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Conserved domains on  [gi|695664495|ref|WP_032624253|]
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MULTISPECIES: trans-aconitate 2-methyltransferase [Enterobacter]

Protein Classification

trans-aconitate 2-methyltransferase( domain architecture ID 11479697)

trans-aconitate 2-methyltransferase catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate at high affinity and of cis-aconitate, isocitrate, and citrate at lower velocities and affinities

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 1-252 3.60e-161

trans-aconitate 2-methyltransferase; Provisional


:

Pssm-ID: 234970  Cd Length: 258  Bit Score: 446.70  E-value: 3.60e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   1 MADWDPSLYLQYSAERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDCHF 80
Cdd:PRK01683   1 MSDWNPSLYLKFEDERTRPARDLLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  81 VESDIRHYKPDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDNWLEPTHALMREVA----WEQGYPDRG- 155
Cdd:PRK01683  81 VEADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLAVQMPDNLDEPSHVLMREVAengpWEQNLPDRGa 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495 156 -REQLPGIHAYYDILTDAGCDVDIWRTTYFHQMSSHQAIIDWVSATGLRPWLQDLNESEQQNFLKRYLELLEEQYPLQEN 234
Cdd:PRK01683 161 rRAPLPPPHAYYDALAPAACRVDIWHTTYYHPMPSAQAIVEWVKGTGLRPFLDPLTESEQAAFLAAYLARIAEAYPLQAD 240

                        250
                 ....*....|....*...
gi 695664495 235 GQILLAFPRLFMVAQRVP 252
Cdd:PRK01683 241 GKVLLAFPRLFIVARRKE 258
 
Name Accession Description Interval E-value
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 1-252 3.60e-161

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 446.70  E-value: 3.60e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   1 MADWDPSLYLQYSAERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDCHF 80
Cdd:PRK01683   1 MSDWNPSLYLKFEDERTRPARDLLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  81 VESDIRHYKPDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDNWLEPTHALMREVA----WEQGYPDRG- 155
Cdd:PRK01683  81 VEADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLAVQMPDNLDEPSHVLMREVAengpWEQNLPDRGa 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495 156 -REQLPGIHAYYDILTDAGCDVDIWRTTYFHQMSSHQAIIDWVSATGLRPWLQDLNESEQQNFLKRYLELLEEQYPLQEN 234
Cdd:PRK01683 161 rRAPLPPPHAYYDALAPAACRVDIWHTTYYHPMPSAQAIVEWVKGTGLRPFLDPLTESEQAAFLAAYLARIAEAYPLQAD 240

                        250
                 ....*....|....*...
gi 695664495 235 GQILLAFPRLFMVAQRVP 252
Cdd:PRK01683 241 GKVLLAFPRLFIVARRKE 258
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
36-130 4.38e-42

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 138.80  E-value: 4.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  36 VDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDCHFVESDIRHYKPDQPLSLIYANASLQWIPDHYHLLPH 115
Cdd:COG4106    6 LDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAALLAR 85

                         90
                 ....*....|....*
gi 695664495 116 LVSLLQLNGVLAIQM 130
Cdd:COG4106   86 LAAALAPGGVLAVQV 100
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 20-127 1.33e-15

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: 73.47  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   20 AAELLARVP--LADITSGV-DLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALP-DCHFVESDIRHYK-PDQPL 94
Cdd:TIGR02072  20 AKRLLALLKekGIFIPASVlDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSeNVQFICGDAEKLPlEDSSF 99

                          90       100       110
                  ....*....|....*....|....*....|...
gi 695664495   95 SLIYANASLQWIPDHYHLLPHLVSLLQLNGVLA 127
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSQALSELARVLKPGGLLA 132
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-109 3.60e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 68.74  E-value: 3.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695664495   37 DLGCGPGNSTALLKQRWpSAQIAGVDNSPAMLEEARQAL----PDCHFVESDIRHYK-PDQPLSLIYANASLQWIPDH 109
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPfPDGSFDLVVSSGVLHHLPDP 79
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-129 2.00e-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: 59.37  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  36 VDLGCGPGNSTALLKQRwPSAQIAGVDNSPAMLEEARQAL-----PDCHFVESDIRH--YKPDQPLSLIYANASLQWIPD 108
Cdd:cd02440    3 LDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAaallaDNVEVLKGDAEElpPEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 695664495 109 HYH-LLPHLVSLLQLNGVLAIQ 129
Cdd:cd02440   82 DLArFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 1-252 3.60e-161

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 446.70  E-value: 3.60e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   1 MADWDPSLYLQYSAERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDCHF 80
Cdd:PRK01683   1 MSDWNPSLYLKFEDERTRPARDLLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  81 VESDIRHYKPDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDNWLEPTHALMREVA----WEQGYPDRG- 155
Cdd:PRK01683  81 VEADIASWQPPQALDLIFANASLQWLPDHLELFPRLVSLLAPGGVLAVQMPDNLDEPSHVLMREVAengpWEQNLPDRGa 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495 156 -REQLPGIHAYYDILTDAGCDVDIWRTTYFHQMSSHQAIIDWVSATGLRPWLQDLNESEQQNFLKRYLELLEEQYPLQEN 234
Cdd:PRK01683 161 rRAPLPPPHAYYDALAPAACRVDIWHTTYYHPMPSAQAIVEWVKGTGLRPFLDPLTESEQAAFLAAYLARIAEAYPLQAD 240

                        250
                 ....*....|....*...
gi 695664495 235 GQILLAFPRLFMVAQRVP 252
Cdd:PRK01683 241 GKVLLAFPRLFIVARRKE 258
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 4-249 7.64e-76

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 230.35  E-value: 7.64e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   4 WDPSLYLQYSAERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDchFVES 83
Cdd:PRK14103   2 WDPDVYLAFADHRGRPFYDLLARVGAERARRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARERGVD--ARTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  84 DIRHYKPDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDNWLEPTHALMREVAWEQGYPDRGREqLPGIH 163
Cdd:PRK14103  80 DVRDWKPKPDTDVVVSNAALQWVPEHADLLVRWVDELAPGSWIAVQVPGNFDAPSHAAVRALARREPWAKLLRD-IPFRV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495 164 A--------YYDILTDAGCDVDIWRTTYFHQMSSHQAIIDWVSATGLRPWLQDLNESEQQNFLKRYLELLEEQYPLQENG 235
Cdd:PRK14103 159 GavvqtpagYAELLTDAGCKVDAWETTYVHQLTGEDPVLDWITGTALRPVRERLSDDSWEQFRAELIPLLREAYPPRADG 238

                        250
                 ....*....|....
gi 695664495 236 QILLAFPRLFMVAQ 249
Cdd:PRK14103 239 TTFFPFRRVFVVAR 252
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
36-130 4.38e-42

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 138.80  E-value: 4.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  36 VDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPDCHFVESDIRHYKPDQPLSLIYANASLQWIPDHYHLLPH 115
Cdd:COG4106    6 LDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAALLAR 85

                         90
                 ....*....|....*
gi 695664495 116 LVSLLQLNGVLAIQM 130
Cdd:COG4106   86 LAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1-139 9.45e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 75.42  E-value: 9.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   1 MAD-WDPSLY--LQYSAERtRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQALPD 77
Cdd:COG4976   14 YADsYDAALVedLGYEAPA-LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGVY 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695664495  78 CHFVESDIRHYK-PDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDnwLEPTH 139
Cdd:COG4976   91 DRLLVADLADLAePDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVED--ADGSG 151
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 14-128 2.56e-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: 73.49  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  14 AERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQALPD----CHFVESDIRHYK 89
Cdd:COG2226    5 AARYDGREALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 695664495  90 -PDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAI 128
Cdd:COG2226   83 fPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 20-127 1.33e-15

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: 73.47  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   20 AAELLARVP--LADITSGV-DLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALP-DCHFVESDIRHYK-PDQPL 94
Cdd:TIGR02072  20 AKRLLALLKekGIFIPASVlDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSeNVQFICGDAEKLPlEDSSF 99

                          90       100       110
                  ....*....|....*....|....*....|...
gi 695664495   95 SLIYANASLQWIPDHYHLLPHLVSLLQLNGVLA 127
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSQALSELARVLKPGGLLA 132
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 37-109 3.60e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 68.74  E-value: 3.60e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695664495   37 DLGCGPGNSTALLKQRWpSAQIAGVDNSPAMLEEARQAL----PDCHFVESDIRHYK-PDQPLSLIYANASLQWIPDH 109
Cdd:pfam13649   3 DLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPfPDGSFDLVVSSGVLHHLPDP 79
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 21-132 7.88e-15

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: 68.89  E-value: 7.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  21 AELLARVPLADITsGVDLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQALPD--CHFVESDIRHYK-PDQPLSLI 97
Cdd:COG2227   15 AALLARLLPAGGR-VLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAElnVDFVQGDLEDLPlEDGSFDLV 91

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695664495  98 YANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPD 132
Cdd:COG2227   92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 12-161 1.31e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.55  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  12 YSAERTRPAAELLARVP-LADITSGVDLGCGPGNSTALLKQRwPSAQIAGVDNSPAMLEEARQ-----ALPDCHFVESDI 85
Cdd:COG0500    6 YSDELLPGLAALLALLErLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARAraakaGLGNVEFLVADL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  86 RHYK--PDQPLSLIYANASLQWIPDHY--HLLPHLVSLLQLNGVLAIQMPDnwLEPTHALMREVAWEQGYPDRGREQLPG 161
Cdd:COG0500   85 AELDplPAESFDLVVAFGVLHHLPPEEreALLRELARALKPGGVLLLSASD--AAAALSLARLLLLATASLLELLLLLRL 162
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-128 6.87e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.99  E-value: 6.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   36 VDLGCGPGNSTALLKQRWPsaQIAGVDNSPAMLEEARQALPD--CHFVESDIRHYK-PDQPLSLIYANASLQWIPDHYHL 112
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPRegLTFVVGDAEDLPfPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 695664495  113 LPHLVSLLQLNGVLAI 128
Cdd:pfam08241  79 LREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 12-177 1.39e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 60.90  E-value: 1.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   12 YSAERTRPAAELLARVPLADITSG--VDLGCGPGNSTALLKQRWPSaqIAGVDNSPAMLEEARQALPDCHFVESDIRhyK 89
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGrvLDFGCGTGIFLRLLRAQGFS--VTGVDPSPIAIERALLNVRFDQFDEQEAA--V 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   90 PDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAIQMPDNwlePTHALMREVAWEQGYPDRGREQLPGIHAYYDIL 169
Cdd:pfam13489  77 PAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLA---SDEADRLLLEWPYLRPRNGHISLFSARSLKRLL 153


                  ....*...
gi 695664495  170 TDAGCDVD 177
Cdd:pfam13489 154 EEAGFEVV 161
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-129 2.00e-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: 59.37  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  36 VDLGCGPGNSTALLKQRwPSAQIAGVDNSPAMLEEARQAL-----PDCHFVESDIRH--YKPDQPLSLIYANASLQWIPD 108
Cdd:cd02440    3 LDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAaallaDNVEVLKGDAEElpPEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|..
gi 695664495 109 HYH-LLPHLVSLLQLNGVLAIQ 129
Cdd:cd02440   82 DLArFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 34-214 1.40e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 56.87  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  34 SGVDLGCGPGNSTALLKQR-WPSAQIAGVDNSPAMLEEARQA----LPDCHFVESDIRHYK-PDQPLSLIYANASLQWIP 107
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERaaglGPNVEFVRGDADGLPfPDGSFDAVRSDRVLQHLE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495 108 DHYHLLPHLVSLLQLNGVLAIQMPD----NWLEPTHALMREV--AWEQGYPD--RGReQLPG-----------IHAYYDI 168
Cdd:PRK08317 102 DPARALAEIARVLRPGGRVVVLDTDwdtlVWHSGDRALMRKIlnFWSDHFADpwLGR-RLPGlfreagltdieVEPYTLI 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 695664495 169 LTDAGCD---VDIWRTtyFHQMSSHQAIidwvSATGLRPWLQDLNESEQ 214
Cdd:PRK08317 181 ETDLKEAdkgFGLIRA--ARRAVEAGGI----SADEADAWLADLAQLAR 223
TIGR00740 TIGR00740
tRNA (cmo5U34)-methyltransferase; This tRNA methyltransferase is involved, together with cmoB, ...
 37-128 4.15e-08

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: 52.32  E-value: 4.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   37 DLGCGPGNSTALLKQ--RWPSAQIAGVDNSPAMLEEARQALPDCH------FVESDIRHYKPDQPlSLIYANASLQWIP- 107
Cdd:TIGR00740  59 DLGCSLGAATLSARRniHHDNCKIIAIDNSPAMIERCRQHIAAYHaeipvdIICGDIRDIAIENA-SMVILNFTLQFLEp 137

                          90       100
                  ....*....|....*....|..
gi 695664495  108 -DHYHLLPHLVSLLQLNGVLAI 128
Cdd:TIGR00740 138 eDRIALLDKIYEGLNPGGALVL 159
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 36-173 4.95e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   36 VDLGCGPGN-STALLKQRWPSAQIAGVDNSPAMLEEARQ-----ALPDCHFVESDIRH---YKPDQPLSLIYANASLQWI 106
Cdd:pfam13847   8 LDLGCGTGHlSFELAEELGPNAEVVGIDISEEAIEKAREnaqklGFDNVEFEQGDIEElpeLLEDDKFDVVISNCVLNHI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695664495  107 PDHYHLLPHLVSLLQLNGVLAIQMPDNWLEPTHALMREVAWEQGYPdrgrEQLPGIHAYYDILTDAG 173
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCV----GGAILKKKLYELLEEAG 150
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 7-127 6.63e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 52.07  E-value: 6.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   7 SLYLQYSAERTRPAAELLARVPLADITSGVDLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQALPDCHFVESDIR 86
Cdd:PRK10258  18 AHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRER--GSQVTALDLSPPMLAQARQKDAADHYLAGDIE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 695664495  87 HYK-PDQPLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLA 127
Cdd:PRK10258  96 SLPlATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVA 137
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-126 7.33e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 49.29  E-value: 7.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   36 VDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQALPD---CHFVESDIRHYKPDQPLS----LIYANASLQWIPD 108
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAlglLNAVRVELFQLDLGELDPgsfdVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 695664495  109 HYHLLPHLVSLLQLNGVL 126
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 12-100 2.51e-07

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: 49.42  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  12 YSAERTRPAAELLAR-VPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQ-----ALPDCHFVESDI 85
Cdd:COG2813   29 FSRDRLDIGTRLLLEhLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARAnaaanGLENVEVLWSDG 108

                         90
                 ....*....|....*
gi 695664495  86 RHYKPDQPLSLIYAN 100
Cdd:COG2813  109 LSGVPDGSFDLILSN 123
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 12-100 2.97e-07

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: 49.13  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   12 YSAERTRPAAELLARVpLADITSG--VDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQ-----ALPDCHFVESD 84
Cdd:pfam05175  11 FSHGRLDIGSRLLLEH-LPKDLSGkvLDLGCGAGVLGAALAKESPDAELTMVDINARALESAREnlaanGLENGEVVASD 89

                          90
                  ....*....|....*.
gi 695664495   85 IRHYKPDQPLSLIYAN 100
Cdd:pfam05175  90 VYSGVEDGKFDLIISN 105
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 20-131 1.20e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 47.23  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  20 AAELLARVPLADITSGVDLGCGPGNSTALLKQRWpSAQIAGVDNSPAMLEEARQA-----LPD-CHFVESDIRHYKPDQP 93
Cdd:COG2230   40 LDLILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERaaeagLADrVEVRLADYRDLPADGQ 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 695664495  94 LSLIYANASLQWIPDHYH--LLPHLVSLLQLNGVLAIQMP 131
Cdd:COG2230  119 FDAIVSIGMFEHVGPENYpaYFAKVARLLKPGGRLLLHTP 158
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 23-100 4.39e-06

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: 46.29  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  23 LLAR-VPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQ-----ALPD-CHFVESDIRHYKPDQPLS 95
Cdd:COG4123   28 LLAAfAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRnvalnGLEDrITVIHGDLKEFAAELPPG 107


                 ....*...
gi 695664495  96 ---LIYAN 100
Cdd:COG4123  108 sfdLVVSN 115
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 24-100 6.12e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  24 LARVPLADITSGVDLGCGPGnstAL---LKQRWPSAQIAGVDNSPAMLEEARQ-----ALPDCHFVESDIRHYKPDQPLS 95
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSG---AIalaLAKERPDAEVTAVDISPEALAVARRnakhgLGARVEFLQGDWFEPLPGGRFD 177


                 ....*
gi 695664495  96 LIYAN 100
Cdd:PRK09328 178 LIVSN 182
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 16-85 1.53e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.66  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695664495  16 RTRpaAELLARVPLADITSGV---DLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQALPDCH------FVESDI 85
Cdd:PRK07580  47 RMR--DTVLSWLPADGDLTGLrilDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPEAGlagnitFEVGDL 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 36-84 1.82e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.60  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 695664495  36 VDLGCGPGNSTALLKQR-WPSAQIAGVDNSPAMLEEARQALPD------CHFVESD 84
Cdd:PRK00216  56 LDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDlglsgnVEFVQGD 111
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 24-100 1.98e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.59  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  24 LARVPLADITSGVDLGCGPGNSTALLKQRWPSAQIAGVDNSPAMLEEARQ------ALPDCHFVESDIRHY-KPDQPLSL 96
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRnaerlgLEDRVRFLQGDLFEPlPGDGRFDL 184


                 ....
gi 695664495  97 IYAN 100
Cdd:COG2890  185 IVSN 188
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
22-128 5.18e-03

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 37.25  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  22 ELLARVPLADITSgVDLGCGPGNSTALLKQRwpSAQIAGVDNSPAMLEEARQA------LPDCHFVES---DIRHYKpDQ 92
Cdd:PRK11036  36 RLLAELPPRPLRV-LDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKQAaeakgvSDNMQFIHCaaqDIAQHL-ET 111

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 695664495  93 PLSLIYANASLQWIPDHYHLLPHLVSLLQLNGVLAI 128
Cdd:PRK11036 112 PVDLILFHAVLEWVADPKSVLQTLWSVLRPGGALSL 147
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
5-87 7.50e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 36.42  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495   5 DPSLYL-QYSaerTRP--AAELLARVPLADITSG---VDLGCGPGNST--ALLKQrwpSAQIAGVDNSPAMLEEARQALP 76
Cdd:COG2263   16 NPKVELeQYP---TPAelAAELLHLAYLRGDIEGktvLDLGCGTGMLAigAALLG---AKKVVGVDIDPEALEIARENAE 89

                         90
                 ....*....|....*
gi 695664495  77 DC----HFVESDIRH 87
Cdd:COG2263   90 RLgvrvDFIRADVTR 104
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 21-97 9.21e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 36.86  E-value: 9.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695664495  21 AELLARVPLADITSGVDLGCGPGnsTALL--KQRWPS-AQIAGVDNSPAMLEEARQ--------ALPDCHFVESDIRHYK 89
Cdd:COG5459   70 AELAEAGPDFAPLTVLDVGAGPG--TAAWaaADAWPSlLDATLLERSAAALALGRRlaraaanpALETAEWRLADLAAAL 147


                 ....*...
gi 695664495  90 PDQPLSLI 97
Cdd:COG5459  148 PAPPADLV 155
 
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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