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Conserved domains on  [gi|492055370|ref|WP_005735111|]
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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 1.98e-105

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: 305.01  E-value: 1.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370    6 DRIFAQPLAQVPDFAFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRSEGCE 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   86 VIAIDNSSAMVERCREYLNAqnsmFQELLPVQVIEGDILALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  166 ILSEKLRFDDEQEHALLTDLHIAFKRANGYSDLEIAQKRSAIENVMKPDSLEEHRQRLLAAGFSKVVPWFQCLNFTSLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 492055370  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 1.98e-105

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: 305.01  E-value: 1.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370    6 DRIFAQPLAQVPDFAFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRSEGCE 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   86 VIAIDNSSAMVERCREYLNAqnsmFQELLPVQVIEGDILALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  166 ILSEKLRFDDEQEHALLTDLHIAFKRANGYSDLEIAQKRSAIENVMKPDSLEEHRQRLLAAGFSKVVPWFQCLNFTSLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 492055370  246 L 246
Cdd:TIGR00740 238 L 238
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
6-246 1.45e-87

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


Pssm-ID: 185348  Cd Length: 247  Bit Score: 259.96  E-value: 1.45e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   6 DRIFAQPLAQVPDFAFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRSEGCE 85
Cdd:PRK15451   5 DTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  86 VIAIDNSSAMVERCREYLNAqnsmFQELLPVQVIEGDILALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGAL 165
Cdd:PRK15451  85 IIAIDNSPAMIERCRRHIDA----YKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370 166 ILSEKLRFDDEQEHALLTDLHIAFKRANGYSDLEIAQKRSAIENVMKPDSLEEHRQRLLAAGFSKVVPWFQCLNFTSLIA 245
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 .
gi 492055370 246 L 246
Cdd:PRK15451 241 L 241
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-169 6.68e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.50  E-value: 6.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  56 QPDTVLyDLGSSLGAVTQALRRhvRSEGCEVIAIDNSSAMVERCREYLNaqnsmfqellPVQVIEGDILALEF-KPASVV 134
Cdd:COG4106    1 PPRRVL-DLGCGTGRLTALLAE--RFPGARVTGVDLSPEMLARARARLP----------NVRFVVADLRDLDPpEPFDLV 67

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 492055370 135 ALNFTLQFIapEQRLTLLGRIRDALVPGGALILSE 169
Cdd:COG4106   68 VSNAALHWL--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-163 5.59e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.45  E-value: 5.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   60 VLyDLGSSLGAVTQALRRHVrseGCEVIAIDNSSAMVERCREYLNAQNsmfqelLPVQVIEGDILALEFKPAS--VVALN 137
Cdd:pfam13649   1 VL-DLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAG------LNVEFVQGDAEDLPFPDGSfdLVVSS 70

                          90       100
                  ....*....|....*....|....*.
gi 492055370  138 FTLQFIAPEQRLTLLGRIRDALVPGG 163
Cdd:pfam13649  71 GVLHHLPDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-168 7.88e-10

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: 54.74  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  61 LYDLGSSLGAVTQALRRHvrsEGCEVIAIDNSSAMVERCREYLNAqnsmfQELLPVQVIEGDILALEFKP---ASVVALN 137
Cdd:cd02440    2 VLDLGCGTGALALALASG---PGARVTGVDISPVALELARKAAAA-----LLADNVEVLKGDAEELPPEAdesFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492055370 138 FTLQFIAPEQRLtLLGRIRDALVPGGALILS 168
Cdd:cd02440   74 PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
43-135 8.41e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370    43 IVENLGVlaaqfaQPDTVLYDLGSSLGAVTQALRRHVRsegcEVIAIDNSSAMVERCREYlnaqnsmFQELLPVQVIEGD 122
Cdd:smart00650   5 IVRAANL------RPGDTVLEIGPGKGALTEELLERAK----RVTAIEIDPRLAPRLREK-------FAAADNLTVIHGD 67

                           90
                   ....*....|....*.
gi 492055370   123 ILALEF---KPASVVA 135
Cdd:smart00650  68 ALKFDLpklQPYKVVG 83
 
Name Accession Description Interval E-value
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 6-246 1.98e-105

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: 305.01  E-value: 1.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370    6 DRIFAQPLAQVPDFAFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRSEGCE 85
Cdd:TIGR00740   2 DTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNCK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   86 VIAIDNSSAMVERCREYLNAqnsmFQELLPVQVIEGDILALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGAL 165
Cdd:TIGR00740  82 IIAIDNSPAMIERCRQHIAA----YHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  166 ILSEKLRFDDEQEHALLTDLHIAFKRANGYSDLEIAQKRSAIENVMKPDSLEEHRQRLLAAGFSKVVPWFQCLNFTSLIA 245
Cdd:TIGR00740 158 VLSEKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIA 237


                  .
gi 492055370  246 L 246
Cdd:TIGR00740 238 L 238
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
6-246 1.45e-87

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


Pssm-ID: 185348  Cd Length: 247  Bit Score: 259.96  E-value: 1.45e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   6 DRIFAQPLAQVPDFAFNEDVVRVFPDMIKRSVPGYPTIVENLGVLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRSEGCE 85
Cdd:PRK15451   5 DTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHHDNCK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  86 VIAIDNSSAMVERCREYLNAqnsmFQELLPVQVIEGDILALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGAL 165
Cdd:PRK15451  85 IIAIDNSPAMIERCRRHIDA----YKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370 166 ILSEKLRFDDEQEHALLTDLHIAFKRANGYSDLEIAQKRSAIENVMKPDSLEEHRQRLLAAGFSKVVPWFQCLNFTSLIA 245
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 .
gi 492055370 246 L 246
Cdd:PRK15451 241 L 241
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-169 6.68e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.50  E-value: 6.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  56 QPDTVLyDLGSSLGAVTQALRRhvRSEGCEVIAIDNSSAMVERCREYLNaqnsmfqellPVQVIEGDILALEF-KPASVV 134
Cdd:COG4106    1 PPRRVL-DLGCGTGRLTALLAE--RFPGARVTGVDLSPEMLARARARLP----------NVRFVVADLRDLDPpEPFDLV 67

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 492055370 135 ALNFTLQFIapEQRLTLLGRIRDALVPGGALILSE 169
Cdd:COG4106   68 VSNAALHWL--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-163 5.59e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.45  E-value: 5.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   60 VLyDLGSSLGAVTQALRRHVrseGCEVIAIDNSSAMVERCREYLNAQNsmfqelLPVQVIEGDILALEFKPAS--VVALN 137
Cdd:pfam13649   1 VL-DLGCGTGRLTLALARRG---GARVTGVDLSPEMLERARERAAEAG------LNVEFVQGDAEDLPFPDGSfdLVVSS 70

                          90       100
                  ....*....|....*....|....*.
gi 492055370  138 FTLQFIAPEQRLTLLGRIRDALVPGG 163
Cdd:pfam13649  71 GVLHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 51-184 1.72e-16

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: 73.87  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  51 AAQFAQPDTVLyDLGSSLGAVTQALRRHvrseGCEVIAIDNSSAMVERCREYLNAQNsmfqelLPVQVIEGDILALEFKP 130
Cdd:COG2226   17 ALGLRPGARVL-DLGCGTGRLALALAER----GARVTGVDISPEMLELARERAAEAG------LNVEFVVGDAEDLPFPD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492055370 131 AS--VVALNFTLQFIAPEQRltLLGRIRDALVPGGALILSEKLRFDDEQEHALLTD 184
Cdd:COG2226   86 GSfdLVISSFVLHHLPDPER--ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-168 7.80e-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: 66.19  E-value: 7.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  49 VLAAQFAQPDTVLyDLGSSLGAVTQALRRHvrseGCEVIAIDNSSAMVERCREYLNAQNsmfqellpVQVIEGDILALEF 128
Cdd:COG2227   17 LLARLLPAGGRVL-DVGCGTGRLALALARR----GADVTGVDISPEALEIARERAAELN--------VDFVQGDLEDLPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492055370 129 KPAS--VVALNFTLQFIapEQRLTLLGRIRDALVPGGALILS 168
Cdd:COG2227   84 EDGSfdLVICSEVLEHL--PDPAALLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 44-168 2.48e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.09  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  44 VENLGVLAAQFAQPDTVLyDLGSSLGAVTQALRRHVRSEgceVIAIDNSSAMVERCREYLNAQNsmfqeLLPVQVIEGDI 123
Cdd:COG0500   14 LAALLALLERLPKGGRVL-DLGCGTGRNLLALAARFGGR---VIGIDLSPEAIALARARAAKAG-----LGNVEFLVADL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 492055370 124 ---LALEFKPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGALILS 168
Cdd:COG0500   85 aelDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLS 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 61-168 7.88e-10

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: 54.74  E-value: 7.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  61 LYDLGSSLGAVTQALRRHvrsEGCEVIAIDNSSAMVERCREYLNAqnsmfQELLPVQVIEGDILALEFKP---ASVVALN 137
Cdd:cd02440    2 VLDLGCGTGALALALASG---PGARVTGVDISPVALELARKAAAA-----LLADNVEVLKGDAEELPPEAdesFDVIISD 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492055370 138 FTLQFIAPEQRLtLLGRIRDALVPGGALILS 168
Cdd:cd02440   74 PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-167 9.98e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.21  E-value: 9.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   63 DLGSSLGAVTQALRRHvrseGCEVIAIDNSSAMVERCREYLNAQnsmfqellPVQVIEGDILALEFKPAS--VVALNFTL 140
Cdd:pfam08241   2 DVGCGTGLLTELLARL----GARVTGVDISPEMLELAREKAPRE--------GLTFVVGDAEDLPFPDNSfdLVLSSEVL 69

                          90       100
                  ....*....|....*....|....*..
gi 492055370  141 QFIapEQRLTLLGRIRDALVPGGALIL 167
Cdd:pfam08241  70 HHV--EDPERALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 58-167 1.68e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  58 DTVLyDLGSSLGAVTQALRRHVrseGCEVIAIDNSSAMVERCREYLNAQNSMFQellpVQVIEGDILALEFK-PASVVAL 136
Cdd:COG2230   53 MRVL-DIGCGWGGLALYLARRY---GVRVTGVTLSPEQLEYARERAAEAGLADR----VEVRLADYRDLPADgQFDAIVS 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492055370 137 NFTLQFIAPEQRLTLLGRIRDALVPGGALIL 167
Cdd:COG2230  125 IGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
PRK08317 PRK08317
hypothetical protein; Provisional
 51-169 4.05e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.25  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  51 AAQFAQPDTVLyDLGSSLGAVTQALRRHVRSEGcEVIAIDNSSAMVERcreylnAQNSMFQELLPVQVIEGDILALEFKP 130
Cdd:PRK08317  14 LLAVQPGDRVL-DVGCGPGNDARELARRVGPEG-RVVGIDRSEAMLAL------AKERAAGLGPNVEFVRGDADGLPFPD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492055370 131 AS---VVALNfTLQFIAPEQRltLLGRIRDALVPGGALILSE 169
Cdd:PRK08317  86 GSfdaVRSDR-VLQHLEDPAR--ALAEIARVLRPGGRVVVLD 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
49-204 6.69e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 6.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  49 VLAAQFAQPDTVLYDLGSSLGAVTQALRRHVRsegcEVIAIDNSSAMVERCREylnaqnsmfqELLPVQVIEGDILALEF 128
Cdd:COG4976   38 LLARLPPGPFGRVLDLGCGTGLLGEALRPRGY----RLTGVDLSEEMLAKARE----------KGVYDRLLVADLADLAE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370 129 KPAS--VVALNFTLQFIAPEQRltLLGRIRDALVPGGALILSEKlRFDDEQEHAL-LTDLHIAFKRA--NGYSDLEIAQK 203
Cdd:COG4976  104 PDGRfdLIVAADVLTYLGDLAA--VFAGVARALKPGGLFIFSVE-DADGSGRYAHsLDYVRDLLAAAgfEVPGLLVVARK 180


                 .
gi 492055370 204 R 204
Cdd:COG4976  181 P 181
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 49-229 1.08e-07

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: 50.87  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   49 VLAAQFAQPDTVLYDLGSSLGAVTQALRRHVrsEGCEVIAIDnSSAMVERCREYLNAqnsmfQELLPVQVIEGDILALEF 128
Cdd:pfam00891  52 VLTAFDLSGFRSLVDVGGGTGALAQAIVSLY--PGCKGIVFD-LPHVVEAAPTHFSA-----GEEPRVTFHGGDFFKDSL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  129 KPASVVALNFTLQFIAPEQRLTLLGRIRDALVPGGALILSEKLRFDDEQE--HALLTDLHIAFKRaNGysdleiaQKRSA 206
Cdd:pfam00891 124 PEADAYILKRVLHDWSDEKCVKLLKRCYKACPAGGKVILVESLLGADPSGplHTQLYSLNMLAQT-EG-------RERTE 195

                         170       180
                  ....*....|....*....|...
gi 492055370  207 ienvmkpdslEEHRQRLLAAGFS 229
Cdd:pfam00891 196 ----------AEYSELLTGAGFS 208
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-169 1.86e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.26  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   57 PDTVLYDLGSSLGAVTQALRRHVRSEGcEVIAIDNSSAMVERCREylNAQNSMFQEllpVQVIEGDILALE--FKPAS-- 132
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNA-EVVGIDISEEAIEKARE--NAQKLGFDN---VEFEQGDIEELPelLEDDKfd 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 492055370  133 VVALNFTLQFIaPEQRLTlLGRIRDALVPGGALILSE 169
Cdd:pfam13847  77 VVISNCVLNHI-PDPDKV-LQEILRVLKPGGRLIISD 111
rADc smart00650
Ribosomal RNA adenine dimethylases;
43-135 8.41e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370    43 IVENLGVlaaqfaQPDTVLYDLGSSLGAVTQALRRHVRsegcEVIAIDNSSAMVERCREYlnaqnsmFQELLPVQVIEGD 122
Cdd:smart00650   5 IVRAANL------RPGDTVLEIGPGKGALTEELLERAK----RVTAIEIDPRLAPRLREK-------FAAADNLTVIHGD 67

                           90
                   ....*....|....*.
gi 492055370   123 ILALEF---KPASVVA 135
Cdd:smart00650  68 ALKFDLpklQPYKVVG 83
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 63-185 4.18e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 37.75  E-value: 4.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370  63 DLGSSLGAVTQALRRhvRSEGCEVIAIDNSSAMVERCREYLnaqnsmfqellpVQVIEGDILALEFKP-ASVVALNFTLQ 141
Cdd:PRK14103  35 DLGCGPGNLTRYLAR--RWPGAVIEALDSSPEMVAAARERG------------VDARTGDVRDWKPKPdTDVVVSNAALQ 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492055370 142 FIaPEQRlTLLGRIRDALVPGGALILSEKLRFdDEQEHALLTDL 185
Cdd:PRK14103 101 WV-PEHA-DLLVRWVDELAPGSWIAVQVPGNF-DAPSHAAVRAL 141
Methyltransf_33 pfam10017
Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family ...
 40-168 5.79e-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: 37.45  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492055370   40 YPTIVEnLGVL---AAQFAQ--PDTVLYDLGSSLGAVTQALRRHVRSEGCEV--IAIDNSSAMVERCREYLNAQnsmFQE 112
Cdd:pfam10017  40 YPTRTE-IAILrrhAAEIAAliPAAVLVELGSGSSRKTRLLLDALPAAGKPVtyVPIDISAEALEESAAALAAD---YPG 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492055370  113 LlPVQVIEGD-ILALEFKPAS-----VVAL------NFTlqfiaPEQRLTLLGRIRDALVPGGALILS 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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