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Conserved domains on  [gi|919009282|emb|CCD73280|]
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Methyltransferase domain-containing protein [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11227116)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens EEF1A lysine methyltransferase 2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
177-294 1.83e-31

Methyltransferase domain; This family appears to have methyltransferase activity.


:

Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 115.21  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  177 ETGGMRVLDVGCGGGSHSSLLAEQ-YPKAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDAGKMPEIWTD-SFDLV 254
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLG--FDNVEFEQGDIEELPELLEDdKFDVV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 919009282  255 LIFDACHDQCRPDLCIREIQRVLKIFGVFAILEINSSGNV 294
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAEL 118
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
177-294 1.83e-31

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 115.21  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  177 ETGGMRVLDVGCGGGSHSSLLAEQ-YPKAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDAGKMPEIWTD-SFDLV 254
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLG--FDNVEFEQGDIEELPELLEDdKFDVV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 919009282  255 LIFDACHDQCRPDLCIREIQRVLKIFGVFAILEINSSGNV 294
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAEL 118
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
167-289 1.65e-23

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: 93.91  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 167 DIGHGVVEKLETG-GMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRKTKSGAafnNLEFIQCDAGKMPe 245
Cdd:COG2226    9 DGREALLAALGLRpGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL---NVEFVVGDAEDLP- 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919009282 246 IWTDSFDLVLIFDACHDQCRPDLCIREIQRVLKIFGVFAILEIN 289
Cdd:COG2226   83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
180-287 4.73e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 70.18  E-value: 4.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQYPK-AHFVGLEIGEDAIRQAKQRKTKSGAaFNNLEFIQCDAGKMPeIWTDSFDLVLI-F 257
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRDLGL-SGNVEFVQGDAEALP-FPDNSFDAVTIaF 129
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 919009282 258 ------DachdqcrPDLCIREIQRVLKIFGVFAILE 287
Cdd:PRK00216 130 glrnvpD-------IDKALREMYRVLKPGGRLVILE 158
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
168-284 1.50e-12

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: 66.16  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  168 IGHGVVEKLETGGM----RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKsgaafnNLEFIQCDAGKM 243
Cdd:TIGR02072  19 MAKRLLALLKEKGIfipaSVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSE------NVQFICGDAEKL 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 919009282  244 PeIWTDSFDLV---LIFDACHDqcrPDLCIREIQRVLKIFGVFA 284
Cdd:TIGR02072  93 P-LEDSSFDLIvsnLALQWCDD---LSQALSELARVLKPGGLLA 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
182-285 3.08e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.06  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 182 RVLDVGCGGGsHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAafNNLEFIQCDAGKMPEIWTDSFDLVLIFDACH 261
Cdd:cd02440    1 RVLDLGCGTG-ALALALASGPGARVTGVDISPVALELARKAAAALLA--DNVEVLKGDAEELPPEADESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*
gi 919009282 262 DQCRPDLC-IREIQRVLKIFGVFAI 285
Cdd:cd02440   78 HLVEDLARfLEEARRLLKPGGVLVL 102
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
182-261 8.93e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 40.09  E-value: 8.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282   182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAGKMPEiwTDSFDLVLIFDACH 261
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQ-GRIRIFYRDSAKDPF--PDTYDLVFGFEVIH 78
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
177-294 1.83e-31

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 115.21  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  177 ETGGMRVLDVGCGGGSHSSLLAEQ-YPKAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDAGKMPEIWTD-SFDLV 254
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLG--FDNVEFEQGDIEELPELLEDdKFDVV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 919009282  255 LIFDACHDQCRPDLCIREIQRVLKIFGVFAILEINSSGNV 294
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAEL 118
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
167-289 1.65e-23

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: 93.91  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 167 DIGHGVVEKLETG-GMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRKTKSGAafnNLEFIQCDAGKMPe 245
Cdd:COG2226    9 DGREALLAALGLRpGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL---NVEFVVGDAEDLP- 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919009282 246 IWTDSFDLVLIFDACHDQCRPDLCIREIQRVLKIFGVFAILEIN 289
Cdd:COG2226   83 FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
183-278 2.03e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.15  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  183 VLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQRKTKSGAafnNLEFIQCDAGKMPEIwTDSFDLVLIFDACHD 262
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL---NVEFVQGDAEDLPFP-DGSFDLVVSSGVLHH 75
                          90
                  ....*....|....*...
gi 919009282  263 QCRPDL--CIREIQRVLK 278
Cdd:pfam13649  76 LPDPDLeaALREIARVLK 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
173-285 2.98e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 78.42  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 173 VEKLETGGmRVLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQRKTKSGAAfnNLEFIQCDAGKMPEIWTDSFD 252
Cdd:COG0500   21 LERLPKGG-RVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG--NVEFLVADLAELDPLPAESFD 96
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 919009282 253 LVLIFDACHDQ---CRPDLcIREIQRVLKIFGVFAI 285
Cdd:COG0500   97 LVVAFGVLHHLppeEREAL-LRELARALKPGGVLLL 131
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
172-289 7.19e-17

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: 75.44  E-value: 7.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 172 VVEKLETGGMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRktksgAAFNNLEFIQCDAGKMPeIWTDSF 251
Cdd:COG2227   17 LLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARER-----AAELNVDFVQGDLEDLP-LEDGSF 88
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919009282 252 DLVLIFDACHDQCRPDLCIREIQRVLKIFGVFAILEIN 289
Cdd:COG2227   89 DLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
184-285 1.07e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 73.85  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  184 LDVGCGGGSHSSLLAEQYPkaHFVGLEIGEDAIRQAKQRKTKSGaafnnLEFIQCDAGKMPeiWTD-SFDLVLIFDACHD 262
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREG-----LTFVVGDAEDLP--FPDnSFDLVLSSEVLHH 71
                          90       100
                  ....*....|....*....|...
gi 919009282  263 QCRPDLCIREIQRVLKIFGVFAI 285
Cdd:pfam08241  72 VEDPERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
179-285 2.12e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 70.62  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 179 GGMRVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRktksgaaFNNLEFIQCDAGKMPeiWTDSFDLVLIFD 258
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR-------LPNVRFVVADLRDLD--PPEPFDLVVSNA 71
                         90       100
                 ....*....|....*....|....*..
gi 919009282 259 ACHDQCRPDLCIREIQRVLKIFGVFAI 285
Cdd:COG4106   72 ALHWLPDHAALLARLAAALAPGGVLAV 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
172-285 2.02e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 69.57  E-value: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 172 VVEKLE-TGGMRVLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAGKMPeiWTDS 250
Cdd:COG2230   43 ILRKLGlKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRDLP--ADGQ 118
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919009282 251 FDLVLIFDA-CH--DQCRPDLcIREIQRVLKIFGVFAI 285
Cdd:COG2230  119 FDAIVSIGMfEHvgPENYPAY-FAKVARLLKPGGRLLL 155
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
180-287 4.73e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 70.18  E-value: 4.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQYPK-AHFVGLEIGEDAIRQAKQRKTKSGAaFNNLEFIQCDAGKMPeIWTDSFDLVLI-F 257
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAVGREKLRDLGL-SGNVEFVQGDAEALP-FPDNSFDAVTIaF 129
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 919009282 258 ------DachdqcrPDLCIREIQRVLKIFGVFAILE 287
Cdd:PRK00216 130 glrnvpD-------IDKALREMYRVLKPGGRLVILE 158
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
184-283 3.52e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 64.31  E-value: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  184 LDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQR-KTKSGAAFNNLEFIQCDAGKMPEIwtdSFDLVLIFDACHD 262
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERlAALGLLNAVRVELFQLDLGELDPG---SFDVVVASNVLHH 77
                          90       100
                  ....*....|....*....|.
gi 919009282  263 QCRPDLCIREIQRVLKIFGVF 283
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
168-284 1.50e-12

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: 66.16  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  168 IGHGVVEKLETGGM----RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKsgaafnNLEFIQCDAGKM 243
Cdd:TIGR02072  19 MAKRLLALLKEKGIfipaSVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSE------NVQFICGDAEKL 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 919009282  244 PeIWTDSFDLV---LIFDACHDqcrPDLCIREIQRVLKIFGVFA 284
Cdd:TIGR02072  93 P-LEDSSFDLIvsnLALQWCDD---LSQALSELARVLKPGGLLA 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
182-285 3.08e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.06  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 182 RVLDVGCGGGsHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAafNNLEFIQCDAGKMPEIWTDSFDLVLIFDACH 261
Cdd:cd02440    1 RVLDLGCGTG-ALALALASGPGARVTGVDISPVALELARKAAAALLA--DNVEVLKGDAEELPPEADESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*
gi 919009282 262 DQCRPDLC-IREIQRVLKIFGVFAI 285
Cdd:cd02440   78 HLVEDLARfLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
180-312 8.53e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 58.02  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQY-PKAHFVGLEIGEDAIRQAKQRKTKSGAafnNLEFIQCDAGKMPeIWTDSFDLVLI-- 256
Cdd:PRK08317  20 GDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGLGP---NVEFVRGDADGLP-FPDGSFDAVRSdr 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919009282 257 -FDACHDqcrPDLCIREIQRVLKIFGVFAILE-------INSSgnvhnDRAnmgSMAALLHGRS 312
Cdd:PRK08317  96 vLQHLED---PARALAEIARVLRPGGRVVVLDtdwdtlvWHSG-----DRA---LMRKILNFWS 148
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
182-285 3.20e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 55.39  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 182 RVLDVGCGGGSHSSLLAEQYpkAHFVGLEIGEDAIRQAKQRKTKSgaafnnlEFIQCDAGKMPEIwTDSFDLVLIFDACH 261
Cdd:COG4976   49 RVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGVYD-------RLLVADLADLAEP-DGRFDLIVAADVLT 118
                         90       100
                 ....*....|....*....|....
gi 919009282 262 DQCRPDLCIREIQRVLKIFGVFAI 285
Cdd:COG4976  119 YLGDLAAVFAGVARALKPGGLFIF 142
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
180-255 8.47e-09

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 55.15  E-value: 8.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQrktksGAAFNNLE----FIQCDAGKMPEIW-TDSFDLV 254
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARR-----NVALNGLEdritVIHGDLKEFAAELpPGSFDLV 112

                 .
gi 919009282 255 L 255
Cdd:COG4123  113 V 113
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
180-255 7.02e-08

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: 52.30  E-value: 7.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919009282  180 GMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRKTKSGAafnNLEFIQCDAGKMPEIWTDSFDLVL 255
Cdd:TIGR01983  47 GLRVLDVGCGGGLLSEPLARL--GANVTGIDASEENIEVAKLHAKKDPL---QIDYRCTTVEDLAEKKAGSFDVVT 117
PRK14968 PRK14968
putative methyltransferase; Provisional
176-255 1.99e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.28  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 176 LETGGMRVLDVGCGGGSHSSLLAEqypKAHFV-GLEIGEDAIRQAKQRKTKSGAAFNNLEFIQCDAgkMPEIWTDSFDLV 254
Cdd:PRK14968  20 VDKKGDRVLEVGTGSGIVAIVAAK---NGKKVvGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDL--FEPFRGDKFDVI 94

                 .
gi 919009282 255 L 255
Cdd:PRK14968  95 L 95
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
183-240 2.81e-07

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 50.14  E-value: 2.81e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919009282 183 VLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAafNNLEFIQCDA 240
Cdd:COG0220   36 VLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGL--TNVRLLRGDA 91
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
183-252 2.89e-06

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 47.08  E-value: 2.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 183 VLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAafNNLEFIQCDAgkmPEIWTDSFD 252
Cdd:PRK00121  44 HLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGL--TNLRLLCGDA---VEVLLDMFP 108
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
182-283 5.23e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 47.21  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 182 RVLDVGCGGGSHSSLLAEQYPKAH---FVGLEIGEDAIRQAKQRktksgaaFNNLEFIQCDAGKMPeIWTDSFDLVL-IF 257
Cdd:PRK11088  88 ALLDIGCGEGYYTHALADALPEITtmqLFGLDISKVAIKYAAKR-------YPQVTFCVASSHRLP-FADQSLDAIIrIY 159
                         90       100
                 ....*....|....*....|....*.
gi 919009282 258 DACHDQcrpdlcirEIQRVLKIFGVF 283
Cdd:PRK11088 160 APCKAE--------ELARVVKPGGIV 177
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
180-260 6.90e-06

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 47.31  E-value: 6.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQYP-KAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDAGKMPEIWTDSFDLVLIfD 258
Cdd:COG0144  250 GERVLDLCAAPGGKTLHLAELMGnKGRVVAVDISEHRLKRLRENLARLG--LSNVEVVVADARELLEWLPGKFDRVLL-D 326

                 ...
gi 919009282 259 A-C 260
Cdd:COG0144  327 ApC 329
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
180-245 1.32e-05

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 46.79  E-value: 1.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAFNnleFIQCDAGKMPE 245
Cdd:PRK06922 419 GDTIVDVGAGGGVMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRSWN---VIKGDAINLSS 481
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
182-257 1.63e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 45.32  E-value: 1.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919009282 182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRktksgaaFNNLEFIQCDAGKmpeiWTDSFDLVLIF 257
Cdd:PRK01683  34 YVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSR-------LPDCQFVEADIAS----WQPPQALDLIF 98
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
182-255 2.08e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.12  E-value: 2.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919009282  182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQrktksGAAFNNLEFIQCDAGKMPEIWTD-SFDLVL 255
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARE-----NLAANGLENGEVVASDVYSGVEDgKFDLII 103
arsM PRK11873
arsenite methyltransferase;
180-288 3.09e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.55  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQY-PKAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDAGKMPeIWTDSFDlvLIFD 258
Cdd:PRK11873  78 GETVLDLGSGGGFDCFLAARRVgPTGKVIGVDMTPEMLAKARANARKAG--YTNVEFRLGEIEALP-VADNSVD--VIIS 152
                         90       100       110
                 ....*....|....*....|....*....|..
gi 919009282 259 ACHDQCRPD--LCIREIQRVLKIFGVFAILEI 288
Cdd:PRK11873 153 NCVINLSPDkeRVFKEAFRVLKPGGRFAISDV 184
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
177-260 3.73e-05

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 42.94  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  177 ETGGMRVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCD-AGKMPEIWTDSFDLVL 255
Cdd:pfam13679  23 ENGPITIVDHGAGKGYLGFILYYLKYGVRVYGIDTRAELVEKANALAQKLGFN-KRMSFLEGTiAGSTPVELPDRVDVVT 101

                  ....*
gi 919009282  256 IFDAC 260
Cdd:pfam13679 102 ALHAC 106
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
182-259 5.37e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 42.86  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 182 RVLDVGCGGGsHSSL-LAEQYPK-AHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAGK-MPEIWTDSFDLVLIfD 258
Cdd:COG4122   19 RILEIGTGTG-YSTLwLARALPDdGRLTTIEIDPERAAIARENFARAGLA-DRIRLILGDALEvLPRLADGPFDLVFI-D 95

                 .
gi 919009282 259 A 259
Cdd:COG4122   96 A 96
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
182-255 6.06e-05

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: 43.25  E-value: 6.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919009282 182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAkqRKTKSGAAFNNLEFIQCDAGKmpEIWTDSFDLVL 255
Cdd:COG2813   52 RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELA--RANAAANGLENVEVLWSDGLS--GVPDGSFDLIL 121
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
183-240 8.65e-05

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 42.28  E-value: 8.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 919009282  183 VLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGaaFNNLEFIQCDA 240
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALG--LQNLRILCGNA 60
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
180-258 1.07e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.90  E-value: 1.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAgkmpEIWTDSFDLVLIFD 258
Cdd:PRK07580  64 GLRILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPEAGLA-GNITFEVGDL----ESLLGRFDTVVCLD 135
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
180-276 1.59e-04

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: 41.97  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  180 GMRVLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQRktksgaafnNLEFIQCDAGKMPEIWTD-SFDLVLIFD 258
Cdd:TIGR02081  14 GSRVLDLGCGDGELLALLRDEK-QVRGYGIEIDQDGVLACVAR---------GVNVIQGDLDEGLEAFPDkSFDYVILSQ 83
                          90
                  ....*....|....*...
gi 919009282  259 ACHDQCRPDLCIREIQRV 276
Cdd:TIGR02081  84 TLQATRNPEEILDEMLRV 101
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
172-222 5.07e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 41.37  E-value: 5.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 919009282 172 VVEKLE-TGGMRVLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQR 222
Cdd:PRK11705 159 ICRKLQlKPGMRVLDIGCGWGGLARYAAEHY-GVSVVGVTISAEQQKLAQER 209
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
180-227 6.70e-04

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: 40.77  E-value: 6.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 919009282  180 GMRVLDVGCGGGSHSSLLAEQYpKAHFVGLEIGEDAIRQAKQRKTKSG 227
Cdd:pfam02353  62 GMTLLDIGCGWGGLMRRAAERY-DVNVVGLTLSKNQYKLARKRVAAEG 108
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
180-273 6.80e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGShSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCdagkmpeiwtDSFDLVLifda 259
Cdd:COG4076   36 GDVVLDIGTGSGL-LSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLS-DRITVINA----------DATDLDL---- 99
                         90
                 ....*....|....
gi 919009282 260 chdQCRPDLCIREI 273
Cdd:COG4076  100 ---PEKADVIISEM 110
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
180-291 7.65e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 40.26  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAEQY-PKAHFVGLEIGEDAIRQAKQRKT-KSGAAFNNLEFIQCDAGKMPeiWTD-SFDLVLI 256
Cdd:PLN02233  74 GDRVLDLCCGSGDLAFLLSEKVgSDGKVMGLDFSSEQLAVAASRQElKAKSCYKNIEWIEGDATDLP--FDDcYFDAITM 151
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 919009282 257 FDACHDQCRPDLCIREIQRVLKIFGVFAILEINSS 291
Cdd:PLN02233 152 GYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKS 186
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
182-261 8.93e-04

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 40.09  E-value: 8.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282   182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAGKMPEiwTDSFDLVLIFDACH 261
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQ-GRIRIFYRDSAKDPF--PDTYDLVFGFEVIH 78
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
180-276 1.03e-03

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: 39.36  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  180 GMRVLDVGCGGGSHSSLLAEQYPKAHFvGLEIGEDAIRQAKQRktksgaafnNLEFIQCDAGKMPEIWTD-SFDLVLIFD 258
Cdd:pfam07021  14 GSRVLDLGCGDGTLLYLLKEEKGVDGY-GIELDAAGVAECVAK---------GLYVIQGDLDEGLEHFPDkSFDYVILSQ 83
                          90
                  ....*....|....*...
gi 919009282  259 ACHDQCRPDLCIREIQRV 276
Cdd:pfam07021  84 TLQATRNPREVLDEMLRI 101
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
182-255 1.06e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919009282 182 RVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAAfNNLEFIQCDAGKmPEIWTDSFDLVL 255
Cdd:COG2890  115 RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLE-DRVRFLQGDLFE-PLPGDGRFDLIV 186
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
175-285 1.78e-03

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 39.72  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282  175 KLETGGMRVLDVGCGGGShsSLLAEQYPK-AHFVGLEIGEDAIRQAKQR--KTKSGAAFNNL----EFIQCDAGK--MPE 245
Cdd:pfam03291  59 FQNSNKRKVLDLGCGKGG--DLEKWFKGGiSQLIGTDIAEVSIEQCRERynKLRSGNKSKYYkfdaEFITGDCFVssLRE 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 919009282  246 IWTD---SFDLVLIFDACH----DQCRPDLCIREIQRVLKIFGVFAI 285
Cdd:pfam03291 137 VFEDpfgKFDIVSCQFAIHysfeSEEKARTMLRNVAELLASGGVFIG 183
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
180-255 2.18e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.73  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGS---HSSLL-AEQypkahFVGLEIGEDAIRQAKQrktKSGAAFNNLEFIQCDAGKMPEIwtDSFDLVL 255
Cdd:COG2263   46 GKTVLDLGCGTGMlaiGAALLgAKK-----VVGVDIDPEALEIARE---NAERLGVRVDFIRADVTRIPLG--GSVDTVV 115
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
168-254 3.15e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.60  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 168 IGHGVVEKLETGGMRVLDVGCGGG----ShsslLAEQYPKAHFVGLEIGEDAIRQAKqRKTKSGAAfNNLEFIQCDAgkM 243
Cdd:PRK09328  97 VEWALEALLLKEPLRVLDLGTGSGaialA----LAKERPDAEVTAVDISPEALAVAR-RNAKHGLG-ARVEFLQGDW--F 168
                         90
                 ....*....|.
gi 919009282 244 PEIWTDSFDLV 254
Cdd:PRK09328 169 EPLPGGRFDLI 179
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
180-239 4.05e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.73  E-value: 4.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919009282  180 GMRVLDVGCGGGSHSSLLAEQY-PKAHFVGLEIGEDAIRQAKQRKTKSGAAfnNLEFIQCD 239
Cdd:pfam01135  74 GMRVLEIGSGSGYLTACFARMVgEVGRVVSIEHIPELVEIARRNLEKLGLE--NVIVVVGD 132
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
173-256 5.01e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 37.29  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 173 VEKLE-TGGMRVLDVGCGGGSHSSLLAEQYPKAHFVGLEIGEDAIRQAKQRKTKSGAafNNLEFIqcdAGKMPEIWTDSF 251
Cdd:PRK08287  24 LSKLElHRAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGC--GNIDII---PGEAPIELPGKA 98

                 ....*
gi 919009282 252 DLVLI 256
Cdd:PRK08287  99 DAIFI 103
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
146-240 5.63e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.38  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 146 YFMGKMSQALHEKhvitdmlpdighgvvekletGGMRVLDVGCGGGSHSSLLAEQypKAHFVGLEIGEDAIRQAKQRKTK 225
Cdd:COG2518   53 YIVARMLEALDLK--------------------PGDRVLEIGTGSGYQAAVLARL--AGRVYSVERDPELAERARERLAA 110
                         90
                 ....*....|....*
gi 919009282 226 SGaaFNNLEFIQCDA 240
Cdd:COG2518  111 LG--YDNVTVRVGDG 123
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
180-286 6.79e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 36.85  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGshsSLLAE-QYPKAHFVGLEIGEDAIRQAKQrktksgaafnNLEF--------IQCDAGKMPeIWTDS 250
Cdd:COG1041   27 GDTVLDPFCGTG---TILIEaGLLGRRVIGSDIDPKMVEGARE----------NLEHygyedadvIRGDARDLP-LADES 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 919009282 251 FDLVlIFDA----CHDQCRPDLC------IREIQRVLKIFGVFAIL 286
Cdd:COG1041   93 VDAI-VTDPpygrSSKISGEELLelyekaLEEAARVLKPGGRVVIV 137
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
180-287 7.40e-03

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 37.59  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919009282 180 GMRVLDVGCGGGSHSSLLAeQY--PKAHFVGL---------EIGEDAIRQAKQRKTKSGAAFNNLEFIQCDAGKMPEIWT 248
Cdd:COG4798   67 GMTVVEIWPGGGWYTEILA-PYlgPKGKVYAAnfdpdseppEYAKRSREAFSAKLAADPALYGNVRVTAFAPPDDPIAPP 145
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 919009282 249 DSFDLVLIFDACHDQCR---PDLCIREIQRVLKIFGVFAILE 287
Cdd:COG4798  146 GSADLVLTFRNYHNWYRagdAAAMFAAFFKALKPGGVLGVVD 187
 
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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