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Conserved domains on  [gi|497370540|ref|WP_009684753|]
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MULTISPECIES: carboxy-S-adenosyl-L-methionine synthase CmoA [Pseudomonas]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 6-246 4.61e-108

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.).


The actual alignment was detected with superfamily member TIGR00740:

Pssm-ID: 473071  Cd Length: 239  Bit Score: 311.56  E-value: 4.61e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540    6 DRLFAQPLEQVPDFVFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAARFAQPHTALYDLGASLGAVTQSLRRHVRSDGCR 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   86 VIAVDNSAAMVERCRQYLTAqdsmFQELLPVQVLEADILALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  166 ILSEKLRFADEQAQDLLNELHLDFKRANGYSELEIAQKRSAIENVMRPDTLETHQERLLAAGFSKVVPWFQCLNFASLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 497370540  246 L 246
Cdd:TIGR00740 238 L 238
 
Name Accession Description Interval E-value
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 6-246 4.61e-108

tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, in preparing the uridine-5-oxyacetic acid (cmo5U) at position 34. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273244  Cd Length: 239  Bit Score: 311.56  E-value: 4.61e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540    6 DRLFAQPLEQVPDFVFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAARFAQPHTALYDLGASLGAVTQSLRRHVRSDGCR 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   86 VIAVDNSAAMVERCRQYLTAqdsmFQELLPVQVLEADILALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  166 ILSEKLRFADEQAQDLLNELHLDFKRANGYSELEIAQKRSAIENVMRPDTLETHQERLLAAGFSKVVPWFQCLNFASLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 497370540  246 L 246
Cdd:TIGR00740 238 L 238
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
6-246 1.13e-91

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 270.36  E-value: 1.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   6 DRLFAQPLEQVPDFVFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAARFAQPHTALYDLGASLGAVTQSLRRHVRSDGCR 85
Cdd:PRK15451   5 DTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  86 VIAVDNSAAMVERCRQYLTAqdsmFQELLPVQVLEADILALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGAL 165
Cdd:PRK15451  85 IIAIDNSPAMIERCRRHIDA----YKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540 166 ILSEKLRFADEQAQDLLNELHLDFKRANGYSELEIAQKRSAIENVMRPDTLETHQERLLAAGFSKVVPWFQCLNFASLIA 245
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 .
gi 497370540 246 L 246
Cdd:PRK15451 241 L 241
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-169 3.76e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.88  E-value: 3.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  57 PHTALYDLGASLGAVTQSLRRhvRSDGCRVIAVDNSAAMVERCRQYLTaqdsmfqellPVQVLEADILALPF-EPASVVA 135
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAE--RFPGARVTGVDLSPEMLARARARLP----------NVRFVVADLRDLDPpEPFDLVV 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 497370540 136 MNFTLQFIapDQRLALLARIRQALLPGGALILSE 169
Cdd:COG4106   69 SNAALHWL--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-163 4.34e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.14  E-value: 4.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   63 DLGASLGAVTQSLRRHVrsdGCRVIAVDNSAAMVERCRQYLTAQDsmfqelLPVQVLEADILALPFEPAS--VVAMNFTL 140
Cdd:pfam13649   3 DLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAG------LNVEFVQGDAEDLPFPDGSfdLVVSSGVL 73

                          90       100
                  ....*....|....*....|...
gi 497370540  141 QFIAPDQRLALLARIRQALLPGG 163
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-168 8.83e-11

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: 57.44  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  61 LYDLGASLGAVTQSLRRHVrsdGCRVIAVDNSAAMVERCRQYLTAqdsmfQELLPVQVLEADILALPF---EPASVVAMN 137
Cdd:cd02440    2 VLDLGCGTGALALALASGP---GARVTGVDISPVALELARKAAAA-----LLADNVEVLKGDAEELPPeadESFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497370540 138 FTLQFIAPDQRlALLARIRQALLPGGALILS 168
Cdd:cd02440   74 PPLHHLVEDLA-RFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 6-246 4.61e-108

tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, in preparing the uridine-5-oxyacetic acid (cmo5U) at position 34. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273244  Cd Length: 239  Bit Score: 311.56  E-value: 4.61e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540    6 DRLFAQPLEQVPDFVFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAARFAQPHTALYDLGASLGAVTQSLRRHVRSDGCR 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   86 VIAVDNSAAMVERCRQYLTAqdsmFQELLPVQVLEADILALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  166 ILSEKLRFADEQAQDLLNELHLDFKRANGYSELEIAQKRSAIENVMRPDTLETHQERLLAAGFSKVVPWFQCLNFASLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 497370540  246 L 246
Cdd:TIGR00740 238 L 238
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
6-246 1.13e-91

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 270.36  E-value: 1.13e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   6 DRLFAQPLEQVPDFVFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAARFAQPHTALYDLGASLGAVTQSLRRHVRSDGCR 85
Cdd:PRK15451   5 DTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  86 VIAVDNSAAMVERCRQYLTAqdsmFQELLPVQVLEADILALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGAL 165
Cdd:PRK15451  85 IIAIDNSPAMIERCRRHIDA----YKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540 166 ILSEKLRFADEQAQDLLNELHLDFKRANGYSELEIAQKRSAIENVMRPDTLETHQERLLAAGFSKVVPWFQCLNFASLIA 245
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 .
gi 497370540 246 L 246
Cdd:PRK15451 241 L 241
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
57-169 3.76e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.88  E-value: 3.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  57 PHTALYDLGASLGAVTQSLRRhvRSDGCRVIAVDNSAAMVERCRQYLTaqdsmfqellPVQVLEADILALPF-EPASVVA 135
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAE--RFPGARVTGVDLSPEMLARARARLP----------NVRFVVADLRDLDPpEPFDLVV 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 497370540 136 MNFTLQFIapDQRLALLARIRQALLPGGALILSE 169
Cdd:COG4106   69 SNAALHWL--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-163 4.34e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.14  E-value: 4.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   63 DLGASLGAVTQSLRRHVrsdGCRVIAVDNSAAMVERCRQYLTAQDsmfqelLPVQVLEADILALPFEPAS--VVAMNFTL 140
Cdd:pfam13649   3 DLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAG------LNVEFVQGDAEDLPFPDGSfdLVVSSGVL 73

                          90       100
                  ....*....|....*....|...
gi 497370540  141 QFIAPDQRLALLARIRQALLPGG 163
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 49-184 6.28e-18

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: 77.73  E-value: 6.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  49 VLAARFAQPHTALYDLGASLGAVTQSLRRHvrsdGCRVIAVDNSAAMVERCRQYLTAQDsmfqelLPVQVLEADILALPF 128
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAG------LNVEFVVGDAEDLPF 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497370540 129 EPAS--VVAMNFTLQFIaPDQRLAlLARIRQALLPGGALILSEKLRFADEQAQDLLNE 184
Cdd:COG2226   84 PDGSfdLVISSFVLHHL-PDPERA-LAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-168 2.27e-14

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: 67.74  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  49 VLAARFAQPHTALyDLGASLGAVTQSLRRHvrsdGCRVIAVDNSAAMVERCRQYLTAqdsmfqelLPVQVLEADILALPF 128
Cdd:COG2227   17 LLARLLPAGGRVL-DVGCGTGRLALALARR----GADVTGVDISPEALEIARERAAE--------LNVDFVQGDLEDLPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 497370540 129 EPAS--VVAMNFTLQFIaPDQRlALLARIRQALLPGGALILS 168
Cdd:COG2227   84 EDGSfdLVICSEVLEHL-PDPA-ALLRELARLLKPGGLLLLS 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-167 1.77e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.53  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   63 DLGASLGAVTQSLRRHvrsdGCRVIAVDNSAAMVERCRQYLTAQdsmfqellPVQVLEADILALPFEPAS--VVAMNFTL 140
Cdd:pfam08241   2 DVGCGTGLLTELLARL----GARVTGVDISPEMLELAREKAPRE--------GLTFVVGDAEDLPFPDNSfdLVLSSEVL 69

                          90       100
                  ....*....|....*....|....*..
gi 497370540  141 QFIAPDQRlaLLARIRQALLPGGALIL 167
Cdd:pfam08241  70 HHVEDPER--ALREIARVLKPGGILII 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 44-168 3.73e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 60.70  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  44 VENLGVLAARFAQPHTALyDLGASLGAVTQSLRRHVRSdgcRVIAVDNSAAMVERCRQYLTAqdsmfQELLPVQVLEADI 123
Cdd:COG0500   14 LAALLALLERLPKGGRVL-DLGCGTGRNLLALAARFGG---RVIGIDLSPEAIALARARAAK-----AGLGNVEFLVADL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 497370540 124 ---LALPFEPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGALILS 168
Cdd:COG0500   85 aelDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLS 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-168 8.83e-11

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: 57.44  E-value: 8.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  61 LYDLGASLGAVTQSLRRHVrsdGCRVIAVDNSAAMVERCRQYLTAqdsmfQELLPVQVLEADILALPF---EPASVVAMN 137
Cdd:cd02440    2 VLDLGCGTGALALALASGP---GARVTGVDISPVALELARKAAAA-----LLADNVEVLKGDAEELPPeadESFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497370540 138 FTLQFIAPDQRlALLARIRQALLPGGALILS 168
Cdd:cd02440   74 PPLHHLVEDLA-RFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
49-204 7.29e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.85  E-value: 7.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  49 VLAARFAQPHTALYDLGASLGAVTQSLRRHVRsdgcRVIAVDNSAAMVERCRqyltaqdsmfQELLPVQVLEADILALPF 128
Cdd:COG4976   38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGY----RLTGVDLSEEMLAKAR----------EKGVYDRLLVADLADLAE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540 129 EPAS--VVAMNFTLQFIApDQRlALLARIRQALLPGGALILS-----EKLRFA--DEQAQDLLNELHLDFkrangYSELE 199
Cdd:COG4976  104 PDGRfdLIVAADVLTYLG-DLA-AVFAGVARALKPGGLFIFSvedadGSGRYAhsLDYVRDLLAAAGFEV-----PGLLV 176


                 ....*
gi 497370540 200 IAQKR 204
Cdd:COG4976  177 VARKP 181
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 56-167 6.10e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 6.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  56 QPHTALYDLGASLGAvtqSLRRHVRSDGCRVIAVDNSAAMVERCRQYLTAQDSMFQellpVQVLEADILALPF-EPASVV 134
Cdd:COG2230   50 KPGMRVLDIGCGWGG---LALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADR----VEVRLADYRDLPAdGQFDAI 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 497370540 135 AMNFTLQFIAPDQRLALLARIRQALLPGGALIL 167
Cdd:COG2230  123 VSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
PRK08317 PRK08317
hypothetical protein; Provisional
 63-169 6.39e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.86  E-value: 6.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  63 DLGASLGAVTQSLRRHVRSDGcRVIAVDNSAAMVErcrqylTAQDSMFQELLPVQVLEADILALPFEPAS---VVAMNfT 139
Cdd:PRK08317  25 DVGCGPGNDARELARRVGPEG-RVVGIDRSEAMLA------LAKERAAGLGPNVEFVRGDADGLPFPDGSfdaVRSDR-V 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 497370540 140 LQFIA-PDQRLALLARIrqaLLPGGALILSE 169
Cdd:PRK08317  97 LQHLEdPARALAEIARV---LRPGGRVVVLD 124
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 49-171 2.33e-05

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 43.93  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   49 VLAARFAQPHTALYDLGASLGAVTQSLRRHVrsDGCRVIAVDnSAAMVERCRQYLTAqdsmfQELLPVQVLEADILALPF 128
Cdd:pfam00891  52 VLTAFDLSGFRSLVDVGGGTGALAQAIVSLY--PGCKGIVFD-LPHVVEAAPTHFSA-----GEEPRVTFHGGDFFKDSL 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 497370540  129 EPASVVAMNFTLQFIAPDQRLALLARIRQALLPGGALILSEKL 171
Cdd:pfam00891 124 PEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGKVILVESL 166
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 55-165 1.74e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 41.85  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  55 AQ-PHTAL---YDLGASLGAVTQSLrrHVRSDGCRVIAVDNSAAMVERCRQYLTAQDsmfqellpvqVLEADILA-LPFE 129
Cdd:PRK01683  25 ARvPLENPryvVDLGCGPGNSTELL--VERWPAARITGIDSSPAMLAEARSRLPDCQ----------FVEADIASwQPPQ 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 497370540 130 PASVVAMNFTLQFIaPDQrLALLARIRQALLPGGAL 165
Cdd:PRK01683  93 ALDLIFANASLQWL-PDH-LELFPRLVSLLAPGGVL 126
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-184 2.44e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.09  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   57 PHTALYDLGASLGAVTQSLRRHVRSDGcRVIAVDNSAAMVERCRQylTAQDSMFQEllpVQVLEADILALP--FEPAS-- 132
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNA-EVVGIDISEEAIEKARE--NAQKLGFDN---VEFEQGDIEELPelLEDDKfd 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 497370540  133 VVAMNFTLQFIaPDQRLALLaRIRQALLPGGALILSEkLRFADEQAQDLLNE 184
Cdd:pfam13847  77 VVISNCVLNHI-PDPDKVLQ-EILRVLKPGGRLIISD-PDSLAELPAHVKED 125
COG4301 COG4301
Uncharacterized protein, contains predicted SAM-dependent methyltransferase domain [General ...
 40-167 5.53e-04

Uncharacterized protein, contains predicted SAM-dependent methyltransferase domain [General function prediction only];


Pssm-ID: 443442  Cd Length: 316  Bit Score: 40.48  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  40 YPTIVEnLGVLA------ARFAQPHTALYDLGASLGAVTQSLRRHVRSDgCRVIAVDNSAAMVERcrqyltAQDSMFQEL 113
Cdd:COG4301   54 YPTRTE-LAILRrhaaeiAALLGPGATLVELGSGSSTKTRLLLDALGRP-AAYVPIDISGEALEE------AAERLAADY 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497370540 114 --LPVQVLEADI---LALPFEPAS---VVAM------NFTlqfiaPDQRLALLARIRQALLPGGALIL 167
Cdd:COG4301  126 pgLEVHPVVADFtrpLALPAGLAAgrrLVFFpgstigNFT-----PEEALAFLRRLRALLGPGDGLLI 188
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 63-167 1.04e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 39.37  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540  63 DLGASLGAVTQSLRRHVRSDGcRVIAVDNSAAMVERCRQYLTAQDSMfqelLPVQVLEADILALPFEPAS--VVAMNFTL 140
Cdd:PRK00216  57 DLACGTGDLAIALAKAVGKTG-EVVGLDFSEGMLAVGREKLRDLGLS----GNVEFVQGDAEALPFPDNSfdAVTIAFGL 131

                         90       100
                 ....*....|....*....|....*....
gi 497370540 141 Q-FIAPDQRLALLARIrqaLLPGG-ALIL 167
Cdd:PRK00216 132 RnVPDIDKALREMYRV---LKPGGrLVIL 157
Methyltransf_33 pfam10017
Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family ...
 40-168 2.47e-03

Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family are expressed from part of the ergothioneine biosynthetic gene cluster. EGTD is the histidine methyltransferase that transfers three methyl groups to the alpha-amino moiety of histidine, in the first stage of the production of this histidine betaine derivative that carries a thiol group attached to the C2 atom of an imidazole ring.


Pssm-ID: 462944  Cd Length: 304  Bit Score: 38.22  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497370540   40 YPTIVEnLGVL---AARFAQ--PHTALYDLGASLGAVTQSLRRHVRSDGCRV--IAVDNSAAMVERCRQYLTAQdsmFQE 112
Cdd:pfam10017  40 YPTRTE-IAILrrhAAEIAAliPAAVLVELGSGSSRKTRLLLDALPAAGKPVtyVPIDISAEALEESAAALAAD---YPG 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497370540  113 LlPVQVLEAD----ILALPFEPASVVAM--------NFTlqfiaPDQRLALLARIRQALLPGGALILS 168
Cdd:pfam10017 116 L-TVHGLVGDyedgLARLPPAGGGPRLVlflgstigNFT-----PDEAAAFLRRIRAALGPGDLLLLG 177
 
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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