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Conserved domains on  [gi|490954841|ref|WP_004816656|]
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MULTISPECIES: methyltransferase domain-containing protein [Acinetobacter]

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; ...
 6-267 1.12e-89

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 PRK11088:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 272  Bit Score: 266.78  E-value: 1.12e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   6 CPVCREALSLSDRTWRCVNNHSYDVAKQGYVNLHVVQHKHSKNPGDTPESVQARRGFLSGGFYAPLQQAVVEKIRELRVE 85
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 N---LLDIGCGEGYYTDAMQHQ-----VMQCIGVDIAKNAVQVAAKLNKDVTWIVGTGATLPVLDHSIDLCTSLFSPIPE 157
Cdd:PRK11088  85 KataLLDIGCGEGYYTHALADAlpeitTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYAPCKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841 158 EEILRVLKPKAYLMVVTPAPEHLYGMREGLFDEVKAHEPQKfvEQLqASFELIEQPIIETTFELDQAQLKNLIAMTPYAY 237
Cdd:PRK11088 165 EELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEA--EQL-EGFELQHSERLAYPMRLTGSEAVALLQMTPFAW 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 490954841 238 KAKSEKRLVLEAQVKTTLKAAFQIYIFQKK 267
Cdd:PRK11088 242 KATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 6-267 1.12e-89

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 266.78  E-value: 1.12e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   6 CPVCREALSLSDRTWRCVNNHSYDVAKQGYVNLHVVQHKHSKNPGDTPESVQARRGFLSGGFYAPLQQAVVEKIRELRVE 85
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 N---LLDIGCGEGYYTDAMQHQ-----VMQCIGVDIAKNAVQVAAKLNKDVTWIVGTGATLPVLDHSIDLCTSLFSPIPE 157
Cdd:PRK11088  85 KataLLDIGCGEGYYTHALADAlpeitTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYAPCKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841 158 EEILRVLKPKAYLMVVTPAPEHLYGMREGLFDEVKAHEPQKfvEQLqASFELIEQPIIETTFELDQAQLKNLIAMTPYAY 237
Cdd:PRK11088 165 EELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEA--EQL-EGFELQHSERLAYPMRLTGSEAVALLQMTPFAW 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 490954841 238 KAKSEKRLVLEAQVKTTLKAAFQIYIFQKK 267
Cdd:PRK11088 242 KATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 71-187 5.06e-20

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: 83.50  E-value: 5.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  71 LQQAVVEKIRELRVENLLDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKD----VTWIVGTGATLPVLDHSID 146
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLPFPDGSFD 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490954841 147 LCTSLFS----PIPE---EEILRVLKPKAYLMVVTPAPEHLYGMREGL 187
Cdd:COG2226   90 LVISSFVlhhlPDPEralAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 88-172 4.40e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 4.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   88 LDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKD--VTWIVGTGATLPVLDHSIDLCTSLFS----PIPEE--- 158
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPRegLTFVVGDAEDLPFPDNSFDLVLSSEVlhhvEDPERalr 80

                          90
                  ....*....|....
gi 490954841  159 EILRVLKPKAYLMV 172
Cdd:pfam08241  81 EIARVLKPGGILII 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-217 5.31e-13

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 66.54  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   68 YAPLQQAV-------VEKIRELRVENLLDIGCGEGYYTDAMQHQ--VMQCIGVDIAKNA-VQVAAKLNKDVTWIVGTGAT 137
Cdd:TIGR02072  12 HAKIQREMakrllalLKEKGIFIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMlAQAKTKLSENVQFICGDAEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  138 LPVLDHSIDLCTS-----LFSPIPE--EEILRVLKPKAYLMVVTPAPEHLYGMREgLFDEVKAHEPQkfVEQLQASF--- 207
Cdd:TIGR02072  92 LPLEDSSFDLIVSnlalqWCDDLSQalSELARVLKPGGLLAFSTFGPGTLHELRQ-SFGQHGLRYLS--LDELKALLkns 168

                         170
                  ....*....|....
gi 490954841  208 ----ELIEQPIIET 217
Cdd:TIGR02072 169 fellTLEEELITLS 182
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 86-173 9.79e-07

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: 46.27  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 NLLDIGCGEGYYTDAM-QHQVMQCIGVDIAKNAVQVA-----AKLNKDVTWIVGTGATLPVL-DHSID--LCTSLFSPIP 156
Cdd:cd02440    1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPEaDESFDviISDPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 490954841 157 E------EEILRVLKPKAYLMVV 173
Cdd:cd02440   81 EdlarflEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 6-267 1.12e-89

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 266.78  E-value: 1.12e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   6 CPVCREALSLSDRTWRCVNNHSYDVAKQGYVNLHVVQHKHSKNPGDTPESVQARRGFLSGGFYAPLQQAVVEKIRELRVE 85
Cdd:PRK11088   5 CPLCHQPLTLEENSWICPQNHQFDCAKEGYVNLLPVQHKRSKDPGDNKEMMQARRAFLDAGHYQPLRDAVANLLAERLDE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 N---LLDIGCGEGYYTDAMQHQ-----VMQCIGVDIAKNAVQVAAKLNKDVTWIVGTGATLPVLDHSIDLCTSLFSPIPE 157
Cdd:PRK11088  85 KataLLDIGCGEGYYTHALADAlpeitTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIIRIYAPCKA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841 158 EEILRVLKPKAYLMVVTPAPEHLYGMREGLFDEVKAHEPQKfvEQLqASFELIEQPIIETTFELDQAQLKNLIAMTPYAY 237
Cdd:PRK11088 165 EELARVVKPGGIVITVTPGPRHLFELKGLIYDEVRLHAPEA--EQL-EGFELQHSERLAYPMRLTGSEAVALLQMTPFAW 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 490954841 238 KAKSEKRLVLEAQVKTTLKAAFQIYIFQKK 267
Cdd:PRK11088 242 KATPEVKQQLAAKGVFSCETDFNIRVYRRS 271
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 71-187 5.06e-20

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: 83.50  E-value: 5.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  71 LQQAVVEKIRELRVENLLDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKD----VTWIVGTGATLPVLDHSID 146
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLPFPDGSFD 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490954841 147 LCTSLFS----PIPE---EEILRVLKPKAYLMVVTPAPEHLYGMREGL 187
Cdd:COG2226   90 LVISSFVlhhlPDPEralAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 88-172 4.40e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 4.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   88 LDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKD--VTWIVGTGATLPVLDHSIDLCTSLFS----PIPEE--- 158
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPRegLTFVVGDAEDLPFPDNSFDLVLSSEVlhhvEDPERalr 80

                          90
                  ....*....|....
gi 490954841  159 EILRVLKPKAYLMV 172
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 88-166 3.37e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.13  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   88 LDIGCGEGYYTDAMQHQVM-QCIGVDIAKNAVQVAAKLNKD----VTWIVGTGATLPVLDHSIDLCTSLFS----PIPE- 157
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlPDPDl 81

                          90
                  ....*....|...
gi 490954841  158 ----EEILRVLKP 166
Cdd:pfam13649  82 eaalREIARVLKP 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 86-175 6.01e-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: 69.66  E-value: 6.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 NLLDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKD--VTWIVGTGATLPVLDHSIDL--CTSLFSPIPE---- 157
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElnVDFVQGDLEDLPLEDGSFDLviCSEVLEHLPDpaal 106

                         90
                 ....*....|....*....
gi 490954841 158 -EEILRVLKPKAYLMVVTP 175
Cdd:COG2227  107 lRELARLLKPGGLLLLSTP 125
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
73-182 5.31e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.40  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  73 QAVVEKIRELRVENLLDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKDVTWIVGTGATLPVLDHSIDL--CTS 150
Cdd:COG4976   36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLivAAD 115

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490954841 151 LFSPIPE-----EEILRVLKPKAYLM--VVTPAPEHLYG 182
Cdd:COG4976  116 VLTYLGDlaavfAGVARALKPGGLFIfsVEDADGSGRYA 154
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-217 5.31e-13

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 66.54  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   68 YAPLQQAV-------VEKIRELRVENLLDIGCGEGYYTDAMQHQ--VMQCIGVDIAKNA-VQVAAKLNKDVTWIVGTGAT 137
Cdd:TIGR02072  12 HAKIQREMakrllalLKEKGIFIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMlAQAKTKLSENVQFICGDAEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  138 LPVLDHSIDLCTS-----LFSPIPE--EEILRVLKPKAYLMVVTPAPEHLYGMREgLFDEVKAHEPQkfVEQLQASF--- 207
Cdd:TIGR02072  92 LPLEDSSFDLIVSnlalqWCDDLSQalSELARVLKPGGLLAFSTFGPGTLHELRQ-SFGQHGLRYLS--LDELKALLkns 168

                         170
                  ....*....|....
gi 490954841  208 ----ELIEQPIIET 217
Cdd:TIGR02072 169 fellTLEEELITLS 182
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
85-174 4.39e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.60  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  85 ENLLDIGCGEGYYTDAMQHQVMQC--IGVDIAKNAVQVAAKLNKDVTWIVGTGATLPvLDHSIDLCTS--LFSPIPE--- 157
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPGArvTGVDLSPEMLARARARLPNVRFVVADLRDLD-PPEPFDLVVSnaALHWLPDhaa 81

                         90
                 ....*....|....*....
gi 490954841 158 --EEILRVLKPKAYLMVVT 174
Cdd:COG4106   82 llARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 69-238 9.38e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 9.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  69 APLQQAVVEKIREL-RVENLLDIGCGEGYYTDAM-QHQVMQCIGVDIAKNAVQVAAKLN-----KDVTWIVGTGATLPVL 141
Cdd:COG0500   11 LPGLAALLALLERLpKGGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARAakaglGNVEFLVADLAELDPL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841 142 DH-SIDL--CTSLFSPIPEE-------EILRVLKPKAYLMV--VTPAPEHLYGMREGLFDEVKAHEPQKFVEQLQASFEL 209
Cdd:COG0500   91 PAeSFDLvvAFGVLHHLPPEereallrELARALKPGGVLLLsaSDAAAALSLARLLLLATASLLELLLLLRLLALELYLR 170

                        170       180
                 ....*....|....*....|....*....
gi 490954841 210 IEQPIIETTFELDQAQLKNLIAMTPYAYK 238
Cdd:COG0500  171 ALLAAAATEDLRSDALLESANALEYLLSK 199
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 73-172 3.93e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 49.77  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  73 QAVVEKIRELRVENLLDIGCGEGYYTDAMQHQVM---QCIGVDIAKNAVQVAAK------LNKDVTWIVGTGATLPVLDH 143
Cdd:PRK00216  41 RKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGMLAVGREklrdlgLSGNVEFVQGDAEALPFPDN 120

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490954841 144 SIDLCTSLF-----SPIPE--EEILRVLKPKAYLMV 172
Cdd:PRK00216 121 SFDAVTIAFglrnvPDIDKalREMYRVLKPGGRLVI 156
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 86-178 5.02e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   86 NLLDIGCGEGYYTDAMQHQVM---QCIGVDIAKNAVQVA----AKLN-KDVTWIVGTGATLPVL--DHSIDL--CTSLFS 153
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKArenaQKLGfDNVEFEQGDIEELPELleDDKFDVviSNCVLN 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 490954841  154 PIPE-----EEILRVLKPKAYLMVVTPAPE 178
Cdd:pfam13847  86 HIPDpdkvlQEILRVLKPGGRLIISDPDSL 115
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 86-173 9.79e-07

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: 46.27  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  86 NLLDIGCGEGYYTDAM-QHQVMQCIGVDIAKNAVQVA-----AKLNKDVTWIVGTGATLPVL-DHSID--LCTSLFSPIP 156
Cdd:cd02440    1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPEaDESFDviISDPPLHHLV 80

                         90       100
                 ....*....|....*....|...
gi 490954841 157 E------EEILRVLKPKAYLMVV 173
Cdd:cd02440   81 EdlarflEEARRLLKPGGVLVLT 103
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 80-184 6.78e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.11  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   80 RELRVENLLDIGCGEGYYTDAMQHQVMQCIGVDIAKNAVQVAAKLNKDVT-----WIVGTGATlpvlD--HSIDLCTSLF 152
Cdd:pfam13489  19 KLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQfdeqeAAVPAGKF----DviVAREVLEHVP 94

                          90       100       110
                  ....*....|....*....|....*....|...
gi 490954841  153 SPIPE-EEILRVLKPKAYLMVVTPAPEHLYGMR 184
Cdd:pfam13489  95 DPPALlRQIAALLKPGGLLLLSTPLASDEADRL 127
PRK08317 PRK08317
hypothetical protein; Provisional
 70-175 3.71e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.77  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  70 PLQQAVVEKIREL----RVENLLDIGCGEGYYTDAMQHQVM---QCIGVDIAKN----AVQVAAKLNKDVTWIVGTGATL 138
Cdd:PRK08317   2 PDFRRYRARTFELlavqPGDRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAmlalAKERAAGLGPNVEFVRGDADGL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490954841 139 PVLDHSIDLCTSL--FSPIPE-----EEILRVLKPKAYLMVVTP 175
Cdd:PRK08317  82 PFPDGSFDAVRSDrvLQHLEDparalAEIARVLRPGGRVVVLDT 125
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 69-175 5.82e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.53  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  69 APLQQAVVEKI-RELRVEN---LLDIGCGEGYYTDAM-QHQVMQCIGVDIAKNAVQVA------AKLNKDVTWIVGTGAT 137
Cdd:COG2230   33 EEAQEAKLDLIlRKLGLKPgmrVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYAreraaeAGLADRVEVRLADYRD 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490954841 138 LPvLDHSIDLCTSL--FSPIPEE-------EILRVLKPKAYLMVVTP 175
Cdd:COG2230  113 LP-ADGQFDAIVSIgmFEHVGPEnypayfaKVARLLKPGGRLLLHTP 158
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 88-166 1.73e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.96  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841   88 LDIGCGEGYYTDAMQHQVMQC--IGVDIAKNAVQVAAKLNKDVTWIVGTGATLPVLD------HSIDL--CTSLFSPIPE 157
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERLAALGLLNAVRVELFQLDlgeldpGSFDVvvASNVLHHLAD 80

                          90
                  ....*....|....
gi 490954841  158 -----EEILRVLKP 166
Cdd:pfam08242  81 pravlRNIRRLLKP 94
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 73-197 2.03e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.98  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490954841  73 QAVVEKIRELRVENLLDIGCGEG--------YYTDAmqhqvmQCIGVDIAKNAVQVAAK------LNKDVTWIVGtgatl 138
Cdd:COG2890  102 ELALALLPAGAPPRVLDLGTGSGaialalakERPDA------RVTAVDISPDALAVARRnaerlgLEDRVRFLQG----- 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490954841 139 pvldhsidlctSLFSPIPEEEilrvlkpkAYLMVVTPAPehlY---GMREGLFDEVKAHEPQ 197
Cdd:COG2890  171 -----------DLFEPLPGDG--------RFDLIVSNPP---YipeDEIALLPPEVRDHEPR 210
 
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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