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Conserved domains on  [gi|1890641966|ref|WP_183169276|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Atlantibacter]

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 3.42e-133

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: 374.32  E-value: 3.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  16 EIAKFEAVASQWWDTEGEFKPLHRINPLRLGYITERAGG-----LFGKTVLDVGCGGGILSESMARQGAKVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  91 LQVARLHALESGVAVDYVQETVEEHAAAHPQKYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890641966 171 VVGAEYILRMVPKGTHDIKKFIKPAELLNWVDHTPLQERHMTGLHFNPLTNRFSLGPGVDVNYM 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 3.42e-133

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: 374.32  E-value: 3.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  16 EIAKFEAVASQWWDTEGEFKPLHRINPLRLGYITERAGG-----LFGKTVLDVGCGGGILSESMARQGAKVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  91 LQVARLHALESGVAVDYVQETVEEHAAAHPQKYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890641966 171 VVGAEYILRMVPKGTHDIKKFIKPAELLNWVDHTPLQERHMTGLHFNPLTNRFSLGPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 16-243 1.44e-65

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 206.12  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  16 EIAKFEAVASQWWDTEGEFKPLHRINPLRLGYITERAGGLFGK-----------TVLDVGCGGGILSESMARQGAKVTGL 84
Cdd:PLN02396   80 ELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGATVTGV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  85 DMGAEPLQVARLHAlesgvAVDYVQETVE------EHAAAHPQKYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHVFFS 158
Cdd:PLN02396  160 DAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLS 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966 159 TLNRNGKSWLMAVVGAEYILRMVPKGTHDIKKFIKPAELLNWVDHTPLQERHMTGLHFNPLTNRFSLGPGVDVNYMLHTQ 238
Cdd:PLN02396  235 TINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIAYGT 314


                  ....*
gi 1890641966 239 ARNQI 243
Cdd:PLN02396  315 KRKDL 319
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 6.70e-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: 133.99  E-value: 6.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALEsgVAVDYVQETVEEHAAAhPQKYDVVTCMEMLEHVP 136
Cdd:COG2227    25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|....*
gi 1890641966 137 DPASVVNACAQLVKPGGHVFFSTLN 161
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-186 1.14e-23

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 93.26  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDmgaeplqvaRLHALESGVAVDYVQETVEEHAAAHPQ-KYDVVTCMEMLEHV 135
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVD---------PSPIAIERALLNVRFDQFDEQEAAVPAgKFDVIVAREVLEHV 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890641966 136 PDPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMavvgAEYILRMVPKGTH 186
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 9.46e-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: 65.53  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  59 TVLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEHAAAHPQKYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1890641966 136 PDPASVVNACAQLVKPGGHVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
58-166 8.98e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966   58 KTVLDVGCGGGILSESMARQGA--KVTGLDMGAEPLQVARLHALESGVavdyvQETVEEHA-----AAHPQKYDVVTCME 130
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALGL-----QGRIRIFYrdsakDPFPDTYDLVFGFE 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1890641966  131 MLEHVPDPASVVNACAQLVKPGGHVFFSTLNRNGKS 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 3.42e-133

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: 374.32  E-value: 3.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  16 EIAKFEAVASQWWDTEGEFKPLHRINPLRLGYITERAGG-----LFGKTVLDVGCGGGILSESMARQGAKVTGLDMGAEP 90
Cdd:TIGR01983   1 EIAKFSALAHEWWDPNGKFKPLHKMNPLRLDYIRDRIRKnfknpLDGLRVLDVGCGGGLLSEPLARLGANVTGIDASEEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  91 LQVARLHALESGVAVDYVQETVEEHAAAHPQKYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMA 170
Cdd:TIGR01983  81 IEVAKLHAKKDPLQIDYRCTTVEDLAEKKAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTPKSYLLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890641966 171 VVGAEYILRMVPKGTHDIKKFIKPAELLNWVDHTPLQERHMTGLHFNPLTNRFSLGPGVDVNYM 234
Cdd:TIGR01983 161 IVGAEYILRIVPKGTHDWEKFIKPSELLSWLESAGLRVKDIKGLVYNPIKNTWKLSKDTDVNYM 224
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 16-243 1.44e-65

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 206.12  E-value: 1.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  16 EIAKFEAVASQWWDTEGEFKPLHRINPLRLGYITERAGGLFGK-----------TVLDVGCGGGILSESMARQGAKVTGL 84
Cdd:PLN02396   80 ELAKFSAIADTWWHSEGPFKPLHQMNPTRLAFIRSTLCRHFSKdpssakpfeglKFIDIGCGGGLLSEPLARMGATVTGV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  85 DMGAEPLQVARLHAlesgvAVDYVQETVE------EHAAAHPQKYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHVFFS 158
Cdd:PLN02396  160 DAVDKNVKIARLHA-----DMDPVTSTIEylcttaEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNGATVLS 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966 159 TLNRNGKSWLMAVVGAEYILRMVPKGTHDIKKFIKPAELLNWVDHTPLQERHMTGLHFNPLTNRFSLGPGVDVNYMLHTQ 238
Cdd:PLN02396  235 TINRTMRAYASTIVGAEYILRWLPKGTHQWSSFVTPEELSMILQRASVDVKEMAGFVYNPITGRWLLSDDISVNYIAYGT 314


                  ....*
gi 1890641966 239 ARNQI 243
Cdd:PLN02396  315 KRKDL 319
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-161 6.70e-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: 133.99  E-value: 6.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALEsgVAVDYVQETVEEHAAAhPQKYDVVTCMEMLEHVP 136
Cdd:COG2227    25 GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLE-DGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|....*
gi 1890641966 137 DPASVVNACAQLVKPGGHVFFSTLN 161
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 48-162 3.08e-26

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: 99.30  E-value: 3.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  48 ITERAGGLFGKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALESGVAVDYVQETVEEHAAAhPQKYDVVT 127
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFP-DGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1890641966 128 CMEMLEHVPDPASVVNACAQLVKPGGHVFFSTLNR 162
Cdd:COG2226    93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-186 1.14e-23

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 93.26  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDmgaeplqvaRLHALESGVAVDYVQETVEEHAAAHPQ-KYDVVTCMEMLEHV 135
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVD---------PSPIAIERALLNVRFDQFDEQEAAVPAgKFDVIVAREVLEHV 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890641966 136 PDPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMavvgAEYILRMVPKGTH 186
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLSTPLASDEADRL----LLEWPYLRPRNGH 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-157 6.02e-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: 6.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  61 LDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALESGvaVDYVQETVEEHAAAhPQKYDVVTCMEMLEHVPDPAS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFP-DNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 1890641966 141 VVNACAQLVKPGGHVFF 157
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-153 1.62e-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: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  60 VLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVAVDYVQETVEEHAAAhPQKYDVVTCMEMLEHVPDP 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 1890641966 139 --ASVVNACAQLVKPGG 153
Cdd:pfam13649  80 dlEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-159 2.15e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 81.90  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  47 YITERAGGLFGKTVLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVA--VDYVQETVEEHAAahPQKY 123
Cdd:COG2230    42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPA--DGQF 119

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1890641966 124 DVVTCMEMLEHVPDP--ASVVNACAQLVKPGGHVFFST 159
Cdd:COG2230   120 DAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
50-159 2.91e-19

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 81.97  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  50 ERAGGLFGKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARlhalESGVAVDYVQETVEEhAAAHPQKYDVVTCM 129
Cdd:COG4976    40 ARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLAD-LAEPDGRFDLIVAA 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1890641966 130 EMLEHVPDPASVVNACAQLVKPGGHVFFST 159
Cdd:COG4976   115 DVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-159 2.59e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.47  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQ--GAKVTGLDMGAEPLQVARlhalESGVAVDYVQETVEEHAAahPQKYDVVTCMEMLEH 134
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARAR----ARLPNVRFVVADLRDLDP--PEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1890641966 135 VPDPASVVNACAQLVKPGGHVFFST 159
Cdd:COG4106    76 LPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 57-158 1.13e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.03  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMA-RQGAKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEHAAAHPQKYDVVTCMEMLEH 134
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDPLPAESFDLVVAFGVLHH 106

                          90       100
                  ....*....|....*....|....*.
gi 1890641966 135 VP--DPASVVNACAQLVKPGGHVFFS 158
Cdd:COG0500   107 LPpeEREALLRELARALKPGGVLLLS 132
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-161 2.11e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 70.91  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMA---RQGAKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEHAAA-HPQKYDVVTCMEM 131
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAeelGPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPELlEDDKFDVVISNCV 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1890641966 132 LEHVPDPASVVNACAQLVKPGGHVFFSTLN 161
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-155 7.72e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 68.16  E-value: 7.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  61 LDVGCGGGILSESMARQ--GAKVTGLDMGAEPLQVARLHALE-SGVAVDYVQETVEEHAAAHPQKYDVVTCMEMLEHVPD 137
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAAlGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1890641966 138 PASVVNACAQLVKPGGHV 155
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-158 9.46e-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: 65.53  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  59 TVLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEHAAAHPQKYDVVTCMEMLEH-V 135
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|...
gi 1890641966 136 PDPASVVNACAQLVKPGGHVFFS 158
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PLN02244 PLN02244
tocopherol O-methyltransferase
 58-159 1.66e-12

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 65.92  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  58 KTVLDVGCGGGILSESMARQ-GAKVTGLDMgaEPLQVARLHAL--ESGVAvDYVQETVEEhAAAHP---QKYDVVTCMEM 131
Cdd:PLN02244  120 KRIVDVGCGIGGSSRYLARKyGANVKGITL--SPVQAARANALaaAQGLS-DKVSFQVAD-ALNQPfedGQFDLVWSMES 195

                          90       100
                  ....*....|....*....|....*...
gi 1890641966 132 LEHVPDPASVVNACAQLVKPGGHVFFST 159
Cdd:PLN02244  196 GEHMPDKRKFVQELARVAAPGGRIIIVT 223
PRK08317 PRK08317
hypothetical protein; Provisional
 57-155 2.16e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 64.57  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQ---GAKVTGLDMGAEPLQVARLHALESGVAVDYVQeTVEEHAAAHPQKYDVVTCMEMLE 133
Cdd:PRK08317   20 GDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVR-GDADGLPFPDGSFDAVRSDRVLQ 98

                          90       100
                  ....*....|....*....|..
gi 1890641966 134 HVPDPASVVNACAQLVKPGGHV 155
Cdd:PRK08317   99 HLEDPARALAEIARVLRPGGRV 120
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
59-213 2.42e-11

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 61.90  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  59 TVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALESGVAVDY--VQETVEEHAAAHPQKYDVVTCMEMLEHVP 136
Cdd:PRK11036   47 RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMqfIHCAAQDIAQHLETPVDLILFHAVLEWVA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966 137 DPASVVNACAQLVKPGGHVFFSTLNRNGKSWLMAVVGA-EYILRMVPKGthdiKKF-------IKPAELLNWVDHTPLQE 208
Cdd:PRK11036  127 DPKSVLQTLWSVLRPGGALSLMFYNANGLLMHNMVAGNfDYVQAGMPKR----KKRtlspdypLDPEQVYQWLEEAGWQI 202


                  ....*
gi 1890641966 209 RHMTG 213
Cdd:PRK11036  203 MGKTG 207
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 57-148 9.09e-10

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 56.77  E-value: 9.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALESGVA--VDYVQETVEEHAAahpqKYDVVTCMEMLEH 134
Cdd:PRK07580   64 GLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDLESLLG----RFDTVVCLDVLIH 139

                          90
                  ....*....|....
gi 1890641966 135 VPDPAsVVNACAQL 148
Cdd:PRK07580  140 YPQED-AARMLAHL 152
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 57-162 4.53e-09

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: 54.89  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGA-KVTGLDMGAEPLQVARLHALESGVAVDYVQETVEEHAAAHpqKYDVVTC------M 129
Cdd:COG3897    71 GKRVLELGCGLGLVGIAAAKAGAaDVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAG--GFDLILGgdvlyeR 148

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890641966 130 EMLEHVpdpASVVNACAqlvKPGGHVFFSTLNR 162
Cdd:COG3897   149 DLAEPL---LPFLDRLA---APGGEVLIGDPGR 175
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 45-137 8.41e-09

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 54.86  E-value: 8.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  45 LGYITERaGGLFGKTVLDVGCGGGILSESMARQGAKVTGLD----MGAEPLQVAR--LHALESGVAVDYVQETVEEHAAa 118
Cdd:PLN02585  134 LLWLAED-GSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDisaaMVAEAERRAKeaLAALPPEVLPKFEANDLESLSG- 211

                          90
                  ....*....|....*....
gi 1890641966 119 hpqKYDVVTCMEMLEHVPD 137
Cdd:PLN02585  212 ---KYDTVTCLDVLIHYPQ 227
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 60-160 1.33e-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: 53.83  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  60 VLDVGCGGGILSESMARQGAKV--TGLDMGAEPLQVARLHaleSGVAVDYVQETVEEHAAAhPQKYDVVTCMEMLEHVPD 137
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLE-DSSFDLIVSNLALQWCDD 113

                          90       100
                  ....*....|....*....|...
gi 1890641966 138 PASVVNACAQLVKPGGHVFFSTL 160
Cdd:TIGR02072 114 LSQALSELARVLKPGGLLAFSTF 136
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
53-126 1.45e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 52.98  E-value: 1.45e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890641966  53 GGLFGKTVLDVGCGGGILSESMARQGA-KVTGLDMGAEPLQVARLHALESGVAVDYVQETVEEHAAahPQKYDVV 126
Cdd:COG2263    42 GDIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPL--GGSVDTV 114
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
57-158 1.92e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 53.64  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAK-VTGLDMGAEPLQVARLHALESGVAvDYVqeTVEEHAAAHPQKYDVVTC------- 128
Cdd:COG2264   149 GKTVLDVGCGSGILAIAAAKLGAKrVLAVDIDPVAVEAARENAELNGVE-DRI--EVVLGDLLEDGPYDLVVAnilanpl 225

                          90       100       110
                  ....*....|....*....|....*....|
gi 1890641966 129 MEMLEHVpdpasvvnacAQLVKPGGHVFFS 158
Cdd:COG2264   226 IELAPDL----------AALLKPGGYLILS 245
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 57-158 2.05e-08

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


Pssm-ID: 273061  Cd Length: 288  Bit Score: 53.68  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGA-KVTGLDMGAEPLQVARLHALESGVAvDYVQETVEEHAAAHPQKYDVVTCMEMLEHV 135
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAaKVVGIDIDPLAVESARKNAELNQVS-DRLQVKLIYLEQPIEGKADVIVANILAEVI 238

                          90       100
                  ....*....|....*....|...
gi 1890641966 136 PDPASVVnacAQLVKPGGHVFFS 158
Cdd:TIGR00406 239 KELYPQF---SRLVKPGGWLILS 258
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-158 4.22e-08

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: 52.65  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAK-VTGLDMGAEPLQVARLHALESGVAvdyVQETVEEHAAAHPQKYDVVTC------- 128
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVE---ARLEVYLPGDLPKEKADVVVAniladpl 238

                          90       100       110
                  ....*....|....*....|....*....|
gi 1890641966 129 MEMLEHVpdpasvvnacAQLVKPGGHVFFS 158
Cdd:pfam06325 239 IELAPDI----------YALVKPGGYLILS 258
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
57-158 8.52e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 51.31  E-value: 8.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAK-VTGLDMGAEPLQVARLHALESGVAVDyvqetveEHAAAHPQKYDVVTC------- 128
Cdd:PRK00517  120 GKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAARENAELNGVELN-------VYLPQGDLKADVIVAnilanpl 192

                          90       100       110
                  ....*....|....*....|....*....|
gi 1890641966 129 MEMLEHVpdpasvvnacAQLVKPGGHVFFS 158
Cdd:PRK00517  193 LELAPDL----------ARLLKPGGRLILS 212
PRK06202 PRK06202
hypothetical protein; Provisional
 43-146 1.08e-07

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 51.15  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  43 LRLGYITERAgglfgKTVLDVGCGGGILSESMA----RQGAK--VTGLDMGAEPLQVARLHALESGVAVDYV--QETVEE 114
Cdd:PRK06202   52 LRPALSADRP-----LTLLDIGCGGGDLAIDLArwarRDGLRleVTAIDPDPRAVAFARANPRRPGVTFRQAvsDELVAE 126

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1890641966 115 haaahPQKYDVVTCMEMLEHVpDPASVVNACA 146
Cdd:PRK06202  127 -----GERFDVVTSNHFLHHL-DDAEVVRLLA 152
PRK14967 PRK14967
putative methyltransferase; Provisional
 50-128 7.29e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  50 ERAGGLFGKTVLDVGCGGGILSESMARQGA-KVTGLDMGAEPLQVARLHALESGVAVDYVQETVEEHAAAHPqkYDVVTC 128
Cdd:PRK14967   30 AAEGLGPGRRVLDLCTGSGALAVAAAAAGAgSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRP--FDVVVS 107
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
47-155 7.30e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.59  E-value: 7.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  47 YITERAGGLFGKTVLDVGCGGG----ILSESMARQGaKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEhAAAHPQ 121
Cdd:pfam01209  33 FTMKCMGVKRGNKFLDVAGGTGdwtfGLSDSAGSSG-KVVGLDINENMLKEGEKKAKEEGKYnIEFLQGNAEE-LPFEDD 110

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1890641966 122 KYDVVTCMEMLEHVPDPASVVNACAQLVKPGGHV 155
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRV 144
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 57-157 1.31e-06

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 47.83  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMAR--QGAKVTGLDMGAEPLQVARLHALESGVA--VDYVQETVEEHAAA-HPQKYDVVTC--- 128
Cdd:COG4123    38 GGRVLDLGTGTGVIALMLAQrsPGARITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFAAElPPGSFDLVVSnpp 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1890641966 129 -MEMLEHV--PDPA-------------SVVNACAQLVKPGGHVFF 157
Cdd:COG4123   118 yFKAGSGRksPDEAraiarhedaltleDLIRAAARLLKPGGRFAL 162
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 59-160 3.86e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 46.67  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  59 TVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARlhalESGVAVDYVQETVEE--HAAAhpqKYDVVTCMEMLEHVP 136
Cdd:PRK10258   45 HVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQAR----QKDAADHYLAGDIESlpLATA---TFDLAWSNLAVQWCG 117

                          90       100
                  ....*....|....*....|....
gi 1890641966 137 DPASVVNACAQLVKPGGHVFFSTL 160
Cdd:PRK10258  118 NLSTALRELYRVVRPGGVVAFTTL 141
PRK14968 PRK14968
putative methyltransferase; Provisional
 57-85 7.65e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.27  E-value: 7.65e-06
                          10        20
                  ....*....|....*....|....*....
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLD 85
Cdd:PRK14968   24 GDRVLEVGTGSGIVAIVAAKNGKKVVGVD 52
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 57-153 9.35e-06

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 45.40  E-value: 9.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCG-GGILSESMARQGAKVTGLDMGAEPLQVA--RLHALESGVAV-----DYVQetveehaaaHPQKYDVVTC 128
Cdd:pfam02353  62 GMTLLDIGCGwGGLMRRAAERYDVNVVGLTLSKNQYKLArkRVAAEGLARKVevllqDYRD---------FDEPFDRIVS 132

                          90       100
                  ....*....|....*....|....*..
gi 1890641966 129 MEMLEHV--PDPASVVNACAQLVKPGG 153
Cdd:pfam02353 133 VGMFEHVghENYDTFFKKLYNLLPPGG 159
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
55-160 1.27e-05

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 45.23  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  55 LFGKTVLDVGCGGGILSESMARQGAK-VTGLDMGaePLQVARLHALE----SGVAVDYVQETVEEHAAahPQKYDVVTCM 129
Cdd:PRK15068  121 LKGRTVLDVGCGNGYHMWRMLGAGAKlVVGIDPS--QLFLCQFEAVRkllgNDQRAHLLPLGIEQLPA--LKAFDTVFSM 196

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890641966 130 EMLEHVPDPASVVNACAQLVKPGGHVFFSTL 160
Cdd:PRK15068  197 GVLYHRRSPLDHLKQLKDQLVPGGELVLETL 227
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 51-155 2.82e-05

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: 44.53  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  51 RAGGLFGKTVLDVGCGG-GILSESMARQG--AKVTGLDMGAEPLQVARlhALESGVAVDyVQETVEEHAAAHPQKYDVVt 127
Cdd:cd08232   160 RAGDLAGKRVLVTGAGPiGALVVAAARRAgaAEIVATDLADAPLAVAR--AMGADETVN-LARDPLAAYAADKGDFDVV- 235

                          90       100
                  ....*....|....*....|....*...
gi 1890641966 128 cmemLEHVPDPASvVNACAQLVKPGGHV 155
Cdd:cd08232   236 ----FEASGAPAA-LASALRVVRPGGTV 258
arsM PRK11873
arsenite methyltransferase;
57-158 3.06e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.17  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGI---LSesmARQ-GA--KVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEE-----HAAahpqkyD 124
Cdd:PRK11873   78 GETVLDLGSGGGFdcfLA---ARRvGPtgKVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEAlpvadNSV------D 148

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890641966 125 VV--TCMEMLehVPDPASVVNACAQLVKPGGHVFFS 158
Cdd:PRK11873  149 VIisNCVINL--SPDKERVFKEAFRVLKPGGRFAIS 182
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
57-153 4.86e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGA-KVTGLDMGAEPLQVARLHALESGVAvDYVqETVEEHAAAH--PQKYDVVTCmEMLE 133
Cdd:COG4076    36 GDVVLDIGTGSGLLSMLAARAGAkKVYAVEVNPDIAAVARRIIAANGLS-DRI-TVINADATDLdlPEKADVIIS-EMLD 112

                          90       100
                  ....*....|....*....|....
gi 1890641966 134 HV-PDP---ASVVNACAQLVKPGG 153
Cdd:COG4076   113 TAlLDEgqvPILNHARKRLLKPGG 136
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-155 5.30e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.22  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  50 ERAGGLFGKTVLDVGCGGGILSESMARQG---AKVTGLDMGAEPLQVA--RLHALESGVAVDYVQetveEHAAAHP---Q 121
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGreKLRDLGLSGNVEFVQ----GDAEALPfpdN 120

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1890641966 122 KYDVVTcmeM---LEHVPDPASVVNACAQLVKPGGHV 155
Cdd:PRK00216  121 SFDAVT---IafgLRNVPDIDKALREMYRVLKPGGRL 154
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 50-155 1.75e-04

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 42.05  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  50 ERAGGLFGKTVLDVGCGG-GILSESMARQ-GA-KVTGLDMGAEPLQVARlhALESGVAVDYVQETVEEHAAAHP--QKYD 124
Cdd:COG1063   155 ERAGVKPGDTVLVIGAGPiGLLAALAARLaGAaRVIVVDRNPERLELAR--ELGADAVVNPREEDLVEAVRELTggRGAD 232

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890641966 125 VVtcmemLEHVPDPAsVVNACAQLVKPGGHV 155
Cdd:COG1063   233 VV-----IEAVGAPA-ALEQALDLVRPGGTV 257
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 40-155 2.77e-04

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: 41.41  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  40 INPLRLGY-ITERAGGLFGKTVLDVGCGG-GILSESMAR-QGAKVTGLDMGAEPLQVARLHALESGVAV--DYVQETVEE 114
Cdd:cd08261   142 VEPLAIGAhAVRRAGVTAGDTVLVVGAGPiGLGVIQVAKaRGARVIVVDIDDERLEFARELGADDTINVgdEDVAARLRE 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1890641966 115 HAAAhpQKYDVV---TCMemlehvpdPASVVNACaQLVKPGGHV 155
Cdd:cd08261   222 LTDG--EGADVVidaTGN--------PASMEEAV-ELVAHGGRV 254
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 57-157 3.02e-04

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: 40.52  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGG----ILseSMARQGAKVTGLDmgaePL--------QVARLHALEsGVAVdyVQETVEEHaaAHPQKYD 124
Cdd:COG0357    68 GARVLDVGSGAGfpgiPL--AIARPDLQVTLVD----SLgkkiaflrEVVRELGLK-NVTV--VHGRAEEL--APREKFD 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1890641966 125 VVTC-----MEMLehvpdpasvVNACAQLVKPGGHVFF 157
Cdd:COG0357   137 VVTAravapLPDL---------LELALPLLKPGGRLLA 165
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 57-126 3.88e-04

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 40.93  E-value: 3.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890641966  57 GKTVLDVGCGGGILSESMARQGAKVTGLDMGAEPLQVARLHALESGVA-VDYVQETVEEHAAAHP--QKYDVV 126
Cdd:COG2265   234 GERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLEEVLPELLwgGRPDVV 306
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 49-155 5.09e-04

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 40.64  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  49 TERAGGLFGKTVLDVGCGG--GILSESMAR-QGAKVTGLDMGAEPLQVARLHALESgvAVDYVQETVEE--HAAAHPQKY 123
Cdd:cd08253   137 FHRAGAKAGETVLVHGGSGavGHAAVQLARwAGARVIATASSAEGAELVRQAGADA--VFNYRAEDLADriLAATAGQGV 214

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1890641966 124 DVVtcMEMLEHVpdpasVVNACAQLVKPGGHV 155
Cdd:cd08253   215 DVI--IEVLANV-----NLAKDLDVLAPGGRI 239
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
78-157 7.16e-04

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 38.36  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  78 GAKVTGLDMGAEPLQVARlhalESG--VAVDYVQETVEE--HAAAHPQKYDVVtcmemLEHVPDPASvVNACAQLVKPGG 153
Cdd:pfam00107  14 GAKVIAVDGSEEKLELAK----ELGadHVINPKETDLVEeiKELTGGKGVDVV-----FDCVGSPAT-LEQALKLLRPGG 83


                  ....
gi 1890641966 154 HVFF 157
Cdd:pfam00107  84 RVVV 87
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
58-166 8.98e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 39.32  E-value: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966   58 KTVLDVGCGGGILSESMARQGA--KVTGLDMGAEPLQVARLHALESGVavdyvQETVEEHA-----AAHPQKYDVVTCME 130
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhlQLHGYTISPEQAEVGRERIRALGL-----QGRIRIFYrdsakDPFPDTYDLVFGFE 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1890641966  131 MLEHVPDPASVVNACAQLVKPGGHVFFSTLNRNGKS 166
Cdd:smart00828  76 VIHHIKDKMDLFSNISRHLKDGGHLVLADFIANLLS 111
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-128 9.63e-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: 38.73  E-value: 9.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890641966  56 FGKTVLDVGCGGGILSESMARQG--AKVTGLDMGAEPLQVARLHALESGV-AVDYVQETVeeHAAAHPQKYDVVTC 128
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLeNGEVVASDV--YSGVEDGKFDLIIS 104
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 57-155 1.16e-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: 38.72  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCG-GGiLSESMARQGA-KVTGLDMG----AEPLQVARLHALESGVAVDYVQETVEEHaaaHPQKYDVVTC-- 128
Cdd:pfam01728  22 GKTVLDLGAApGG-WSQVALQRGAgKVVGVDLGpmqlWKPRNDPGVTFIQGDIRDPETLDLLEEL---LGRKVDLVLSdg 97

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890641966 129 ---MEMLEHVPDPASV------VNACAQLVKPGGHV 155
Cdd:pfam01728  98 spfISGNKVLDHLRSLdlvkaaLEVALELLRKGGNF 133
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 51-157 1.33e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 38.90  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  51 RAGGLFGKTVLDVGCGGGILSESMARQ--GAKVTGLDMGAEPLQVARlhalesGVAVDYVQETVEEHAAAHPqkYDVVTC 128
Cdd:PRK14103   24 RVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR------ERGVDARTGDVRDWKPKPD--TDVVVS 95

                          90       100
                  ....*....|....*....|....*....
gi 1890641966 129 MEMLEHVPDPASVVNACAQLVKPGGHVFF 157
Cdd:PRK14103   96 NAALQWVPEHADLLVRWVDELAPGSWIAV 124
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 40-155 1.50e-03

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


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 38.99  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  40 INPLRLGYITERAGGLFGKTVLDVGCGGGILSESMAR----QGaKVTGLDMGAEPLQVARLHALESGV--AVDYVQETVE 113
Cdd:COG2519    75 IYPKDAGYIIARLDIFPGARVLEAGTGSGALTLALARavgpEG-KVYSYERREDFAEIARKNLERFGLpdNVELKLGDIR 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1890641966 114 EHAAahPQKYDVVtcmeMLEhVPDPASVVNACAQLVKPGGHV 155
Cdd:COG2519   154 EGID--EGDVDAV----FLD-MPDPWEALEAVAKALKPGGVL 188
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 57-128 1.89e-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: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQ--GAKVTGLDmgaeplqvarlhalESGVAVDYVQETVEEH-------------AAAHPQ 121
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRnpEARVTLVD--------------VNARAVELARANAAANglenvevlwsdglSGVPDG 115


                  ....*..
gi 1890641966 122 KYDVVTC 128
Cdd:COG2813   116 SFDLILS 122
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 50-128 1.91e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.59  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  50 ERAGGLFGKTVLDVGCGGGILSESMA--RQGAKVTGLDMGAEPLQVAR----LHALESGVAV---DYVQetveehAAAHP 120
Cdd:COG2890   106 ALLPAGAPPRVLDLGTGSGAIALALAkeRPDARVTAVDISPDALAVARrnaeRLGLEDRVRFlqgDLFE------PLPGD 179


                  ....*...
gi 1890641966 121 QKYDVVTC 128
Cdd:COG2890   180 GRFDLIVS 187
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
57-135 3.68e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 37.91  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVAV---DYVQETveehaaahpQKYDVVTCMEML 132
Cdd:PRK11705  168 GMRVLDIGCGWGGLARYAAEHyGVSVVGVTISAEQQKLAQERCAGLPVEIrlqDYRDLN---------GQFDRIVSVGMF 238


                  ...
gi 1890641966 133 EHV 135
Cdd:PRK11705  239 EHV 241
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 57-95 5.27e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 5.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1890641966  57 GKTVLDVGCGGGILSESMA--RQGAKVTGLDMGAEPLQVAR 95
Cdd:PRK09328  109 PLRVLDLGTGSGAIALALAkeRPDAEVTAVDISPEALAVAR 149
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 57-143 5.97e-03

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


Pssm-ID: 273958  Cd Length: 194  Bit Score: 36.58  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMaRQGAKVTGldMGAEPLQVARLHALESGVAVdyVQETVEEHAAAHP-QKYDVVTCMEMLEHV 135
Cdd:TIGR02081  14 GSRVLDLGCGDGELLALL-RDEKQVRG--YGIEIDQDGVLACVARGVNV--IQGDLDEGLEAFPdKSFDYVILSQTLQAT 88


                  ....*...
gi 1890641966 136 PDPASVVN 143
Cdd:TIGR02081  89 RNPEEILD 96
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 57-158 6.89e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.42  E-value: 6.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890641966  57 GKTVLDVGCGGGILSESMARQ-GAKVTGLDMGAEPLQVARLHALESGVAVDY-VQETVEEHAAAHpqKYDVVTCMEMLEH 134
Cdd:PLN02336  267 GQKVLDVGCGIGGGDFYMAENfDVHVVGIDLSVNMISFALERAIGRKCSVEFeVADCTKKTYPDN--SFDVIYSRDTILH 344

                          90       100
                  ....*....|....*....|....
gi 1890641966 135 VPDPASVVNACAQLVKPGGHVFFS 158
Cdd:PLN02336  345 IQDKPALFRSFFKWLKPGGKVLIS 368
 
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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