NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1125799894|ref|WP_075114520|]
View 

malonyl-ACP O-methyltransferase BioC [Aeromonas sp. YN13HZO-058]

Protein Classification

malonyl-ACP O-methyltransferase( domain architecture ID 11493568)

malonyl-[acyl-carrier protein] O-methyltransferase BioC is a class I SAM-dependent methyltransferase in the biotin biosynthesis pathway that converts the free carboxyl group of a malonyl-thioester to its methyl ester using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-269 1.61e-61

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: 194.04  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  16 RFGAAARHYDAHARFQQEVGQALLEWMPDRPvgTDLTVSGLDLGCGTGFFLPQLANRCHQ--LVGLDLAPGMLAQAALRG 93
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKG--IFIPASVLDIGCGTGYLTRALLKRFPQaeFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  94 SGARL-LCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQldgraHVN 172
Cdd:TIGR02072  79 SENVQfICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894 173 RFLSLPQLEQALAAAG-VASHELRCITwdLAYLELPQLLRDLKGIGANQVNDNQgsaapaglSGRARLQQLAQAYEAFRQ 251
Cdd:TIGR02072 154 RYLSLDELKALLKNSFeLLTLEEELIT--LSFDDPLDVLRHLKKTGANGLSSGR--------TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 1125799894 252 PDGrLVASYRVCLGRLSK 269
Cdd:TIGR02072 224 PDG-LPLTYHVVYGIAKK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-269 1.61e-61

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: 194.04  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  16 RFGAAARHYDAHARFQQEVGQALLEWMPDRPvgTDLTVSGLDLGCGTGFFLPQLANRCHQ--LVGLDLAPGMLAQAALRG 93
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKG--IFIPASVLDIGCGTGYLTRALLKRFPQaeFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  94 SGARL-LCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQldgraHVN 172
Cdd:TIGR02072  79 SENVQfICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894 173 RFLSLPQLEQALAAAG-VASHELRCITwdLAYLELPQLLRDLKGIGANQVNDNQgsaapaglSGRARLQQLAQAYEAFRQ 251
Cdd:TIGR02072 154 RYLSLDELKALLKNSFeLLTLEEELIT--LSFDDPLDVLRHLKKTGANGLSSGR--------TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 1125799894 252 PDGrLVASYRVCLGRLSK 269
Cdd:TIGR02072 224 PDG-LPLTYHVVYGIAKK 240
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 8-265 1.11e-51

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 169.17  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894   8 VDKAQLARRFGAAARHYDAHARFQQEVGQALLEWMPDRPVGTDLtvsglDLGCGTGFFLPQLANRCHQLVGLDLAPGMLA 87
Cdd:PRK10258    4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVL-----DAGCGPGWMSRYWRERGSQVTALDLSPPMLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  88 QAALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQLDG 167
Cdd:PRK10258   79 QARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894 168 RAHVNRFLSLPQLEQALAAAGvASHELRCITwdLAYLELPQLLRDLKGIGANQVNDNQGSAapagLSGRARLQQLAQAYE 247
Cdd:PRK10258  159 RPHANRFLPPDAIEQALNGWR-YQHHIQPIT--LWFDDALSAMRSLKGIGATHLHEGRDPR----ILTRSQLQRLQLAWP 231

                         250
                  ....*....|....*...
gi 1125799894 248 afrQPDGRLVASYRVCLG 265
Cdd:PRK10258  232 ---QQQGRYPLTYHLFLG 246
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 17-164 8.77e-35

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: 122.41  E-value: 8.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  17 FGAAARHYDAHarfqqevgQALLEWMPDRPvgtDLTVsgLDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQAALR---- 92
Cdd:COG2226     1 FDRVAARYDGR--------EALLAALGLRP---GARV--LDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaea 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125799894  93 GSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQ 164
Cdd:COG2226    68 GLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-147 2.09e-30

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 109.29  E-value: 2.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQA--ALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFG 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAreKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 1125799894 134 ELLRVVKPGGQIFF 147
Cdd:pfam08241  81 EIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-151 7.35e-15

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 68.61  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRC-HQLVGLDLAPGMLAQA-----ALRGSGARLLCGDAEQLPF-ADSAFDWVFSSLALQW-CER 127
Cdd:cd02440     3 LDLGCGTGALALALASGPgARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlVED 82

                          90       100
                  ....*....|....*....|....
gi 1125799894 128 PAHAFGELLRVVKPGGQIFFSTLL 151
Cdd:cd02440    83 LARFLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-269 1.61e-61

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: 194.04  E-value: 1.61e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  16 RFGAAARHYDAHARFQQEVGQALLEWMPDRPvgTDLTVSGLDLGCGTGFFLPQLANRCHQ--LVGLDLAPGMLAQAALRG 93
Cdd:TIGR02072   1 SFNKAAKTYDRHAKIQREMAKRLLALLKEKG--IFIPASVLDIGCGTGYLTRALLKRFPQaeFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  94 SGARL-LCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQldgraHVN 172
Cdd:TIGR02072  79 SENVQfICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894 173 RFLSLPQLEQALAAAG-VASHELRCITwdLAYLELPQLLRDLKGIGANQVNDNQgsaapaglSGRARLQQLAQAYEAFRQ 251
Cdd:TIGR02072 154 RYLSLDELKALLKNSFeLLTLEEELIT--LSFDDPLDVLRHLKKTGANGLSSGR--------TSRKQLKAFLERYEQEFQ 223

                         250
                  ....*....|....*...
gi 1125799894 252 PDGrLVASYRVCLGRLSK 269
Cdd:TIGR02072 224 PDG-LPLTYHVVYGIAKK 240
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 8-265 1.11e-51

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 169.17  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894   8 VDKAQLARRFGAAARHYDAHARFQQEVGQALLEWMPDRPVGTDLtvsglDLGCGTGFFLPQLANRCHQLVGLDLAPGMLA 87
Cdd:PRK10258    4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVL-----DAGCGPGWMSRYWRERGSQVTALDLSPPMLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  88 QAALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQLDG 167
Cdd:PRK10258   79 QARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894 168 RAHVNRFLSLPQLEQALAAAGvASHELRCITwdLAYLELPQLLRDLKGIGANQVNDNQGSAapagLSGRARLQQLAQAYE 247
Cdd:PRK10258  159 RPHANRFLPPDAIEQALNGWR-YQHHIQPIT--LWFDDALSAMRSLKGIGATHLHEGRDPR----ILTRSQLQRLQLAWP 231

                         250
                  ....*....|....*...
gi 1125799894 248 afrQPDGRLVASYRVCLG 265
Cdd:PRK10258  232 ---QQQGRYPLTYHLFLG 246
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 17-164 8.77e-35

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: 122.41  E-value: 8.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  17 FGAAARHYDAHarfqqevgQALLEWMPDRPvgtDLTVsgLDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQAALR---- 92
Cdd:COG2226     1 FDRVAARYDGR--------EALLAALGLRP---GARV--LDLGCGTGRLALALAERGARVTGVDISPEMLELARERaaea 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1125799894  93 GSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTLLDESLWQLRAAWQQ 164
Cdd:COG2226    68 GLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-147 2.09e-30

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 109.29  E-value: 2.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQA--ALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFG 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAreKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 1125799894 134 ELLRVVKPGGQIFF 147
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-143 2.15e-26

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 98.79  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRC-HQLVGLDLAPGMLAQA----ALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAH 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGgARVTGVDLSPEMLERAreraAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 1125799894 131 --AFGELLRVVKPGG 143
Cdd:pfam13649  82 eaALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 56-149 9.30e-25

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: 95.47  E-value: 9.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQAALRGS--GARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFG 133
Cdd:COG2227    29 LDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAelNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPAALLR 108

                          90
                  ....*....|....*.
gi 1125799894 134 ELLRVVKPGGQIFFST 149
Cdd:COG2227   109 ELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-188 5.36e-24

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 95.45  E-value: 5.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  10 KAQLARRFGAAARHYDAHA------RFQQEVGQALLEWMPDRPVGtdltvSGLDLGCGTGFFLPQLANRCHQLVGLDLAP 83
Cdd:COG4976     4 DAYVEALFDQYADSYDAALvedlgyEAPALLAEELLARLPPGPFG-----RVLDLGCGTGLLGEALRPRGYRLTGVDLSE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  84 GMLAQAALRGSGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQIFFSTlldeslwqlraawQ 163
Cdd:COG4976    79 EMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSV-------------E 145

                         170       180
                  ....*....|....*....|....*
gi 1125799894 164 QLDGRAHvnRFLSLPQLEQALAAAG 188
Cdd:COG4976   146 DADGSGR--YAHSLDYVRDLLAAAG 168
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-149 2.50e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 88.34  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRC--HQLVGLDLAPGMLAQAALRGSGARLLCGDAEQLPFaDSAFDWVFSSLALQWCERPAHAFG 133
Cdd:COG4106     6 LDLGCGTGRLTALLAERFpgARVTGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVVSNAALHWLPDHAALLA 84

                          90
                  ....*....|....*.
gi 1125799894 134 ELLRVVKPGGQIFFST 149
Cdd:COG4106    85 RLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
 54-145 1.11e-20

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 88.07  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  54 SGLDLGCGTGFFLPQLANRCH---QLVGLDLAPGMLAQAALR----GSGARLLCGDAEQLPFADSAFDWVFSSLALQWCE 126
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLE 101

                          90
                  ....*....|....*....
gi 1125799894 127 RPAHAFGELLRVVKPGGQI 145
Cdd:PRK08317  102 DPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-151 7.35e-15

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 68.61  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRC-HQLVGLDLAPGMLAQA-----ALRGSGARLLCGDAEQLPF-ADSAFDWVFSSLALQW-CER 127
Cdd:cd02440     3 LDLGCGTGALALALASGPgARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlVED 82

                          90       100
                  ....*....|....*....|....
gi 1125799894 128 PAHAFGELLRVVKPGGQIFFSTLL 151
Cdd:cd02440    83 LARFLEEARRLLKPGGVLVLTLVL 106
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 56-146 9.45e-15

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 71.52  E-value: 9.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQLANRCHQLVGLDLAPGMLAQAALRG---SGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPA 129
Cdd:TIGR01934  44 LDVACGTGdlaIELAKSAPDRGKVTGVDFSSEMLEVAKKKSelpLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQ 123

                          90
                  ....*....|....*..
gi 1125799894 130 HAFGELLRVVKPGGQIF 146
Cdd:TIGR01934 124 KALREMYRVLKPGGRLV 140
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 56-188 9.50e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.32  E-value: 9.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANR-CHQLVGLDLAPGMLAQA-----ALRGSGARLLCGDAEQL-PFADSAFDWVFSSLALQWC--E 126
Cdd:COG0500    31 LDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALAraraaKAGLGNVEFLVADLAELdPLPAESFDLVVAFGVLHHLppE 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125799894 127 RPAHAFGELLRVVKPGGQIFFS---TLLDESLWQLRAAWQQLDGRAHVN-RFLSLPQLEQALAAAG 188
Cdd:COG0500   111 EREALLRELARALKPGGVLLLSasdAAAALSLARLLLLATASLLELLLLlRLLALELYLRALLAAA 176
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 56-144 3.08e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 64.40  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQLANRCHQLVGLDLAPGMLAQAALR------GSGARLLCGDAEQLPFADSAFDWVFSSLALQWCE 126
Cdd:PRK00216   56 LDLACGTGdlaIALAKAVGKTGEVVGLDFSEGMLAVGREKlrdlglSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVP 135

                          90
                  ....*....|....*...
gi 1125799894 127 RPAHAFGELLRVVKPGGQ 144
Cdd:PRK00216  136 DIDKALREMYRVLKPGGR 153
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
56-145 3.06e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 61.69  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQLANRCHQLVGLDLAPGML--AQAALRGSG---ARLLCGDAEQLPFADSAFDWVFSSLALQWCER 127
Cdd:pfam01209  47 LDVAGGTGdwtFGLSDSAGSSGKVVGLDINENMLkeGEKKAKEEGkynIEFLQGNAEELPFEDDSFDIVTISFGLRNFPD 126

                          90
                  ....*....|....*...
gi 1125799894 128 PAHAFGELLRVVKPGGQI 145
Cdd:pfam01209 127 YLKVLKEAFRVLKPGGRV 144
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-145 5.02e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.15  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCHQL--VGLDLAPGMLAQAALRGSGARLLCGDAEQLPFADSA------FDWVFSSLALQWCER 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGeldpgsFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1125799894 128 PAHAFGELLRVVKPGGQI 145
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-143 9.61e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.89  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCH---QLVGLDLAPGMLAQAALRG-----SGARLLCGDAEQLP--FADSAFDWVFSSLALQWC 125
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAqklgfDNVEFEQGDIEELPelLEDDKFDVVISNCVLNHI 87

                          90
                  ....*....|....*...
gi 1125799894 126 ERPAHAFGELLRVVKPGG 143
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGG 105
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 14-143 7.58e-09

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 55.30  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  14 ARRFGAAARHYDAharFQQEVGQALLEWMPDRPVgtdltvSGLDLGCGTGFFLPQLANRCH-----QLVGLDLAPGMLAQ 88
Cdd:PRK11088   57 ARRAFLDAGHYQP---LRDAVANLLAERLDEKAT------ALLDIGCGEGYYTHALADALPeittmQLFGLDISKVAIKY 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1125799894  89 AALRGSGARLLCGDAEQLPFADSAFDWVFSSLAlqwcerPAHAfGELLRVVKPGG 143
Cdd:PRK11088  128 AAKRYPQVTFCVASSHRLPFADQSLDAIIRIYA------PCKA-EELARVVKPGG 175
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 56-149 1.73e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.62  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCH-QLVGLDLAPGML--AQAALRGSG----ARLLCGDAEQLPfADSAFDWVFSSLALQW--CE 126
Cdd:COG2230    56 LDIGCGWGGLALYLARRYGvRVTGVTLSPEQLeyARERAAEAGladrVEVRLADYRDLP-ADGQFDAIVSIGMFEHvgPE 134

                          90       100
                  ....*....|....*....|...
gi 1125799894 127 RPAHAFGELLRVVKPGGQIFFST 149
Cdd:COG2230   135 NYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-188 2.03e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 49.73  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQAALrgsGARLLCGDAEQLPFADSAFDWVFSSLALQWCERPAHAFGEL 135
Cdd:pfam13489  27 LDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALL---NVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPALLRQI 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1125799894 136 LRVVKPGGQIFFSTLLDESLW-QLRAAWQQLDGRAHVNRFLSLPQLEQALAAAG 188
Cdd:pfam13489 104 AALLKPGGLLLLSTPLASDEAdRLLLEWPYLRPRNGHISLFSARSLKRLLEEAG 157
arsM PRK11873
arsenite methyltransferase;
56-148 5.28e-07

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 49.56  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGF--FL--PQLANRCHqLVGLDLAPGMLAQAalRGSGARL-------LCGDAEQLPFADSAFDWVFSSLALQW 124
Cdd:PRK11873   82 LDLGSGGGFdcFLaaRRVGPTGK-VIGVDMTPEMLAKA--RANARKAgytnvefRLGEIEALPVADNSVDVIISNCVINL 158

                          90       100
                  ....*....|....*....|....
gi 1125799894 125 CERPAHAFGELLRVVKPGGQIFFS 148
Cdd:PRK11873  159 SPDKERVFKEAFRVLKPGGRFAIS 182
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 56-145 3.98e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 46.81  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQLANRCHQLVGLDLAPGMLAQAALRGSGARLLC--------GDAEQLPFADSAFDWVFSSLALQW 124
Cdd:PLN02233   78 LDLCCGSGdlaFLLSEKVGSDGKVMGLDFSSEQLAVAASRQELKAKSCykniewieGDATDLPFDDCYFDAITMGYGLRN 157

                          90       100
                  ....*....|....*....|.
gi 1125799894 125 CERPAHAFGELLRVVKPGGQI 145
Cdd:PLN02233  158 VVDRLKAMQEMYRVLKPGSRV 178
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 50-144 3.60e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 44.50  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  50 DLTVsgLDLGCGTGFFLPQLANRC--HQLVGLDLAPGMLAQA----ALRGsgARLLCGDAEQLPFADSAFDWVFSSLALQ 123
Cdd:PLN02490  114 NLKV--VDVGGGTGFTTLGIVKHVdaKNVTILDQSPHQLAKAkqkePLKE--CKIIEGDAEDLPFPTDYADRYVSAGSIE 189

                          90       100
                  ....*....|....*....|.
gi 1125799894 124 WCERPAHAFGELLRVVKPGGQ 144
Cdd:PLN02490  190 YWPDPQRGIKEAYRVLKIGGK 210
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 37-138 8.09e-05

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 42.44  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  37 ALLEWMPDRPvgtdlTVsgLDLGCGTGFFLPQLANrcHQLV---GLDLAPGMLAQAALRGsgARLLCGDAEQ--LPFADS 111
Cdd:pfam07021   6 YILEWIPPGS-----RV--LDLGCGDGTLLYLLKE--EKGVdgyGIELDAAGVAECVAKG--LYVIQGDLDEglEHFPDK 74

                          90       100
                  ....*....|....*....|....*..
gi 1125799894 112 AFDWVFSSLALQWCERPAHAFGELLRV 138
Cdd:pfam07021  75 SFDYVILSQTLQATRNPREVLDEMLRI 101
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 59-150 8.80e-05

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


Pssm-ID: 399030  Cd Length: 218  Bit Score: 42.80  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  59 GCGTGFFLPQLANRCHQLVGLDLAPGMLAQAA-----------------LRGSGARLLCGDAEQLPFAD-SAFDWVFSSL 120
Cdd:pfam05724  45 LCGKALDMVWLAEQGHFVVGVEISELAVEKFFaeaglsppitelsgfkeYSSGNISLYCGDFFTLPREElGKFDLIYDRA 124

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1125799894 121 ALQWCE---RPAHAfGELLRVVKPGGQIFFSTL 150
Cdd:pfam05724 125 ALCALPpemRPRYA-KQMYELLPPGGRGLLITL 156
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 38-92 2.37e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.36  E-value: 2.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1125799894  38 LLEWMPDRPVGTDLTVsgLDLGCGTGFFLPQLANRCHQLVGLDLAPGMLAQAALR 92
Cdd:PRK07580   52 VLSWLPADGDLTGLRI--LDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARER 104
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
36-143 5.00e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 40.72  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  36 QALLEWMPDRPvgtdLTVsgLDLGCGTGFFLPQLANRCHQLVGLDLAPGML--AQAALRGSGA----RLLCGDAEQL-PF 108
Cdd:PRK11036   35 DRLLAELPPRP----LRV--LDAGGGEGQTAIKLAELGHQVILCDLSAEMIqrAKQAAEAKGVsdnmQFIHCAAQDIaQH 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1125799894 109 ADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGG 143
Cdd:PRK11036  109 LETPVDLILFHAVLEWVADPKSVLQTLWSVLRPGG 143
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 77-145 5.01e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 39.67  E-value: 5.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125799894  77 VGLDLAPGMLAQAALRGSGARLLC--------GDAEQLPFADSAFDWVFSSLALQWCERPAHAFGELLRVVKPGGQI 145
Cdd:PLN02232    1 MGLDFSSEQLAVAATRQSLKARSCykciewieGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRV 77
PLN02244 PLN02244
tocopherol O-methyltransferase
 56-149 5.15e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.88  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFLPQLANR--ChQLVGLDLAP------GMLAQAALRGSGARLLCGDAEQLPFADSAFDWVfsslalqWC-E 126
Cdd:PLN02244  123 VDVGCGIGGSSRYLARKygA-NVKGITLSPvqaaraNALAAAQGLSDKVSFQVADALNQPFEDGQFDLV-------WSmE 194

                          90       100
                  ....*....|....*....|....*....
gi 1125799894 127 RPAH-----AF-GELLRVVKPGGQIFFST 149
Cdd:PLN02244  195 SGEHmpdkrKFvQELARVAAPGGRIIIVT 223
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 57-137 5.56e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 40.44  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  57 DLGCGTGFFLPQLANRC--HQLVGLDLAPGMLAQAALRGSGARLlcGDAEQ-LPFADSafDWVFSSLALQWCerPAHAfg 133
Cdd:PRK14103   35 DLGCGPGNLTRYLARRWpgAVIEALDSSPEMVAAARERGVDART--GDVRDwKPKPDT--DVVVSNAALQWV--PEHA-- 106


                  ....
gi 1125799894 134 ELLR 137
Cdd:PRK14103  107 DLLV 110
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
56-179 1.13e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 39.93  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTGFFL----PQLANRCHqLVGLDLAPGML----AQAALRGSGARLLCGDAEQLPFADSaFDWVFSSL------- 120
Cdd:COG0827   120 LDPAVGTGNLLttvlNQLKKKVN-AYGVEVDDLLIrlaaVLANLQGHPVELFHQDALQPLLIDP-VDVVISDLpvgyypn 197

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1125799894 121 -----ALQWCERPAHAFGELL------RVVKPGGQIFF---STLLDESLWQLRAAWqqLDGRAHVNRFLSLPQ 179
Cdd:COG0827   198 derakRFKLKADEGHSYAHHLfieqslNYLKPGGYLFFlvpSNLFESDQAAQLREF--LKEKAHIQGLIQLPE 268
PRK05785 PRK05785
hypothetical protein; Provisional
 56-140 1.61e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 38.90  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQLANRchQLVGLDLAPGMLAQAALRGSgaRLLcGDAEQLPFADSAFDWVFSSLALqwcerpaHAF 132
Cdd:PRK05785   56 LDVAAGKGelsYHFKKVFKY--YVVALDYAENMLKMNLVADD--KVV-GSFEALPFRDKSFDVVMSSFAL-------HAS 123


                  ....*...
gi 1125799894 133 GELLRVVK 140
Cdd:PRK05785  124 DNIEKVIA 131
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
56-118 2.73e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.96  E-value: 2.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125799894  56 LDLGCGTGFFL--PQLANrCHQLVGLDLAPGMLAQAAL----RGSGARLLCGDAEQLPFADSaFDWVFS 118
Cdd:COG2263    50 LDLGCGTGMLAigAALLG-AKKVVGVDIDPEALEIAREnaerLGVRVDFIRADVTRIPLGGS-VDTVVM 116
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 56-148 3.30e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.58  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  56 LDLGCGTG---FFLPQlaNRCHQLVGLDLAPGMLAQAALRGSGARLL----CGDAEQLPFADSAFDWVFSS---LALQwc 125
Cdd:PLN02336  271 LDVGCGIGggdFYMAE--NFDVHVVGIDLSVNMISFALERAIGRKCSvefeVADCTKKTYPDNSFDVIYSRdtiLHIQ-- 346

                          90       100
                  ....*....|....*....|...
gi 1125799894 126 ERPAhAFGELLRVVKPGGQIFFS 148
Cdd:PLN02336  347 DKPA-LFRSFFKWLKPGGKVLIS 368
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 57-143 5.88e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 37.23  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  57 DLGCGTGFFLPQLANR--CHQLVGLDLAPGMLAQAALRGSGARLLCGD-AEQLPfaDSAFDWVFSSLALQWCERPAHAFG 133
Cdd:PRK01683   37 DLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLPDCQFVEADiASWQP--PQALDLIFANASLQWLPDHLELFP 114

                          90
                  ....*....|
gi 1125799894 134 ELLRVVKPGG 143
Cdd:PRK01683  115 RLVSLLAPGG 124
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 36-117 9.61e-03

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 37.08  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125799894  36 QALLEWMPDRPvgtDLTVsgLDLGCGTGFF-LPqLANRCHQLVGLDLAPGMLAQA----ALRG-SGARLLCGDAEQ-LP- 107
Cdd:COG2265   223 AAALEWLDLTG---GERV--LDLYCGVGTFaLP-LARRAKKVIGVEIVPEAVEDArenaRLNGlKNVEFVAGDLEEvLPe 296

                          90
                  ....*....|.
gi 1125799894 108 -FADSAFDWVF 117
Cdd:COG2265   297 lLWGGRPDVVV 307
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH