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Conserved domains on  [gi|520900465|ref|WP_020323281|]
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carboxy-S-adenosyl-L-methionine synthase CmoA [Erwinia tracheiphila]

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; ...
 4-242 1.25e-168

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: 464.48  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465    4 RDTLFAAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLARRFVQPDSQVYDLGCSLGAATLSVRRNIQASGC 83
Cdd:TIGR00740   1 KDTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   84 KIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLVVLNFTLQFLAPEERQALIARILSGLRPGGALVLS 163
Cdd:TIGR00740  81 KIIAIDNSPAMIERCRQHIAAYHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGALVLS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520900465  164 EKFSFADEKVGALLFDMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLQTAGFKHVELWFQCFNFGSLIALK 242
Cdd:TIGR00740 161 EKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIALK 239
 
Name Accession Description Interval E-value
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 4-242 1.25e-168

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: 464.48  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465    4 RDTLFAAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLARRFVQPDSQVYDLGCSLGAATLSVRRNIQASGC 83
Cdd:TIGR00740   1 KDTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   84 KIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLVVLNFTLQFLAPEERQALIARILSGLRPGGALVLS 163
Cdd:TIGR00740  81 KIIAIDNSPAMIERCRQHIAAYHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGALVLS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520900465  164 EKFSFADEKVGALLFDMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLQTAGFKHVELWFQCFNFGSLIALK 242
Cdd:TIGR00740 161 EKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIALK 239
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
1-244 1.23e-155

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


Pssm-ID: 185348  Cd Length: 247  Bit Score: 432.14  E-value: 1.23e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   1 MSNRDTLFAAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLARRFVQPDSQVYDLGCSLGAATLSVRRNIQA 80
Cdd:PRK15451   1 MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  81 SGCKIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLVVLNFTLQFLAPEERQALIARILSGLRPGGAL 160
Cdd:PRK15451  81 DNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465 161 VLSEKFSFADEKVGALLFDMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLQTAGFKHVELWFQCFNFGSLIA 240
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 ....
gi 520900465 241 LKAG 244
Cdd:PRK15451 241 LKAE 244
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-164 5.89e-27

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 99.90  E-value: 5.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  56 PDSQVYDLGCSLGAATLSVRRNIQasGCKIISVDNSPAMIERCRRHIDafraetPVEVVEADIRNITI-ENASLVVLNFT 134
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFP--GARVTGVDLSPEMLARARARLP------NVRFVVADLRDLDPpEPFDLVVSNAA 72

                         90       100       110
                 ....*....|....*....|....*....|
gi 520900465 135 LQFLapEERQALIARILSGLRPGGALVLSE 164
Cdd:COG4106   73 LHWL--PDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-158 5.84e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 78.76  E-value: 5.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   60 VYDLGCSLGAATLSVRRniqASGCKIISVDNSPAMIERCRRHidAFRAETPVEVVEADIRNITIENAS--LVVLNFTLQF 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR---RGGARVTGVDLSPEMLERARER--AAEAGLNVEFVQGDAEDLPFPDGSfdLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 520900465  138 LAPEERQALIARILSGLRPGG 158
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-163 1.95e-13

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: 64.37  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  60 VYDLGCSLGAATLSVRRniqASGCKIISVDNSPAMIERCRRHIDAFRAEtPVEVVEADIRNIT---IENASLVVLNFTLQ 136
Cdd:cd02440    2 VLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPpeaDESFDVIISDPPLH 77

                         90       100
                 ....*....|....*....|....*..
gi 520900465 137 FLaPEERQALIARILSGLRPGGALVLS 163
Cdd:cd02440   78 HL-VEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 4-242 1.25e-168

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: 464.48  E-value: 1.25e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465    4 RDTLFAAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLARRFVQPDSQVYDLGCSLGAATLSVRRNIQASGC 83
Cdd:TIGR00740   1 KDTLFSAPIAKLGDFIFDENVAEVFPDMIQRSVPGYSNIISAIGMLAERFVQADSNVYDLGCSLGAATLSARRNIHHDNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   84 KIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLVVLNFTLQFLAPEERQALIARILSGLRPGGALVLS 163
Cdd:TIGR00740  81 KIIAIDNSPAMIERCRQHIAAYHAEIPVDIICGDIRDIAIENASMVILNFTLQFLEPEDRIALLDKIYEGLNPGGALVLS 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520900465  164 EKFSFADEKVGALLFDMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLQTAGFKHVELWFQCFNFGSLIALK 242
Cdd:TIGR00740 161 EKFRFEDAKIGELLFDLHHDFKRANGYSELEISQKRSALENVMLTDSIETHKARLHNAGFEHSELWFQCFNFGSLIALK 239
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
1-244 1.23e-155

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


Pssm-ID: 185348  Cd Length: 247  Bit Score: 432.14  E-value: 1.23e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   1 MSNRDTLFAAPIASLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLARRFVQPDSQVYDLGCSLGAATLSVRRNIQA 80
Cdd:PRK15451   1 MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQVYDLGCSLGAATLSVRRNIHH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  81 SGCKIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLVVLNFTLQFLAPEERQALIARILSGLRPGGAL 160
Cdd:PRK15451  81 DNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRDIAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465 161 VLSEKFSFADEKVGALLFDMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLQTAGFKHVELWFQCFNFGSLIA 240
Cdd:PRK15451 161 VLSEKFSFEDAKVGELLFNMHHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHKAGFEHSELWFQCFNFGSLVA 240


                 ....
gi 520900465 241 LKAG 244
Cdd:PRK15451 241 LKAE 244
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-164 5.89e-27

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 99.90  E-value: 5.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  56 PDSQVYDLGCSLGAATLSVRRNIQasGCKIISVDNSPAMIERCRRHIDafraetPVEVVEADIRNITI-ENASLVVLNFT 134
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFP--GARVTGVDLSPEMLARARARLP------NVRFVVADLRDLDPpEPFDLVVSNAA 72

                         90       100       110
                 ....*....|....*....|....*....|
gi 520900465 135 LQFLapEERQALIARILSGLRPGGALVLSE 164
Cdd:COG4106   73 LHWL--PDHAALLARLAAALAPGGVLAVQV 100
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 48-177 2.58e-19

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: 81.19  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVQPDSQVYDLGCSLGAATLSVRRNiqasGCKIISVDNSPAMIERCRRHIDafRAETPVEVVEADIRNITIENAS 127
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER----GARVTGVDISPEMLELARERAA--EAGLNVEFVVGDAEDLPFPDGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520900465 128 --LVVLNFTLQFLapEERQALIARILSGLRPGGALVLSEKFSFADEKVGALL 177
Cdd:COG2226   88 fdLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-158 5.84e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 78.76  E-value: 5.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   60 VYDLGCSLGAATLSVRRniqASGCKIISVDNSPAMIERCRRHidAFRAETPVEVVEADIRNITIENAS--LVVLNFTLQF 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR---RGGARVTGVDLSPEMLERARER--AAEAGLNVEFVQGDAEDLPFPDGSfdLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 520900465  138 LAPEERQALIARILSGLRPGG 158
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-163 1.97e-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: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  49 LARRFVQPDSQVYDLGCSLGAATLSVRRNiqasGCKIISVDNSPAMIERCRRHIDAFRaetpVEVVEADIRNITIENAS- 127
Cdd:COG2227   17 LLARLLPAGGRVLDVGCGTGRLALALARR----GADVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEDGSf 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 520900465 128 -LVVLNFTLQFLapEERQALIARILSGLRPGGALVLS 163
Cdd:COG2227   89 dLVICSEVLEHL--PDPAALLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 37-187 1.67e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.86  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  37 PGYSNIISMIGMLarrfvQPDSQVYDLGCSLGAATLSVRrniQASGCKIISVDNSPAMIERCRRHIDAFRAEtPVEVVEA 116
Cdd:COG0500   12 PGLAALLALLERL-----PKGGRVLDLGCGTGRNLLALA---ARFGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465 117 DIRNITIENAS---LVVLNFTLQFLAPEERQALIARILSGLRPGGALVLS------EKFSFADEKVGALLFDMHHDFKRA 187
Cdd:COG0500   83 DLAELDPLPAEsfdLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSasdaaaALSLARLLLLATASLLELLLLLRL 162
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 48-162 1.85e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.11  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVQPDSQVYDLGCSLGAATLsvrRNIQASGCKIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENA- 126
Cdd:COG2230   43 ILRKLGLKPGMRVLDIGCGWGGLAL---YLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQf 119

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520900465 127 SLVVLNFTLQFLAPEERQALIARILSGLRPGGALVL 162
Cdd:COG2230  120 DAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-163 1.95e-13

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: 64.37  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  60 VYDLGCSLGAATLSVRRniqASGCKIISVDNSPAMIERCRRHIDAFRAEtPVEVVEADIRNIT---IENASLVVLNFTLQ 136
Cdd:cd02440    2 VLDLGCGTGALALALAS---GPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPpeaDESFDVIISDPPLH 77

                         90       100
                 ....*....|....*....|....*..
gi 520900465 137 FLaPEERQALIARILSGLRPGGALVLS 163
Cdd:cd02440   78 HL-VEDLARFLEEARRLLKPGGVLVLT 103
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 48-160 7.44e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 63.42  E-value: 7.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVQPDSQVYDLGCSLGAAT-LSVRRNIQAsgcKIISVDNSPAMIERCRRHIdafraetP-VEVVEADIRNIT-IE 124
Cdd:PRK01683  23 LLARVPLENPRYVVDLGCGPGNSTeLLVERWPAA---RITGIDSSPAMLAEARSRL-------PdCQFVEADIASWQpPQ 92

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520900465 125 NASLVVLNFTLQFLApeERQALIARILSGLRPGGAL 160
Cdd:PRK01683  93 ALDLIFANASLQWLP--DHLELFPRLVSLLAPGGVL 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 62-162 4.54e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 57.67  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   62 DLGCSLGAATLSVRRNiqasGCKIISVDNSPAMIERCRRHIdafrAETPVEVVEADIRNITIENAS--LVVLNFTLQFLa 139
Cdd:pfam08241   2 DVGCGTGLLTELLARL----GARVTGVDISPEMLELAREKA----PREGLTFVVGDAEDLPFPDNSfdLVLSSEVLHHV- 72

                          90       100
                  ....*....|....*....|...
gi 520900465  140 pEERQALIARILSGLRPGGALVL 162
Cdd:pfam08241  73 -EDPERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
48-163 8.85e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.16  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVQPDSQVYDLGCSLGAATLSVRrniqASGCKIISVDNSPAMIERCRRHidafraETPVEVVEADIRNITIENAS 127
Cdd:COG4976   38 LLARLPPGPFGRVLDLGCGTGLLGEALR----PRGYRLTGVDLSEEMLAKAREK------GVYDRLLVADLADLAEPDGR 107

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520900465 128 --LVVLNFTLQFLapEERQALIARILSGLRPGGALVLS 163
Cdd:COG4976  108 fdLIVAADVLTYL--GDLAAVFAGVARALKPGGLFIFS 143
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 62-160 4.87e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 49.67  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   62 DLGCSLGAATLSVRRNIqaSGCKIISVDNSPAMIERCRRHIDAFRAE--TPVEVVEADIRNITIENASLVVLNFTLQFLA 139
Cdd:pfam08242   2 EIGCGTGTLLRALLEAL--PGLEYTGLDISPAALEAARERLAALGLLnaVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90       100
                  ....*....|....*....|.
gi 520900465  140 peERQALIARILSGLRPGGAL 160
Cdd:pfam08242  80 --DPRAVLRNIRRLLKPGGVL 98
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 48-160 3.14e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 50.07  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVQPDSQVYDLGCSLGAATLSVRRniQASGCKIISVDNSPAMIERCR-RHIDAfraetpvevVEADIRNIT-IEN 125
Cdd:PRK14103  21 LLARVGAERARRVVDLGCGPGNLTRYLAR--RWPGAVIEALDSSPEMVAAAReRGVDA---------RTGDVRDWKpKPD 89

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 520900465 126 ASLVVLNFTLQFLaPEERqALIARILSGLRPGGAL 160
Cdd:PRK14103  90 TDVVVSNAALQWV-PEHA-DLLVRWVDELAPGSWI 122
PRK08317 PRK08317
hypothetical protein; Provisional
 54-164 5.01e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.16  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  54 VQPDSQVYDLGCSLGAATLSVRRNIQASGcKIISVDNSPAMIERCRRHIDAfrAETPVEVVEADIRNITIENASL--VVL 131
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARRVGPEG-RVVGIDRSEAMLALAKERAAG--LGPNVEFVRGDADGLPFPDGSFdaVRS 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 520900465 132 NFTLQFLapEERQALIARILSGLRPGGALVLSE 164
Cdd:PRK08317  94 DRVLQHL--EDPARALAEIARVLRPGGRVVVLD 124
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 48-163 1.81e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 41.67  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  48 MLARRFVqpdSQVYDLGCSLGAATLSVRrniqASGCKIISVDNSPAMIERCRRHIDAFRaetpveVVEADIRNITIENAS 127
Cdd:PRK10258  37 MLPQRKF---THVLDAGCGPGWMSRYWR----ERGSQVTALDLSPPMLAQARQKDAADH------YLAGDIESLPLATAT 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 520900465 128 --LVVLNFTLQFLApEERQALiARILSGLRPGGALVLS 163
Cdd:PRK10258 104 fdLAWSNLAVQWCG-NLSTAL-RELYRVVRPGGVVAFT 139
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 55-164 2.62e-04

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: 40.85  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   55 QPDSQVYDLGCSLGAATLSVRRniQASGCKIISVDnSPAMIERCRRHIDAfRAETPVEVVEADIRNITIENASLVVLNFT 134
Cdd:pfam00891  59 SGFRSLVDVGGGTGALAQAIVS--LYPGCKGIVFD-LPHVVEAAPTHFSA-GEEPRVTFHGGDFFKDSLPEADAYILKRV 134

                          90       100       110
                  ....*....|....*....|....*....|
gi 520900465  135 LQFLAPEERQALIARILSGLRPGGALVLSE 164
Cdd:pfam00891 135 LHDWSDEKCVKLLKRCYKACPAGGKVILVE 164
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
51-161 3.99e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  51 RRFVQPDSQVYDLGCSLGA-ATLSVRRNIQasgcKIISVDNSPAMIERCRRHIDAFRAETPVEVVEADIRNITIENASLV 129
Cdd:COG4076   30 ERVVKPGDVVLDIGTGSGLlSMLAARAGAK----KVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADV 105

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 520900465 130 VLNFTLQFLAPEERQalIARILSG----LRPGGALV 161
Cdd:COG4076  106 IISEMLDTALLDEGQ--VPILNHArkrlLKPGGRII 139
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-164 6.81e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.94  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465   56 PDSQVYDLGCSLGAATLSVRRNIqASGCKIISVDNSPAMIERCRRHidafRAETPVEVVEADIRNIT-------IENASL 128
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEEL-GPNAEVVGIDISEEAIEKAREN----AQKLGFDNVEFEQGDIEelpelleDDKFDV 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 520900465  129 VVLNFTLQFLApeERQALIARILSGLRPGGALVLSE 164
Cdd:pfam13847  78 VISNCVLNHIP--DPDKVLQEILRVLKPGGRLIISD 111
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
62-158 2.89e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 37.79  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520900465  62 DLGCSLGaatlsvrRN---IQASGCKIISVDNSPAMIERCRRHIDAFRAETpVEVVEADIRNITIENA-SLVVLNFTLQF 137
Cdd:PRK11207  36 DLGCGNG-------RNslyLAANGFDVTAWDKNPMSIANLERIKAAENLDN-LHTAVVDLNNLTFDGEyDFILSTVVLMF 107

                         90       100
                 ....*....|....*....|.
gi 520900465 138 LAPEERQALIARILSGLRPGG 158
Cdd:PRK11207 108 LEAKTIPGLIANMQRCTKPGG 128
 
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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