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Conserved domains on  [gi|1690525108|ref|WP_139371096|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Xanthomonas cissicola]

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 ...
 81-190 6.08e-20

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: 83.14  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAGEGA-ILELGCGNGWLSHLLAQsLQREVCGIDVNRTELsQAARVFGHATGLSFIAGDIQTVALPREVFDII 159
Cdd:COG2227    14 LAALLARLLPAGGrVLDVGCGTGRLALALAR-RGADVTGVDISPEAL-EIARERAAELNVDFVQGDLEDLPLEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1690525108 160 VLPACVQYFADPGALIERLLAHLREDGVLHI 190
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 81-190 6.08e-20

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: 83.14  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAGEGA-ILELGCGNGWLSHLLAQsLQREVCGIDVNRTELsQAARVFGHATGLSFIAGDIQTVALPREVFDII 159
Cdd:COG2227    14 LAALLARLLPAGGrVLDVGCGTGRLALALAR-RGADVTGVDISPEAL-EIARERAAELNVDFVQGDLEDLPLEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1690525108 160 VLPACVQYFADPGALIERLLAHLREDGVLHI 190
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-186 6.87e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.44  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQA-ARVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFADPG 172
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERArERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 1690525108 173 --ALIERLLAHLREDG 186
Cdd:pfam13649  81 leAALREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 93-189 5.97e-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: 5.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  93 AILELGCGNGWLS-HLLAQSLQREVCGIDVNRTELSQAARVFGhaTGLSFIAGDIQTVALPREVFDIIVLPACVQYFADP 171
Cdd:TIGR02072  37 SVLDIGCGTGYLTrALLKRFPQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDL 114

                          90
                  ....*....|....*...
gi 1690525108 172 GALIERLLAHLREDGVLH 189
Cdd:TIGR02072 115 SQALSELARVLKPGGLLA 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-190 2.43e-09

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: 53.59  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIDVNR--TELSQAARVFGHATGLSFIAGDIQTVAL-PREVFDIIVL-PACVQYFA 169
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPvaLELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISdPPLHHLVE 81

                          90       100
                  ....*....|....*....|.
gi 1690525108 170 DPGALIERLLAHLREDGVLHI 190
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 94-193 5.12e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.63  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQRE--VCGIDVNRTELSQAA-RVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFAD 170
Cdd:PRK08317   23 VLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLED 102

                          90       100
                  ....*....|....*....|...
gi 1690525108 171 PGALIERLLAHLREDGVLHILDS 193
Cdd:PRK08317  103 PARALAEIARVLRPGGRVVVLDT 125
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 81-190 6.08e-20

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: 83.14  E-value: 6.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAGEGA-ILELGCGNGWLSHLLAQsLQREVCGIDVNRTELsQAARVFGHATGLSFIAGDIQTVALPREVFDII 159
Cdd:COG2227    14 LAALLARLLPAGGrVLDVGCGTGRLALALAR-RGADVTGVDISPEAL-EIARERAAELNVDFVQGDLEDLPLEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1690525108 160 VLPACVQYFADPGALIERLLAHLREDGVLHI 190
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
92-190 1.12e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 78.71  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  92 GAILELGCGNGWLSHLLAQSL-QREVCGIDVNRTELSQAARvfgHATGLSFIAGDIQTVALPREvFDIIVLPACVQYFAD 170
Cdd:COG4106     3 RRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARA---RLPNVRFVVADLRDLDPPEP-FDLVVSNAALHWLPD 78

                          90       100
                  ....*....|....*....|
gi 1690525108 171 PGALIERLLAHLREDGVLHI 190
Cdd:COG4106    79 HAALLARLAAALAPGGVLAV 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 81-192 2.23e-16

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 73.87  E-value: 2.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAGEgAILELGCGNGWLSHLLAQsLQREVCGIDVNRTELSQAARVFGHA-TGLSFIAGDIQTVALPREVFDII 159
Cdd:COG2226    14 LLAALGLRPGA-RVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAgLNVEFVVGDAEDLPFPDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1690525108 160 VLPACVQYFADPGALIERLLAHLREDGVLHILD 192
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-186 6.87e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.44  E-value: 6.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQA-ARVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFADPG 172
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERArERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 1690525108 173 --ALIERLLAHLREDG 186
Cdd:pfam13649  81 leAALREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 93-189 5.97e-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: 5.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  93 AILELGCGNGWLS-HLLAQSLQREVCGIDVNRTELSQAARVFGhaTGLSFIAGDIQTVALPREVFDIIVLPACVQYFADP 171
Cdd:TIGR02072  37 SVLDIGCGTGYLTrALLKRFPQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDL 114

                          90
                  ....*....|....*...
gi 1690525108 172 GALIERLLAHLREDGVLH 189
Cdd:TIGR02072 115 SQALSELARVLKPGGLLA 132
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 95-190 1.35e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.60  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  95 LELGCGNGWLSHLLAQSLqREVCGIDVNrTELSQAARVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFADPGAL 174
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDIS-PEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*.
gi 1690525108 175 IERLLAHLREDGVLHI 190
Cdd:pfam08241  79 LREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
64-188 3.40e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 60.78  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  64 KLGATLEWRVRALsssLLAQHLATHAGEGA--ILELGCGNGWLSHLLAQsLQREVCGIDVNRTELSQAARvfgHATGLSF 141
Cdd:COG4976    21 ALVEDLGYEAPAL---LAEELLARLPPGPFgrVLDLGCGTGLLGEALRP-RGYRLTGVDLSEEMLAKARE---KGVYDRL 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1690525108 142 IAGDIQTVALPREVFDIIVLPACVQYFADPGALIERLLAHLREDGVL 188
Cdd:COG4976    94 LVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLF 140
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 94-192 1.89e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.81  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSL--QREVCGIDVNRTELSQA---ARVFGhATGLSFIAGDIQ--TVALPREVFDIIVLPACVQ 166
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELgpNAEVVGIDISEEAIEKArenAQKLG-FDNVEFEQGDIEelPELLEDDKFDVVISNCVLN 85

                          90       100
                  ....*....|....*....|....*.
gi 1690525108 167 YFADPGALIERLLAHLREDGVLHILD 192
Cdd:pfam13847  86 HIPDPDKVLQEILRVLKPGGRLIISD 111
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 81-247 2.61e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.77  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAGEGAILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQAARVFGHAT--GLSFIAGDI-QTVALPREVFD 157
Cdd:COG0500    17 LLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgNVEFLVADLaELDPLPAESFD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108 158 IIVLPACVQYF--ADPGALIERLLAHLREDGVLhILDSPLYATPQQGQESAARSLRYFTE----LGVPELAAHYHQHTYA 231
Cdd:COG0500    97 LVVAFGVLHHLppEEREALLRELARALKPGGVL-LLSASDAAAALSLARLLLLATASLLEllllLRLLALELYLRALLAA 175

                         170
                  ....*....|....*.
gi 1690525108 232 TFDRFAVQWLFDPRRW 247
Cdd:COG0500   176 AATEDLRSDALLESAN 191
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 78-190 8.27e-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: 57.12  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  78 SSLLAQHLATHAGeGAILELGCGNGWLSHLLAQSL-QREVCGIDVNRT--ELSQA-ARVFGhATGLSFIAGDIqTVALPR 153
Cdd:COG2813    38 TRLLLEHLPEPLG-GRVLDLGCGYGVIGLALAKRNpEARVTLVDVNARavELARAnAAANG-LENVEVLWSDG-LSGVPD 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1690525108 154 EVFDIIVL--PACVQYFADPG---ALIERLLAHLREDGVLHI 190
Cdd:COG2813   115 GSFDLILSnpPFHAGRAVDKEvahALIADAARHLRPGGELWL 156
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 95-188 1.09e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 54.30  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  95 LELGCGNG-WLSHLLAQSLQREVCGIDVNRTELSQAARVFGHATGLS-----FIAGDIQTVALPRevFDIIVLPACVQYF 168
Cdd:pfam08242   1 LEIGCGTGtLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavrveLFQLDLGELDPGS--FDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|
gi 1690525108 169 ADPGALIERLLAHLREDGVL 188
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-190 2.43e-09

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: 53.59  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIDVNR--TELSQAARVFGHATGLSFIAGDIQTVAL-PREVFDIIVL-PACVQYFA 169
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPvaLELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISdPPLHHLVE 81

                          90       100
                  ....*....|....*....|.
gi 1690525108 170 DPGALIERLLAHLREDGVLHI 190
Cdd:cd02440    82 DLARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
 94-193 5.12e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 52.63  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQRE--VCGIDVNRTELSQAA-RVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFAD 170
Cdd:PRK08317   23 VLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLED 102

                          90       100
                  ....*....|....*....|...
gi 1690525108 171 PGALIERLLAHLREDGVLHILDS 193
Cdd:PRK08317  103 PARALAEIARVLRPGGRVVVLDT 125
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 80-190 1.32e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.93  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  80 LLAQHLATHAGEgAILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQA---ARVFGHATGLSFIAGDIQTVALPREvF 156
Cdd:COG2230    42 LILRKLGLKPGM-RVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYArerAAEAGLADRVEVRLADYRDLPADGQ-F 119

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1690525108 157 DIIVLPACVQYFADP--GALIERLLAHLREDGVLHI 190
Cdd:COG2230   120 DAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLL 155
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 78-190 9.31e-07

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 47.97  E-value: 9.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  78 SSLLAQHLATHAGeGAILELGCGNGWLSHLLAQ-SLQREVCGIDVNR--TELSQAARVFGHATGLSFIAGDIqTVALPRE 154
Cdd:pfam05175  20 SRLLLEHLPKDLS-GKVLDLGCGAGVLGAALAKeSPDAELTMVDINAraLESARENLAANGLENGEVVASDV-YSGVEDG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1690525108 155 VFDIIVL-PACVQYFADPGALIERLLA----HLREDGVLHI 190
Cdd:pfam05175  98 KFDLIISnPPFHAGLATTYNVAQRFIAdakrHLRPGGELWI 138
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 72-243 5.09e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.50  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  72 RVRALSSSLLAQHLATHAGEGAILELGCGNGWLSHLLAQSlQREVCGIDVNRtELSQAARVFGHATGLsfiagDIQTVAL 151
Cdd:pfam13489   4 QRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQ-GFSVTGVDPSP-IAIERALLNVRFDQF-----DEQEAAV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108 152 PREVFDIIVLPACVQYFADPGALIERLLAHLREDGVLHILDsplyatpqqgQESAARSLRYFTELGvpeLAAHYHQHtYA 231
Cdd:pfam13489  77 PAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLST----------PLASDEADRLLLEWP---YLRPRNGH-IS 142

                         170
                  ....*....|..
gi 1690525108 232 TFDRFAVQWLFD 243
Cdd:pfam13489 143 LFSARSLKRLLE 154
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-164 6.25e-06

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 44.87  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  79 SLLAQHLATHAGEGAILELGCGNGWLSHLLA-QSLQREVCGIDVnRTELSQAARV----FGHATGLSFIAGDIQT---VA 150
Cdd:pfam13679  14 APLLKELLDENGPITIVDHGAGKGYLGFILYyLKYGVRVYGIDT-RAELVEKANAlaqkLGFNKRMSFLEGTIAGstpVE 92

                          90
                  ....*....|....
gi 1690525108 151 LPREVFDIIVLPAC 164
Cdd:pfam13679  93 LPDRVDVVTALHAC 106
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 80-160 8.27e-05

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: 42.82  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  80 LLAqHLATHAGEGAILELGCGNGWLSHLLAQ-SLQREVCGIDVNRTELSQAARVFGH---ATGLSFIAGDIQTVA--LPR 153
Cdd:COG4123    28 LLA-AFAPVKKGGRVLDLGTGTGVIALMLAQrSPGARITGVEIQPEAAELARRNVALnglEDRITVIHGDLKEFAaeLPP 106


                  ....*..
gi 1690525108 154 EVFDIIV 160
Cdd:COG4123   107 GSFDLVV 113
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 80-188 1.21e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 42.62  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  80 LLAQhlATHAGEGAILELGCGNGWLSHLLAQSL-QREVCGIDVNRTELSQAARvfgHATGLSFIAGDIQTVALPREVfDI 158
Cdd:PRK01683   23 LLAR--VPLENPRYVVDLGCGPGNSTELLVERWpAARITGIDSSPAMLAEARS---RLPDCQFVEADIASWQPPQAL-DL 96

                          90       100       110
                  ....*....|....*....|....*....|
gi 1690525108 159 IVLPACVQYFADPGALIERLLAHLREDGVL 188
Cdd:PRK01683   97 IFANASLQWLPDHLELFPRLVSLLAPGGVL 126
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 94-179 1.29e-04

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 42.06  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIdvnrtELSQAARVFGHATGLSFIAGDIQT--VALPREVFDIIVLPACVQYFADP 171
Cdd:pfam07021  17 VLDLGCGDGTLLYLLKEEKGVDGYGI-----ELDAAGVAECVAKGLYVIQGDLDEglEHFPDKSFDYVILSQTLQATRNP 91


                  ....*...
gi 1690525108 172 GALIERLL 179
Cdd:pfam07021  92 REVLDEML 99
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
81-160 7.39e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 39.89  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  81 LAQHLATHAG-----EGA-ILELGCGNGWLShLLAQSLQ-REVCGIDVNRTELSQAAR-VFGHATGLSFIAGDIQTVALP 152
Cdd:COG2263    30 LAAELLHLAYlrgdiEGKtVLDLGCGTGMLA-IGAALLGaKKVVGVDIDPEALEIAREnAERLGVRVDFIRADVTRIPLG 108


                  ....*...
gi 1690525108 153 REvFDIIV 160
Cdd:COG2263   109 GS-VDTVV 115
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
91-160 1.17e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.25  E-value: 1.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1690525108  91 EGAILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQAARV---FGHATGLSFIAGDIQTVALPREVfDIIV 160
Cdd:COG4076    36 GDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIiaaNGLSDRITVINADATDLDLPEKA-DVII 107
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 80-188 1.31e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 38.92  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  80 LLAQHLATHAGEgAILELGCGNGWLSHLLAQsLQREVCGIDVNRtELSQAARVFGHATGL---SFIAGDIQTVALPREVF 156
Cdd:COG2518    57 RMLEALDLKPGD-RVLEIGTGSGYQAAVLAR-LAGRVYSVERDP-ELAERARERLAALGYdnvTVRVGDGALGWPEHAPF 133

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1690525108 157 DIIVLPACVQYFADPgalierLLAHLREDGVL 188
Cdd:COG2518   134 DRIIVTAAAPEVPEA------LLEQLAPGGRL 159
PLN02672 PLN02672
methionine S-methyltransferase
 96-122 3.00e-03

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 38.98  E-value: 3.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 1690525108   96 ELGCGNGWLSHLLAQS-LQREVCGIDVN 122
Cdd:PLN02672   124 ELGCGNGWISIAIAEKwLPSKVYGLDIN 151
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 94-192 5.05e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.19  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQREVCGIDVNRTELSQA-ARVFGHATGLSFIAGDIQTVALPREVFDIIVLPACVQYFADPG 172
Cdd:PLN02336  270 VLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFAlERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKP 349

                          90       100
                  ....*....|....*....|
gi 1690525108 173 ALIERLLAHLREDGVLHILD 192
Cdd:PLN02336  350 ALFRSFFKWLKPGGKVLISD 369
Methyltransf_33 pfam10017
Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family ...
 79-131 5.88e-03

Histidine-specific methyltransferase, SAM-dependent; The mycobacterial members of this family are expressed from part of the ergothioneine biosynthetic gene cluster. EGTD is the histidine methyltransferase that transfers three methyl groups to the alpha-amino moiety of histidine, in the first stage of the production of this histidine betaine derivative that carries a thiol group attached to the C2 atom of an imidazole ring.


Pssm-ID: 462944  Cd Length: 304  Bit Score: 37.45  E-value: 5.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1690525108  79 SLLAQH---LATHAGEGAILELGCGNGW-----LSHLLAQSLQREVCGIDVNRTELSQAAR 131
Cdd:pfam10017  47 AILRRHaaeIAALIPAAVLVELGSGSSRktrllLDALPAAGKPVTYVPIDISAEALEESAA 107
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 94-159 7.55e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.05  E-value: 7.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1690525108  94 ILELGCGNGWLSHLLAQSLQR--EVCGIDVNRTELSQA---ARVFGHATGLSFIAGDIQTVALPREVFDII 159
Cdd:PRK00216   55 VLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGrekLRDLGLSGNVEFVQGDAEALPFPDNSFDAV 125
 
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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