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Conserved domains on  [gi|814585857|ref|WP_046385066|]
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MULTISPECIES: bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Pseudomonas]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
39-151 1.44e-28

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: 103.56  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  39 IDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:COG2227   14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAREraaELNVDFVQGDLEDLPLEDGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 814585857 116 ANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPR 151
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
39-151 1.44e-28

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: 103.56  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  39 IDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:COG2227   14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAREraaELNVDFVQGDLEDLPLEDGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 814585857 116 ANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPR 151
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
54-143 6.82e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 6.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   54 VLDFGCGPGRDLQTFTRM-GHIAVGLDGSERFAQMARE-----DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPKQE 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERAREraaeaGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90
                  ....*....|....*.
gi 814585857  128 LPRVLKQLHGALKPGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-146 5.97e-15

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: 67.84  E-value: 5.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  53 TVLDFGCGPGRDLQTF-TRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDL-PNARFDGIFANAVLFHIP 124
Cdd:cd02440    1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80
                         90       100
                 ....*....|....*....|..
gi 814585857 125 kQELPRVLKQLHGALKPGGVLF 146
Cdd:cd02440   81 -EDLARFLEEARRLLKPGGVLV 101
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
40-185 1.22e-10

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: 58.84  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   40 DALLRHIQGAAPFT---VLDFGCGPG---RDL-QTFTRMGHIAvgLDGSERFAQMAREDSGCEV--LQQDFLKLDLPNAR 110
Cdd:TIGR02072  21 KRLLALLKEKGIFIpasVLDIGCGTGyltRALlKRFPQAEFIA--LDISAGMLAQAKTKLSENVqfICGDAEKLPLEDSS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  111 FDGIFANAVL--FHipkqELPRVLKQLHGALKPGGVL-FSSNPRGDNRE-----GWNGPRYGSYHDLEAWqsLLTAAGFV 182
Cdd:TIGR02072  99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLRYLSLDELKAL--LKNSFELL 172

                  ...
gi 814585857  183 ELE 185
Cdd:TIGR02072 173 TLE 175
PRK08317 PRK08317
hypothetical protein; Provisional
40-143 3.24e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.64  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  40 DALLRHIQGAAPFTVLDFGCGPGRDLQTFTRM----GHiAVGLDGSER---FAQMAREDSG--CEVLQQDFLKLDLPNAR 110
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGS 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 814585857 111 FDGIFANAVLFHIPkqELPRVLKQLHGALKPGG 143
Cdd:PRK08317  88 FDAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
rADc smart00650
Ribosomal RNA adenine dimethylases;
39-117 5.44e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857    39 IDALLRHIQGAAPFTVLDFGCGPGRdlqtFT----RMGH--IAVGLDgsERFAQMARE----DSGCEVLQQDFLKLDLPN 108
Cdd:smart00650   2 IDKIVRAANLRPGDTVLEIGPGKGA----LTeellERAKrvTAIEID--PRLAPRLREkfaaADNLTVIHGDALKFDLPK 75

                   ....*....
gi 814585857   109 ARFDGIFAN 117
Cdd:smart00650  76 LQPYKVVGN 84
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
39-151 1.44e-28

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: 103.56  E-value: 1.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  39 IDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:COG2227   14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAREraaELNVDFVQGDLEDLPLEDGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 814585857 116 ANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPR 151
Cdd:COG2227   93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-207 6.85e-27

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 101.23  E-value: 6.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  10 QITATTLDHYNSVAEDFregtrDHDVSQN---------IDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDG 80
Cdd:COG4976    2 ALDAYVEALFDQYADSY-----DAALVEDlgyeapallAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  81 SERFAQMARE-DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPRGDNREgwn 159
Cdd:COG4976   77 SEEMLAKAREkGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIFSVEDADGSG--- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 814585857 160 gpRYgsYHDLEAWQSLLTAAGFvelehyyrpaglpreQQPWLASVWRK 207
Cdd:COG4976  152 --RY--AHSLDYVRDLLAAAGF---------------EVPGLLVVARK 180
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
54-143 6.82e-24

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 90.70  E-value: 6.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   54 VLDFGCGPGRDLQTFTRM-GHIAVGLDGSERFAQMARE-----DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPKQE 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERAREraaeaGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80
                          90
                  ....*....|....*.
gi 814585857  128 LPRVLKQLHGALKPGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
19-181 2.85e-23

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: 90.44  E-value: 2.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  19 YNSVAEDFREGtrdhdvsqniDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE-----DSG 93
Cdd:COG2226    1 FDRVAARYDGR----------EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAREraaeaGLN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  94 CEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVLKQLHGALKPGGVLFSSNPrgdnregwngprygSYHDLEAWQ 173
Cdd:COG2226   71 VEFVVGDAEDLPFPDGSFDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVVDF--------------SPPDLAELE 134

                 ....*...
gi 814585857 174 SLLTAAGF 181
Cdd:COG2226  135 ELLAEAGF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
50-146 3.43e-23

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.11  E-value: 3.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  50 APFTVLDFGCGPGRDLQTFTRM--GHIAVGLDGSERFAQMARE-DSGCEVLQQDFLKLDlPNARFDGIFANAVLFHIPkq 126
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARArLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLP-- 77
                         90       100
                 ....*....|....*....|
gi 814585857 127 ELPRVLKQLHGALKPGGVLF 146
Cdd:COG4106   78 DHAALLARLAAALAPGGVLA 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
55-146 5.97e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 80.40  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   55 LDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE---DSGCEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRV 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkapREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE--DPERA 78
                          90
                  ....*....|....*
gi 814585857  132 LKQLHGALKPGGVLF 146
Cdd:pfam08241  79 LREIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
50-182 4.56e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.12  E-value: 4.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  50 APFTVLDFGCGPGRDLQTFTRMGHIAV-GLDGSERFAQMARED------SGCEVLQQDFLKL-DLPNARFDGIFANAVLF 121
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARFGGRViGIDLSPEAIALARARaakaglGNVEFLVADLAELdPLPAESFDLVVAFGVLH 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585857 122 HIPKQELPRVLKQLHGALKPGGVLF----SSNPRGDNREGWNGPRYGSYHDLEAWQSLLTAAGFV 182
Cdd:COG0500  106 HLPPEEREALLRELARALKPGGVLLlsasDAAAALSLARLLLLATASLLELLLLLRLLALELYLR 170
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
17-146 1.16e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.12  E-value: 1.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  17 DHYNSVAEDFRE-------------GTRDHDVSQNIDALLRHIQGAAPF----TVLDFGCGPGRDLQTFTRM-GHIAVGL 78
Cdd:COG2230    1 HHYDLGNDFYRLfldptmtyscayfEDPDDTLEEAQEAKLDLILRKLGLkpgmRVLDIGCGWGGLALYLARRyGVRVTGV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585857  79 DGSERFAQMARE-------DSGCEVLQQDFLKLDlPNARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGGVLF 146
Cdd:COG2230   81 TLSPEQLEYAREraaeaglADRVEVRLADYRDLP-ADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
53-146 5.97e-15

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: 67.84  E-value: 5.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  53 TVLDFGCGPGRDLQTF-TRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDL-PNARFDGIFANAVLFHIP 124
Cdd:cd02440    1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80
                         90       100
                 ....*....|....*....|..
gi 814585857 125 kQELPRVLKQLHGALKPGGVLF 146
Cdd:cd02440   81 -EDLARFLEEARRLLKPGGVLV 101
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
53-181 1.29e-12

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 62.83  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   53 TVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMAREDSgcEVLQQDFLKLDLPNARFDGIFANAVLFHIPkqELPRVL 132
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNV--RFDQFDEQEAAVPAGKFDVIVAREVLEHVP--DPPALL 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 814585857  133 KQLHGALKPGGVLFSSNPRGDNREG-----WNGPRY----GSYHDLEAWQSLLTAAGF 181
Cdd:pfam13489 101 RQIAALLKPGGLLLLSTPLASDEADrllleWPYLRPrnghISLFSARSLKRLLEEAGF 158
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
53-152 1.14e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.12  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   53 TVLDFGCGPGRDL-QTFTRMGHIA--VGLDGSERFAQMARED------SGCEVLQQDFLKLD--LPNARFDGIFANAVLF 121
Cdd:pfam13847   6 RVLDLGCGTGHLSfELAEELGPNAevVGIDISEEAIEKARENaqklgfDNVEFEQGDIEELPelLEDDKFDVVISNCVLN 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 814585857  122 HIPkqELPRVLKQLHGALKPGGVLFSSNPRG 152
Cdd:pfam13847  86 HIP--DPDKVLQEILRVLKPGGRLIISDPDS 114
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
55-145 1.03e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.22  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   55 LDFGCGPGRDLQTFTRMGHIA--VGLDGSERFAQMARE----DSGCEVLQQDFLKLDLPN---ARFDGIFANAVLFHIPk 125
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARErlaaLGLLNAVRVELFQLDLGEldpGSFDVVVASNVLHHLA- 79
                          90       100
                  ....*....|....*....|
gi 814585857  126 qELPRVLKQLHGALKPGGVL 145
Cdd:pfam08242  80 -DPRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
40-185 1.22e-10

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: 58.84  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   40 DALLRHIQGAAPFT---VLDFGCGPG---RDL-QTFTRMGHIAvgLDGSERFAQMAREDSGCEV--LQQDFLKLDLPNAR 110
Cdd:TIGR02072  21 KRLLALLKEKGIFIpasVLDIGCGTGyltRALlKRFPQAEFIA--LDISAGMLAQAKTKLSENVqfICGDAEKLPLEDSS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  111 FDGIFANAVL--FHipkqELPRVLKQLHGALKPGGVL-FSSNPRGDNRE-----GWNGPRYGSYHDLEAWqsLLTAAGFV 182
Cdd:TIGR02072  99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLRYLSLDELKAL--LKNSFELL 172

                  ...
gi 814585857  183 ELE 185
Cdd:TIGR02072 173 TLE 175
PRK08317 PRK08317
hypothetical protein; Provisional
40-143 3.24e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.64  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  40 DALLRHIQGAAPFTVLDFGCGPGRDLQTFTRM----GHiAVGLDGSER---FAQMAREDSG--CEVLQQDFLKLDLPNAR 110
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGS 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 814585857 111 FDGIFANAVLFHIPkqELPRVLKQLHGALKPGG 143
Cdd:PRK08317  88 FDAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
42-145 3.19e-08

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 52.25  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  42 LLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIA--VGLDGSERFAQMAREdsgcEVLQQDFLKLDL----PNARFDGIF 115
Cdd:PRK01683  23 LLARVPLENPRYVVDLGCGPGNSTELLVERWPAAriTGIDSSPAMLAEARS----RLPDCQFVEADIaswqPPQALDLIF 98
                         90       100       110
                 ....*....|....*....|....*....|
gi 814585857 116 ANAVLFHIPKQElpRVLKQLHGALKPGGVL 145
Cdd:PRK01683  99 ANASLQWLPDHL--ELFPRLVSLLAPGGVL 126
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
54-184 8.59e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 48.59  E-value: 8.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  54 VLDFGCG-PGRDLQTFTRMGHIAVGLDGSERFAQMAREDS---GCEVLQQ--DFLKLDLPNARFDGIFANAVLFHIpkQE 127
Cdd:PLN02336 270 VLDVGCGiGGGDFYMAENFDVHVVGIDLSVNMISFALERAigrKCSVEFEvaDCTKKTYPDNSFDVIYSRDTILHI--QD 347
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585857 128 LPRVLKQLHGALKPGG-VLFSSNPRgdnREGWNGPRYGSY--------HDLEAWQSLLTAAGFVEL 184
Cdd:PLN02336 348 KPALFRSFFKWLKPGGkVLISDYCR---SPGTPSPEFAEYikqrgydlHDVQAYGQMLKDAGFDDV 410
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
42-159 1.04e-06

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 48.04  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  42 LLRHIQGAAPFTVLDFGCGPGRDLQTFT-RMGHIAVGLDGSERFAQMARE----DSGCEVLQQDFLKLDLPNARFDGIFA 116
Cdd:PTZ00098  44 ILSDIELNENSKVLDIGSGLGGGCKYINeKYGAHVHGVDICEKMVNIAKLrnsdKNKIEFEANDILKKDFPENTFDMIYS 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 814585857 117 NAVLFHIPKQELPRVLKQLHGALKPGGVLFSSNPRGDNREGWN 159
Cdd:PTZ00098 124 RDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADKIENWD 166
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
37-145 1.40e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 47.45  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  37 QNIDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE-DSGCEVLQQDFLKLDLPNARFDGIF 115
Cdd:PRK10258  29 QSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQkDAADHYLAGDIESLPLATATFDLAW 108
                         90       100       110
                 ....*....|....*....|....*....|.
gi 814585857 116 AN-AVLFHipkQELPRVLKQLHGALKPGGVL 145
Cdd:PRK10258 109 SNlAVQWC---GNLSTALRELYRVVRPGGVV 136
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
103-145 3.65e-06

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 45.24  E-value: 3.65e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 814585857 103 KLDLPNARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGGVL 145
Cdd:COG4627   39 PLPFPDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGIL 81
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
53-189 3.88e-06

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 45.32  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  53 TVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMARE------DSGCEVLQQDFLKLDLPNARFDGIFANA-------V 119
Cdd:COG1041   29 TVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGAREnlehygYEDADVIRGDARDLPLADESVDAIVTDPpygrsskI 108
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585857 120 LFHIPKQELPRVLKQLHGALKPGGVL-FSSNPRgdnregwngprygsyhdleaWQSLLTAAGFVELEHYYR 189
Cdd:COG1041  109 SGEELLELYEKALEEAARVLKPGGRVvIVTPRD--------------------IDELLEEAGFKVLERHEQ 159
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
40-146 4.24e-05

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 43.31  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  40 DALLRHIQGAAPFTVLDFGCGPGRDLqtFtRM----GHIAVGLDGSERF-------AQMAREDsgcevLQQDFLKL---D 105
Cdd:PRK15068 112 DRVLPHLSPLKGRTVLDVGCGNGYHM--W-RMlgagAKLVVGIDPSQLFlcqfeavRKLLGND-----QRAHLLPLgieQ 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 814585857 106 LP-NARFDGIFANAVLFHipkqelpR-----VLKQLHGALKPGGVLF 146
Cdd:PRK15068 184 LPaLKAFDTVFSMGVLYH-------RrspldHLKQLKDQLVPGGELV 223
arsM PRK11873
arsenite methyltransferase;
53-184 1.51e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.47  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  53 TVLDFGCGPGRD-LQTFTRMGHI--AVGLDGSERFAQMARED------SGCEVLQQDFLKLDLPNARFDGIFANAVLFHI 123
Cdd:PRK11873  80 TVLDLGSGGGFDcFLAARRVGPTgkVIGVDMTPEMLAKARANarkagyTNVEFRLGEIEALPVADNSVDVIISNCVINLS 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 124 PKQElpRVLKQLHGALKPGG-------VLFSSNPRG--DNREGWNGPRYGSYhDLEAWQSLLTAAGFVEL 184
Cdd:PRK11873 160 PDKE--RVFKEAFRVLKPGGrfaisdvVLRGELPEEirNDAELYAGCVAGAL-QEEEYLAMLAEAGFVDI 226
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
29-148 1.52e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 41.48  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   29 GTRDHDVSQ-NIDALLRHIQGAApfTVLDFGCGPGrdlqtftrmghI------------AVGLDGSE---RFAQMAREDS 92
Cdd:pfam06325 141 GTGTHPTTKlCLEALERLVKPGE--SVLDVGCGSG-----------IlaiaalklgakkVVGVDIDPvavRAAKENAELN 207
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 814585857   93 GCEVLQQDFLKLDLPNARFDGIFANaVLFHIpkqeLPRVLKQLHGALKPGGVLFSS 148
Cdd:pfam06325 208 GVEARLEVYLPGDLPKEKADVVVAN-ILADP----LIELAPDIYALVKPGGYLILS 258
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
28-146 2.96e-04

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: 40.17  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  28 EGTRdhdvsqnidALLRHIQGAAPFTVLDFGCG------------PGRDLqtftrmghiaVGLDGSERFAQMARE----- 90
Cdd:COG2813   36 IGTR---------LLLEHLPEPLGGRVLDLGCGygviglalakrnPEARV----------TLVDVNARAVELARAnaaan 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585857  91 -DSGCEVLQQDFLKlDLPNARFDGIFANAVlFHIPKQELPRVLKQL----HGALKPGGVLF 146
Cdd:COG2813   97 gLENVEVLWSDGLS-GVPDGSFDLILSNPP-FHAGRAVDKEVAHALiadaARHLRPGGELW 155
rADc smart00650
Ribosomal RNA adenine dimethylases;
39-117 5.44e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857    39 IDALLRHIQGAAPFTVLDFGCGPGRdlqtFT----RMGH--IAVGLDgsERFAQMARE----DSGCEVLQQDFLKLDLPN 108
Cdd:smart00650   2 IDKIVRAANLRPGDTVLEIGPGKGA----LTeellERAKrvTAIEID--PRLAPRLREkfaaADNLTVIHGDALKFDLPK 75

                   ....*....
gi 814585857   109 ARFDGIFAN 117
Cdd:smart00650  76 LQPYKVVGN 84
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
39-195 9.44e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.99  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  39 IDALLRHIQGAAPFTVLDFGCGPG----------RDLQtftrmghiAVGLDGSERFAQMARE------DSGCEVLQQDFL 102
Cdd:PRK09328  97 VEWALEALLLKEPLRVLDLGTGSGaialalakerPDAE--------VTAVDISPEALAVARRnakhglGARVEFLQGDWF 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857 103 KlDLPNARFDGIFANA--------------VLFHIPKQEL----------PRVLKQLHGALKPGGVLFSsnprgdnrE-G 157
Cdd:PRK09328 169 E-PLPGGRFDLIVSNPpyipeadihllqpeVRDHEPHLALfggedgldfyRRIIEQAPRYLKPGGWLLL--------EiG 239
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 814585857 158 WNGprygsyhdLEAWQSLLTAAGFVELEHYYRPAGLPR 195
Cdd:PRK09328 240 YDQ--------GEAVRALLAAAGFADVETRKDLAGRDR 269
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
42-146 3.15e-03

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: 36.80  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   42 LLRHIQGAAPFTVLDFGCGPGR-DLQTFTRMGHIAV-GLDGSERFAQMARED------SGCEVLQQDFLKlDLPNARFDG 113
Cdd:pfam05175  23 LLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELtMVDINARALESARENlaanglENGEVVASDVYS-GVEDGKFDL 101
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 814585857  114 IFANAVlFHIPKQELP----RVLKQLHGALKPGGVLF 146
Cdd:pfam05175 102 IISNPP-FHAGLATTYnvaqRFIADAKRHLRPGGELW 137
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
101-146 4.33e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 37.27  E-value: 4.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 814585857   101 FLKLDL-----PNARFDGIFANAVL--FHIPKQElpRVLKQLHGALKPGGVLF 146
Cdd:smart00138 189 FAKHNLlaespPLGDFDLIFCRNVLiyFDEPTQR--KLLNRFAEALKPGGYLF 239
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
35-145 4.44e-03

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 36.87  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857  35 VSQNIDALLRHIqGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSERFAQMAR---EDSGceVLQQ-DFLK------- 103
Cdd:PRK11036  30 LWQDLDRLLAEL-PPRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKqaaEAKG--VSDNmQFIHcaaqdia 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 814585857 104 --LDLPnarfdgifANAVLFHI-------PKQelprVLKQLHGALKPGGVL 145
Cdd:PRK11036 107 qhLETP--------VDLILFHAvlewvadPKS----VLQTLWSVLRPGGAL 145
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
54-185 5.51e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 36.63  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857    54 VLDFGCGPGRDLQTF-TRMGHIA-VGLDGSERFAQMARE-------DSGCEVLQQDFLKLDLPnARFDGIFANAVLFHIP 124
Cdd:smart00828   3 VLDFGCGYGSDLIDLaERHPHLQlHGYTISPEQAEVGREriralglQGRIRIFYRDSAKDPFP-DTYDLVFGFEVIHHIK 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585857   125 KQELprVLKQLHGALKPGGVLFSSNPRGDNREGWNGPRYGSYH-DLEAWQSLLTAAGFVELE 185
Cdd:smart00828  82 DKMD--LFSNISRHLKDGGHLVLADFIANLLSAIEHEETTSYLvTREEWAELLARNNLRVVE 141
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
33-143 5.65e-03

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 36.64  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585857   33 HDVSQNIDALLRHIQGAAPFTVLDFGCGPGRDLQTFTRMGHIAVGLDGSE-----------------RFAQMAREDSG-C 94
Cdd:pfam05724  20 EGVNPLLVRHWDALKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISElavekffaeaglsppitELSGFKEYSSGnI 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 814585857   95 EVLQQDFLKLDLPN-ARFDGIFANAVLFHIPKQELPRVLKQLHGALKPGG 143
Cdd:pfam05724 100 SLYCGDFFTLPREElGKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGG 149
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
98-146 8.50e-03

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 36.29  E-value: 8.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 814585857  98 QQDFLKLDLPNARFDGIF-ANaVL--FHIPKQElpRVLKQLHGALKPGGVLF 146
Cdd:COG1352  194 QHNLLDDPPPFGRFDLIFcRN-VLiyFDPELQR--RVLRRFHDSLAPGGYLF 242
 
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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