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Conserved domains on  [gi|479375206|gb|ENP55434|]
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hypothetical protein C072_00043 [Brucella abortus 863/67]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-146 1.02e-30

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: 111.62  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  28 APEWPVVRSLLPDLT---GRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDA--VCYIQADMERLEL 102
Cdd:COG2226    5 AARYDGREALLAALGlrpGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGlnVEFVVGDAEDLPF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 479375206 103 PEASFDLVYSSLAFHYIRDFPRILKTIHAALRPDGRFVFTIEHP 146
Cdd:COG2226   84 PDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-146 1.02e-30

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: 111.62  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  28 APEWPVVRSLLPDLT---GRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDA--VCYIQADMERLEL 102
Cdd:COG2226    5 AARYDGREALLAALGlrpGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGlnVEFVVGDAEDLPF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 479375206 103 PEASFDLVYSSLAFHYIRDFPRILKTIHAALRPDGRFVFTIEHP 146
Cdd:COG2226   84 PDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-141 3.74e-29

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 105.82  E-value: 3.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   48 DLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIRDFPRILK 127
Cdd:pfam08241   2 DVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 479375206  128 TIHAALRPDGRFVF 141
Cdd:pfam08241  81 EIARVLKPGGILII 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 46-143 7.13e-21

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: 88.11  E-value: 7.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   46 IADLGCGFGWFCRFAREQG-AASVTGYDLSQNMLERARRDtQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIRDFPR 124
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK-LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQ 116

                          90
                  ....*....|....*....
gi 479375206  125 ILKTIHAALRPDGRFVFTI 143
Cdd:TIGR02072 117 ALSELARVLKPGGLLAFST 135
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 37-142 1.15e-20

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 87.89  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  37 LLPDLTGRDIA---DLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRdtQDDAVCYIQADMERLELPEASFDLVYSS 113
Cdd:PRK10258  34 LLAMLPQRKFThvlDAGCGPGWMSRYWRERGS-QVTALDLSPPMLAQARQ--KDAADHYLAGDIESLPLATATFDLAWSN 110

                         90       100
                 ....*....|....*....|....*....
gi 479375206 114 LAFHYIRDFPRILKTIHAALRPDGRFVFT 142
Cdd:PRK10258 111 LAVQWCGNLSTALRELYRVVRPGGVVAFT 139
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-145 5.25e-18

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: 77.09  E-value: 5.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  45 DIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQ---DDAVCYIQADMERL-ELPEASFDLVYSSLAFHYI- 119
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallADNVEVLKGDAEELpPEADESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|....*.
gi 479375206 120 RDFPRILKTIHAALRPDGRFVFTIEH 145
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-146 1.02e-30

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: 111.62  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  28 APEWPVVRSLLPDLT---GRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDA--VCYIQADMERLEL 102
Cdd:COG2226    5 AARYDGREALLAALGlrpGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGlnVEFVVGDAEDLPF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 479375206 103 PEASFDLVYSSLAFHYIRDFPRILKTIHAALRPDGRFVFTIEHP 146
Cdd:COG2226   84 PDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 41-142 4.23e-30

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: 109.34  E-value: 4.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  41 LTGRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIR 120
Cdd:COG2227   23 PAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLP 101

                         90       100
                 ....*....|....*....|..
gi 479375206 121 DFPRILKTIHAALRPDGRFVFT 142
Cdd:COG2227  102 DPAALLRELARLLKPGGLLLLS 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-141 3.74e-29

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 105.82  E-value: 3.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   48 DLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIRDFPRILK 127
Cdd:pfam08241   2 DVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 479375206  128 TIHAALRPDGRFVF 141
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-137 1.30e-28

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 104.57  E-value: 1.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   46 IADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQDDA--VCYIQADMERLELPEASFDLVYSSLAFHYI--RD 121
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGlnVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80

                          90
                  ....*....|....*.
gi 479375206  122 FPRILKTIHAALRPDG 137
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
38-145 7.59e-27

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 102.38  E-value: 7.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  38 LPDLTGRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDAVcyIQADMERLELPEASFDLVYSSLAFH 117
Cdd:COG4976   42 LPPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKGVYDRL--LVADLADLAEPDGRFDLIVAADVLT 118

                         90       100
                 ....*....|....*....|....*...
gi 479375206 118 YIRDFPRILKTIHAALRPDGRFVFTIEH 145
Cdd:COG4976  119 YLGDLAAVFAGVARALKPGGLFIFSVED 146
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
43-142 1.37e-26

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 99.13  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  43 GRDIADLGCGFGWFCR-FAREQGAASVTGYDLSQNMLERARRdtQDDAVCYIQADMERLELPEaSFDLVYSSLAFHYIRD 121
Cdd:COG4106    2 PRRVLDLGCGTGRLTAlLAERFPGARVTGVDLSPEMLARARA--RLPNVRFVVADLRDLDPPE-PFDLVVSNAALHWLPD 78

                         90       100
                 ....*....|....*....|.
gi 479375206 122 FPRILKTIHAALRPDGRFVFT 142
Cdd:COG4106   79 HAALLARLAAALAPGGVLAVQ 99
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 46-143 7.13e-21

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: 88.11  E-value: 7.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   46 IADLGCGFGWFCRFAREQG-AASVTGYDLSQNMLERARRDtQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIRDFPR 124
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK-LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQ 116

                          90
                  ....*....|....*....
gi 479375206  125 ILKTIHAALRPDGRFVFTI 143
Cdd:TIGR02072 117 ALSELARVLKPGGLLAFST 135
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 37-142 1.15e-20

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 87.89  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  37 LLPDLTGRDIA---DLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRdtQDDAVCYIQADMERLELPEASFDLVYSS 113
Cdd:PRK10258  34 LLAMLPQRKFThvlDAGCGPGWMSRYWRERGS-QVTALDLSPPMLAQARQ--KDAADHYLAGDIESLPLATATFDLAWSN 110

                         90       100
                 ....*....|....*....|....*....
gi 479375206 114 LAFHYIRDFPRILKTIHAALRPDGRFVFT 142
Cdd:PRK10258 111 LAVQWCGNLSTALRELYRVVRPGGVVAFT 139
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 43-143 4.14e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 81.51  E-value: 4.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  43 GRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQ----DDAVCYIQADMERLELPEaSFDLVYSSLAFHY 118
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAeaglADRVEVRLADYRDLPADG-QFDAIVSIGMFEH 130

                         90       100
                 ....*....|....*....|....*..
gi 479375206 119 I--RDFPRILKTIHAALRPDGRFVFTI 143
Cdd:COG2230  131 VgpENYPAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 26-153 4.58e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 82.27  E-value: 4.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  26 EGAPEWPVVRSLLPDLT-GRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQD---DAVCYIQADM-ERL 100
Cdd:COG0500    9 ELLPGLAALLALLERLPkGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKaglGNVEFLVADLaELD 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 479375206 101 ELPEASFDLVYSSLAFHYIRDFPR--ILKTIHAALRPDGRFVFTIEHPIFMASLA 153
Cdd:COG0500   89 PLPAESFDLVVAFGVLHHLPPEEReaLLRELARALKPGGVLLLSASDAAAALSLA 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-145 5.25e-18

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: 77.09  E-value: 5.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  45 DIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQ---DDAVCYIQADMERL-ELPEASFDLVYSSLAFHYI- 119
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallADNVEVLKGDAEELpPEADESFDVIISDPPLHHLv 80

                         90       100
                 ....*....|....*....|....*.
gi 479375206 120 RDFPRILKTIHAALRPDGRFVFTIEH 145
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLVL 106
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-139 5.06e-17

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 74.33  E-value: 5.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   48 DLGCGFGWFCRFAREQGA-ASVTGYDLSQNMLERAR----RDTQDDAVCYIQADMERLELPEASFDLVYSSLAFHYIRDF 122
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPgLEYTGLDISPAALEAARerlaALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLADP 81

                          90
                  ....*....|....*..
gi 479375206  123 PRILKTIHAALRPDGRF 139
Cdd:pfam08242  82 RAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 48-185 5.74e-16

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 72.83  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   48 DLGCGFGWFCRFAREQGA--ASVTGYDLSQNMLERARRDTQD---DAVCYIQADMERLE--LPEASFDLVYSSLAFHYIR 120
Cdd:pfam13847   9 DLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKlgfDNVEFEQGDIEELPelLEDDKFDVVISNCVLNHIP 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479375206  121 DFPRILKTIHAALRPDGRFVftIEHPIFMASLaPGWIEEGNGQKRWPVDHyAVEGERQTDWLAEG 185
Cdd:pfam13847  89 DPDKVLQEILRVLKPGGRLI--ISDPDSLAEL-PAHVKEDSTYYAGCVGG-AILKKKLYELLEEA 149
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-142 1.53e-15

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 72.08  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   33 VVRSLLPDLTGRDIADLGCGFGWFCRFAREQGAaSVTGYDLSQNMLERARRDTQDDavcyiQADMERLELPEASFDLVYS 112
Cdd:pfam13489  13 LLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIAIERALLNVRFD-----QFDEQEAAVPAGKFDVIVA 86

                          90       100       110
                  ....*....|....*....|....*....|
gi 479375206  113 SLAFHYIRDFPRILKTIHAALRPDGRFVFT 142
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGLLLLS 116
PRK08317 PRK08317
hypothetical protein; Provisional
 48-140 3.46e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 72.66  E-value: 3.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  48 DLGCGFGWFCR-FAREQGAAS-VTGYDLSQNMLERARRDTQDDA--VCYIQADMERLELPEASFDLVYSSLAFHYIRDFP 123
Cdd:PRK08317  25 DVGCGPGNDAReLARRVGPEGrVVGIDRSEAMLALAKERAAGLGpnVEFVRGDADGLPFPDGSFDAVRSDRVLQHLEDPA 104

                         90
                 ....*....|....*..
gi 479375206 124 RILKTIHAALRPDGRFV 140
Cdd:PRK08317 105 RALAEIARVLRPGGRVV 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 46-140 3.23e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 64.40  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  46 IADLGCGFG-WFCRFAREQGA-ASVTGYDLSQNML----ERARRDTQDDAVCYIQADMERLELPEASFDLVysSLAFHyI 119
Cdd:PRK00216  55 VLDLACGTGdLAIALAKAVGKtGEVVGLDFSEGMLavgrEKLRDLGLSGNVEFVQGDAEALPFPDNSFDAV--TIAFG-L 131

                         90       100
                 ....*....|....*....|....
gi 479375206 120 RDFPRI---LKTIHAALRPDGRFV 140
Cdd:PRK00216 132 RNVPDIdkaLREMYRVLKPGGRLV 155
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-140 1.21e-10

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 59.76  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   40 DLTGRDIADLGCGFG-WFCRFAREQGAA-SVTGYDLSQNMLERARRDTQDDA---VCYIQADMERLELPEASFDLVYSSL 114
Cdd:pfam01209  40 VKRGNKFLDVAGGTGdWTFGLSDSAGSSgKVVGLDINENMLKEGEKKAKEEGkynIEFLQGNAEELPFEDDSFDIVTISF 119

                          90       100
                  ....*....|....*....|....*.
gi 479375206  115 AFHYIRDFPRILKTIHAALRPDGRFV 140
Cdd:pfam01209 120 GLRNFPDYLKVLKEAFRVLKPGGRVV 145
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 38-141 8.93e-10

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: 56.74  E-value: 8.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  38 LPDLTGRDIADLGCGFGWF-CRFAREQGAASVTGYDLSQNMLERARR---DTQDDAVCYIQADMeRLELPEASFDLVYSS 113
Cdd:COG2813   45 LPEPLGGRVLDLGCGYGVIgLALAKRNPEARVTLVDVNARAVELARAnaaANGLENVEVLWSDG-LSGVPDGSFDLILSN 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 479375206 114 LAFH---YIRDFP--RILKTIHAALRPDGRFVF 141
Cdd:COG2813  124 PPFHagrAVDKEVahALIADAARHLRPGGELWL 156
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 48-166 3.67e-09

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 55.80  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   48 DLGCGFGWFCRFAREQGAASVTGYDLSQNMLERAR-----RDTQDDAVCYIQaDMERLELPeasFDLVYSSLAFHYI--R 120
Cdd:pfam02353  67 DIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARkrvaaEGLARKVEVLLQ-DYRDFDEP---FDRIVSVGMFEHVghE 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 479375206  121 DFPRILKTIHAALRPDGRFVFtieHPIFMasLAPGWIEEGNGQKRW 166
Cdd:pfam02353 143 NYDTFFKKLYNLLPPGGLMLL---HTITG--LHPDETSERGLPLKF 183
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
37-110 2.72e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 52.60  E-value: 2.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479375206  37 LLPDLTGRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARR--DTQDDAVCYIQADMERLELPEaSFDLV 110
Cdd:COG2263   40 LRGDIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIAREnaERLGVRVDFIRADVTRIPLGG-SVDTV 114
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 21-142 5.65e-08

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 53.22  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  21 SVHGLEGAPEWPVVRSLLPdltGRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNM----LERA--RRdtqddavCYIQ 94
Cdd:PLN02336 248 STGGLETTKEFVDKLDLKP---GQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMisfaLERAigRK-------CSVE 317

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 479375206  95 ---ADMERLELPEASFDLVYSSLAFHYIRDFPRILKTIHAALRPDGRFVFT 142
Cdd:PLN02336 318 fevADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLIS 368
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 35-137 8.19e-08

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 51.87  E-value: 8.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  35 RSLL---PDLTGRDIADLGCGFGWFCRFAREQ-GAASVTGYDLSQNMLERARRDTQDdaVCYIQADMERLElPEASFDLV 110
Cdd:PRK01683  21 RDLLarvPLENPRYVVDLGCGPGNSTELLVERwPAARITGIDSSPAMLAEARSRLPD--CQFVEADIASWQ-PPQALDLI 97

                         90       100
                 ....*....|....*....|....*..
gi 479375206 111 YSSLAFHYIRDFPRILKTIHAALRPDG 137
Cdd:PRK01683  98 FANASLQWLPDHLELFPRLVSLLAPGG 124
arsM PRK11873
arsenite methyltransferase;
48-140 9.20e-08

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 51.87  E-value: 9.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  48 DLGCGFGWFCRFAREQGAAS--VTGYDLSQNMLERARRDTQD---DAVCYIQADMERLELPEASFDLVYSSLAFHYIRDF 122
Cdd:PRK11873  83 DLGSGGGFDCFLAARRVGPTgkVIGVDMTPEMLAKARANARKagyTNVEFRLGEIEALPVADNSVDVIISNCVINLSPDK 162

                         90
                 ....*....|....*...
gi 479375206 123 PRILKTIHAALRPDGRFV 140
Cdd:PRK11873 163 ERVFKEAFRVLKPGGRFA 180
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 46-142 1.09e-07

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 51.51  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  46 IADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQDDAVCYIQA-DMERLELPEASFDLVYSSLAFHYI--RDF 122
Cdd:PTZ00098  56 VLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEAnDILKKDFPENTFDMIYSRDAILHLsyADK 135

                         90       100
                 ....*....|....*....|
gi 479375206 123 PRILKTIHAALRPDGRFVFT 142
Cdd:PTZ00098 136 KKLFEKCYKWLKPNGILLIT 155
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 38-142 3.99e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 46.75  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  38 LPDLTGRDIADLGCGFGWFC-RFAREqgAASVTGYDLSQNMLERARRDTQ----DDAVCYIQADMERLelpEASFDLVys 112
Cdd:PRK07580  59 DGDLTGLRILDAGCGVGSLSiPLARR--GAKVVASDISPQMVEEARERAPeaglAGNITFEVGDLESL---LGRFDTV-- 131

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 479375206 113 sLAF----HYIR-DFPRILKtiHAALRPDGRFVFT 142
Cdd:PRK07580 132 -VCLdvliHYPQeDAARMLA--HLASLTRGSLIFT 163
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 38-139 4.83e-06

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: 45.66  E-value: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   38 LPDLTGRDIADLGCGFGWF-CRFAREQGAASVTGYDLSQNMLERARRDTQD---DAVCYIQADMeRLELPEASFDLVYSS 113
Cdd:pfam05175  27 LPKDLSGKVLDLGCGAGVLgAALAKESPDAELTMVDINARALESARENLAAnglENGEVVASDV-YSGVEDGKFDLIISN 105

                          90       100       110
                  ....*....|....*....|....*....|.
gi 479375206  114 LAFHYIRDFP-----RILKTIHAALRPDGRF 139
Cdd:pfam05175 106 PPFHAGLATTynvaqRFIADAKRHLRPGGEL 136
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
19-137 1.39e-05

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 45.62  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  19 PRSVHGLEGAPEWpvvRS------LLP---DLTGRDIADLGCGFGWFC-RFArEQGAASVTGYDLSQNML---ERARR-D 84
Cdd:PRK15068  93 PFSLFGIHIDTEW---RSdwkwdrVLPhlsPLKGRTVLDVGCGNGYHMwRML-GAGAKLVVGIDPSQLFLcqfEAVRKlL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 479375206  85 TQDDAVCYIQADMERLELPEAsFDLVYsSLAFHYIRDFP-RILKTIHAALRPDG 137
Cdd:PRK15068 169 GNDQRAHLLPLGIEQLPALKA-FDTVF-SMGVLYHRRSPlDHLKQLKDQLVPGG 220
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 43-140 2.34e-05

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 43.73  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   43 GRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARrdtQDDAVCYIQADMERLELPEA-------SFDLVYSSLA 115
Cdd:pfam01728  22 GKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLWKPR---NDPGVTFIQGDIRDPETLDLleellgrKVDLVLSDGS 98

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 479375206  116 F----HYIRDFPRILKTIHAA-------LRPDGRFV 140
Cdd:pfam01728  99 PfisgNKVLDHLRSLDLVKAAlevalelLRKGGNFV 134
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 39-143 3.78e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 43.91  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  39 PDLTGRDIADLGCGFGWFCR-FAREQGAASVTGYDLSQNMLERARRDTQDDAVcyiqADMeRLELPEASFDLVYSSLAFH 117
Cdd:PRK14103  26 GAERARRVVDLGCGPGNLTRyLARRWPGAVIEALDSSPEMVAAARERGVDART----GDV-RDWKPKPDTDVVVSNAALQ 100

                         90       100
                 ....*....|....*....|....*.
gi 479375206 118 YIRDFPRILKTIHAALRPDGRFVFTI 143
Cdd:PRK14103 101 WVPEHADLLVRWVDELAPGSWIAVQV 126
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 46-141 1.33e-04

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: 42.05  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  46 IADLGCGFG-----WFCRFAreqgAASVTGYDLSQNMLERARRDTQ----DDAVCYIQADMERL--ELPEASFDLVYS-- 112
Cdd:COG4123   41 VLDLGTGTGvialmLAQRSP----GARITGVEIQPEAAELARRNVAlnglEDRITVIHGDLKEFaaELPPGSFDLVVSnp 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 479375206 113 ----------------SLAFHYIR-DFPRILKTIHAALRPDGRFVF 141
Cdd:COG4123  117 pyfkagsgrkspdearAIARHEDAlTLEDLIRAAARLLKPGGRFAL 162
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 41-141 1.57e-04

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 41.53  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206   41 LTGRDIAD---LGCGFGWFCRFAREQgAASVTGYDLSQNMLERAR-RDTQDDAVCYIQADMERLELpEASFDLVYSSLAF 116
Cdd:pfam05401  39 LGDGDAADaleIGCAAGAFTEMLAIL-CERLTVVDLMPEAIAKAQeRTGKWSDIIWHECDICQFDL-NAKFDLIICAEVL 116

                          90       100
                  ....*....|....*....|....*...
gi 479375206  117 HYIRDFPRI---LKTIHAALRPDGRFVF 141
Cdd:pfam05401 117 YYIHDKEELhaaIENIVQLLAPDEQFIF 144
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 34-110 3.04e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 41.70  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  34 VRSLLPDLTGRDIADLGCGFGWF-CRFAReqGAASVTGYDLSQNMLERARRDTQD---DAVCYIQADMERL---ELPEAS 106
Cdd:COG2265  225 ALEWLDLTGGERVLDLYCGVGTFaLPLAR--RAKKVIGVEIVPEAVEDARENARLnglKNVEFVAGDLEEVlpeLLWGGR 302


                 ....
gi 479375206 107 FDLV 110
Cdd:COG2265  303 PDVV 306
PLN02244 PLN02244
tocopherol O-methyltransferase
 44-112 6.24e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.50  E-value: 6.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 479375206  44 RDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQD----DAVCYIQADMERLELPEASFDLVYS 112
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAqglsDKVSFQVADALNQPFEDGQFDLVWS 192
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
43-156 1.90e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.48  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  43 GRDIADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARR----DTQDDAVCYIQADMERLELPEAsFDLVYSSLAFHY 118
Cdd:COG4076   36 GDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRiiaaNGLSDRITVINADATDLDLPEK-ADVIISEMLDTA 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 479375206 119 IRDfPRILKTIHAA----LRPDGRF----VFTIEHPIFMASLAPGW 156
Cdd:COG4076  115 LLD-EGQVPILNHArkrlLKPGGRIiperITNAAQPVESPVDAEGF 159
PRK06202 PRK06202
hypothetical protein; Provisional
 32-127 2.04e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 38.44  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  32 PVVRSLLPDLTGRDIADLGCGFG-----WFCRFAREQGAASVTGYDLSQNMLERARRDTQDDAVCYIQADMERLELPEAS 106
Cdd:PRK06202  50 RLLRPALSADRPLTLLDIGCGGGdlaidLARWARRDGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGER 129

                         90       100
                 ....*....|....*....|...
gi 479375206 107 FDLVYSSLAFHYIRD--FPRILK 127
Cdd:PRK06202 130 FDVVTSNHFLHHLDDaeVVRLLA 152
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 30-121 2.10e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.96  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  30 EWPVVRSLLPDLTGRDIADLGCGFGwfcRFARE--QGAASVTGYDLSQNMLERARR-DTQDDAVCYIQADM--ERLELPE 104
Cdd:PLN02336  25 ERPEILSLLPPYEGKSVLELGAGIG---RFTGElaKKAGQVIALDFIESVIKKNESiNGHYKNVKFMCADVtsPDLNISD 101

                         90
                 ....*....|....*..
gi 479375206 105 ASFDLVYSSLAFHYIRD 121
Cdd:PLN02336 102 GSVDLIFSNWLLMYLSD 118
PRK05785 PRK05785
hypothetical protein; Provisional
 46-140 3.07e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 38.13  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  46 IADLGCGFGWFCRFAREQGAASVTGYDLSQNMLERArrDTQDDAVcyiQADMERLELPEASFDLVYSSLAFH-------Y 118
Cdd:PRK05785  55 VLDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMN--LVADDKV---VGSFEALPFRDKSFDVVMSSFALHasdniekV 129

                         90       100
                 ....*....|....*....|....*
gi 479375206 119 IRDFPRILKTIHAAL---RPDGRFV 140
Cdd:PRK05785 130 IAEFTRVSRKQVGFIamgKPDNVIK 154
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 64-141 3.23e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 38.24  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  64 GAASVTGYDLSQNMLERARRDTQ----DDAVCYIQAD----MERLELPEASFDLV------YSSLAFHY---IRDFPRIL 126
Cdd:COG1092  238 GAKSVTSVDLSATALEWAKENAAlnglDDRHEFVQADafdwLRELAREGERFDLIildppaFAKSKKDLfdaQRDYKDLN 317

                         90
                 ....*....|....*
gi 479375206 127 KTIHAALRPDGRFVF 141
Cdd:COG1092  318 RLALKLLAPGGILVT 332
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
48-139 8.89e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 37.13  E-value: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375206  48 DLGCGFGWFCRFAREQGAASVTGYDLSQNMLERARRDTQDDAVCYIQADMERLelpEASFDLVYSSLAFHYI--RDFPRI 125
Cdd:PRK11705 173 DIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGLPVEIRLQDYRDL---NGQFDRIVSVGMFEHVgpKNYRTY 249

                         90
                 ....*....|....
gi 479375206 126 LKTIHAALRPDGRF 139
Cdd:PRK11705 250 FEVVRRCLKPDGLF 263
 
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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