37e-07

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 48.70  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  55 LFGKKVLDVGCGGGILAESMAREGA-TVTGLD------MGFEPLQvaklHALESGIQVDYVQETVEEHAAKHAgqYDVVT 127
Cdd:PRK15068  121 LKGRTVLDVGCGNGYHMWRMLGAGAkLVVGIDpsqlflCQFEAVR----KLLGNDQRAHLLPLGIEQLPALKA--FDTVF 194

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1487550534 128 CMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTL 160
Cdd:PRK15068  195 SMGVLYHRRSPLDHLKQLKDQLVPGGELVLETL 227
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 57-128 1.09e-06

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: 47.96  E-value: 1.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAkhAGQYDVVTC 128
Cdd:COG3897    71 GKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPA--AGGFDLILG 141
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 57-158 1.64e-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: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVAKLHALESGIQvDYVQETVEEHAAKHAGQYDVVTCMEMLEHV 135
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAaKVVGIDIDPLAVESARKNAELNQVS-DRLQVKLIYLEQPIEGKADVIVANILAEVI 238

                          90       100
                  ....*....|....*....|....*
gi 1487550534 136 PD--PQSVvracaQLVKPGGDVFFS 158
Cdd:TIGR00406 239 KElyPQFS-----RLVKPGGWLILS 258
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-158 2.87e-06

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: 47.26  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMgfEPLQV------AKLHALESGIQVDYVQETVEEhaakhagQYDVVTC- 128
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKkVVGVDI--DPVAVraakenAELNGVEARLEVYLPGDLPKE-------KADVVVAn 232

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1487550534 129 ------MEMLEHVpdpqsvvracAQLVKPGGDVFFS 158
Cdd:pfam06325 233 iladplIELAPDI----------YALVKPGGYLILS 258
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
57-158 8.26e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 45.55  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDmgFEPLQV------AKLHALESGIQVdyVQETVEEHaakhaGQYDVVTC- 128
Cdd:COG2264   149 GKTVLDVGCGSGILAIAAAKLGAKrVLAVD--IDPVAVeaarenAELNGVEDRIEV--VLGDLLED-----GPYDLVVAn 219

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1487550534 129 ------MEMLEHVpdpqsvvracAQLVKPGGDVFFS 158
Cdd:COG2264   220 ilanplIELAPDL----------AALLKPGGYLILS 245
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 57-157 1.10e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 45.14  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAR--EGATVTGLDmgfepLQV---------AKLHALESGIQV---DyVQETVEEHAakhAGQ 122
Cdd:COG4123    38 GGRVLDLGTGTGVIALMLAQrsPGARITGVE-----IQPeaaelarrnVALNGLEDRITVihgD-LKEFAAELP---PGS 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1487550534 123 YDVVTC----MEMLEHV--PDPQ-------------SVVRACAQLVKPGGDVFF 157
Cdd:COG4123   109 FDLVVSnppyFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
57-158 1.26e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 45.14  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGAT-VTGLDMgfEPL--QVAKLHALESGIQVDyvqetveEHAAKHAGQYDVVTC----- 128
Cdd:PRK00517  120 GKTVLDVGCGSGILAIAAAKLGAKkVLAVDI--DPQavEAARENAELNGVELN-------VYLPQGDLKADVIVAnilan 190

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1487550534 129 --MEMLEHVpdpqsvvracAQLVKPGGDVFFS 158
Cdd:PRK00517  191 plLELAPDL----------ARLLKPGGRLILS 212
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-153 2.21e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 44.37  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  50 ERAGGLFGKKVLDVGCGGGILAESMAREG---ATVTGLDMGFEPLQVA--KLHALESGIQVDYVQETVEE--HAAKHagq 122
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGreKLRDLGLSGNVEFVQGDAEAlpFPDNS--- 121

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1487550534 123 YDVVTcmeM---LEHVPDPQSVVRACAQLVKPGG 153
Cdd:PRK00216  122 FDAVT---IafgLRNVPDIDKALREMYRVLKPGG 152
PRK14967 PRK14967
putative methyltransferase; Provisional
 48-128 3.80e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 43.50  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  48 IAERAGGLFGKKVLDVGCGGGILAESMAREGA-TVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEhaAKHAGQYDVV 126
Cdd:PRK14967   28 ALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWAR--AVEFRPFDVV 105


                  ..
gi 1487550534 127 TC 128
Cdd:PRK14967  106 VS 107
PRK14968 PRK14968
putative methyltransferase; Provisional
 57-85 4.68e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 4.68e-05
                          10        20
                  ....*....|....*....|....*....
gi 1487550534  57 GKKVLDVGCGGGILAESMAREGATVTGLD 85
Cdd:PRK14968   24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVD 52
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-128 3.48e-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: 39.88  E-value: 3.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1487550534  56 FGKKVLDVGCGGGILAESMAREG--ATVTGLDMGFEPLQVAKLHALESGIQ-VDYVQETVeeHAAKHAGQYDVVTC 128
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLEnGEVVASDV--YSGVEDGKFDLIIS 104
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 50-128 5.14e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  50 ERAGGLFGKKVLDVGCGGGILAESMARE--GATVTGLDMGFEPLQVAK----LHALESGIQV---DYVQetveehAAKHA 120
Cdd:COG2890   106 ALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARrnaeRLGLEDRVRFlqgDLFE------PLPGD 179


                  ....*...
gi 1487550534 121 GQYDVVTC 128
Cdd:COG2890   180 GRFDLIVS 187
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 57-191 6.55e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGFEPLQVAKLHALESGIQVDY-VQETVEEHAAKHAgqYDVVTCMEMLEH 134
Cdd:PLN02336  267 GQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEFeVADCTKKTYPDNS--FDVIYSRDTILH 344

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487550534 135 VPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSwlmavVGAEYILRMVPKG--THDVKKF 191
Cdd:PLN02336  345 IQDKPALFRSFFKWLKPGGKVLISDYCRSPGT-----PSPEFAEYIKQRGydLHDVQAY 398
arsM PRK11873
arsenite methyltransferase;
41-158 8.44e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 39.55  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  41 NPLRLGYIAEragglfGKKVLDVGCGGGI---LAesmARE-GAT--VTGLDMGFEPLQVAKLHALESGIqvdyvqETVE- 113
Cdd:PRK11873   68 NPTALAELKP------GETVLDLGSGGGFdcfLA---ARRvGPTgkVIGVDMTPEMLAKARANARKAGY------TNVEf 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1487550534 114 -----EHAAKHAGQYDVV--TCMEMLehVPDPQSVVRACAQLVKPGGDVFFS 158
Cdd:PRK11873  133 rlgeiEALPVADNSVDVIisNCVINL--SPDKERVFKEAFRVLKPGGRFAIS 182
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 57-153 1.50e-03

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: 38.59  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGG----ILAesMAREGATVTGLDmgfePLQ---------VAKLHAleSGIQVdyVQETVEEHAAKhaGQY 123
Cdd:COG0357    68 GARVLDVGSGAGfpgiPLA--IARPDLQVTLVD----SLGkkiaflrevVRELGL--KNVTV--VHGRAEELAPR--EKF 135

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1487550534 124 DVVTC-----MEMLehvpdpqsvVRACAQLVKPGG 153
Cdd:COG0357   136 DVVTAravapLPDL---------LELALPLLKPGG 161
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 60-160 2.44e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 38.20  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  60 VLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKlhalESGIQVDYVQETVEehAAKHA-GQYDVVTCMEMLEHVPDP 138
Cdd:PRK10258   46 VLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR----QKDAADHYLAGDIE--SLPLAtATFDLAWSNLAVQWCGNL 119

                          90       100
                  ....*....|....*....|..
gi 1487550534 139 QSVVRACAQLVKPGGDVFFSTL 160
Cdd:PRK10258  120 STALRELYRVVRPGGVVAFTTL 141
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
57-135 2.45e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 38.68  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGILAESMARE-GATVTGLDMGFEplQVAKLHALESGIQV-----DYVQETveehaakhaGQYDVVTCME 130
Cdd:PRK11705  168 GMRVLDIGCGWGGLARYAAEHyGVSVVGVTISAE--QQKLAQERCAGLPVeirlqDYRDLN---------GQFDRIVSVG 236


                  ....*
gi 1487550534 131 MLEHV 135
Cdd:PRK11705  237 MFEHV 241
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 57-135 5.08e-03

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: 37.31  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCG-GGILAESMAREGATVTGLDMGFEplqvaklhalesgiQVDYVQETVEEHAAKH------------AGQY 123
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKN--------------QYKLARKRVAAEGLARkvevllqdyrdfDEPF 127

                          90
                  ....*....|..
gi 1487550534 124 DVVTCMEMLEHV 135
Cdd:pfam02353 128 DRIVSVGMFEHV 139
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 49-155 5.18e-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: 37.60  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  49 AERAGGLFGKKVLDVGCGG-GILAESMAREG--ATVTGLDMGFEPLQVAKlhALESGIQVDyVQETVEEHAAKHAGQYDV 125
Cdd:cd08232   158 VNRAGDLAGKRVLVTGAGPiGALVVAAARRAgaAEIVATDLADAPLAVAR--AMGADETVN-LARDPLAAYAADKGDFDV 234

                          90       100       110
                  ....*....|....*....|....*....|
gi 1487550534 126 VtcmemLEHVPDPQSvVRACAQLVKPGGDV 155
Cdd:cd08232   235 V-----FEASGAPAA-LASALRVVRPGGTV 258
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 51-153 5.86e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 36.98  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  51 RAGGLFGKKVLDVGCGGGILAESMARE--GATVTGLDMgfEPLQVAKlhALESGiqVDYVQETVEEHAAKHagQYDVVTC 128
Cdd:PRK14103   24 RVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDS--SPEMVAA--ARERG--VDARTGDVRDWKPKP--DTDVVVS 95

                          90       100
                  ....*....|....*....|....*
gi 1487550534 129 MEMLEHVPDPQSVVRACAQLVKPGG 153
Cdd:PRK14103   96 NAALQWVPEHADLLVRWVDELAPGS 120
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 55-160 5.93e-03

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: 37.38  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  55 LFGKKVLDVGCGGGILAESMAREGATVTgldMGFEPLQ--------VAKL-------HALESGIqvdyvqETVEEHAAkh 119
Cdd:pfam08003 114 LKGRTILDVGCGNGYHMWRMLGEGAAMV---VGIDPSElflcqfeaVRKLlgndqraHLLPLGI------EQLPALAA-- 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1487550534 120 agqYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTL 160
Cdd:pfam08003 183 ---FDTVFSMGVLYHRRSPLDHLLQLKDQLVKGGELVLETL 220
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 57-183 6.75e-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: 37.20  E-value: 6.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  57 GKKVLDVGCGGGI--LAESMAR-EGATVTG------LDMgfeplqVAKLHALESgiqVDYVQETVEEHAAKHaGQYDVVt 127
Cdd:cd08267   144 GQRVLINGASGGVgtFAVQIAKaLGAHVTGvcstrnAEL------VRSLGADEV---IDYTTEDFVALTAGG-EKYDVI- 212

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1487550534 128 cmemLEHVPDPQSVVRACAQLVKPGGdvFFSTLNRNGKSWLMAVVGAEYILRMVPK 183
Cdd:cd08267   213 ----FDAVGNSPFSLYRASLALKPGG--RYVSVGGGPSGLLLVLLLLPLTLGGGGR 262
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 57-126 8.94e-03

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 36.48  E-value: 8.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487550534  57 GKKVLDVGCGGGI---LAESMAREGATVTGLDMGFEPLQVAKLHAlesgIQVDYVQETveEHAAKHAGQYDVV 126
Cdd:PRK06550    5 TKTVLITGAASGIglaQARAFLAQGAQVYGVDKQDKPDLSGNFHF----LQLDLSDDL--EPLFDWVPSVDIL 71
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 40-153 9.27e-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: 36.78  E-value: 9.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  40 INPLRLGY-IAERAGGLFGKKVLDVGCGG-GILAESMAR-EGATVTGLDMGFEPLQVAKLHALESGIQV--DYVQETVEE 114
Cdd:cd08261   142 VEPLAIGAhAVRRAGVTAGDTVLVVGAGPiGLGVIQVAKaRGARVIVVDIDDERLEFARELGADDTINVgdEDVAARLRE 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1487550534 115 HAAkhAGQYDVV---TCMemlehvpdPQSVVRACaQLVKPGG 153
Cdd:cd08261   222 LTD--GEGADVVidaTGN--------PASMEEAV-ELVAHGG 252
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
8-139 9.86e-03

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 36.79  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534   8 VNHNVDHEEIAKFEAVASrwwdlegefkplhriNPLRLgY--------IAERAGG--LFGKkVLDVGCG----------- 66
Cdd:PRK09605  106 VNHCVAHVEIGRLTTGAE---------------DPVTL-YvsggntqvLAYLNGRyrVFGE-TLDIGVGnaldkfarhvg 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487550534  67 ----GGILAESMAREGA-------TVTGLDMGFEPLQVAKLHALESGIQVDYV----QET-------VEEHAAKHAGQYD 124
Cdd:PRK09605  169 lphpGGPKIEKLAKDGKkyidlpyVVKGMDFSFSGLLTAAKRAYDAGEPLEDVcyslQETafamlteVTERALAHTGKDE 248

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1487550534 125 VVTC---------MEMLE----------HVPDPQ 139
Cdd:PRK09605  249 VLLVggvaannrlREMLKemceergadfYVPEPR 282
 
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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