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Conserved domains on  [gi|1196866242|ref|WP_086311059|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Enterococcus sp. 3G1_DIV0629]

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 ...
 18-127 3.05e-18

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: 80.83  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  18 IAAQIKPGSKVLEFGPGNGRLTKHLigAKQ-CEVSIVELDKELFDFVSEFAQDG----FYGDIESFEwanyYAGQTFDYV 92
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALAL--ARRgADVTGVDISPEALEIARERAAELnvdfVQGDLEDLP----LEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPN 127
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-127 3.05e-18

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: 80.83  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  18 IAAQIKPGSKVLEFGPGNGRLTKHLigAKQ-CEVSIVELDKELFDFVSEFAQDG----FYGDIESFEwanyYAGQTFDYV 92
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALAL--ARRgADVTGVDISPEALEIARERAAELnvdfVQGDLEDLP----LEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPN 127
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 17-172 1.56e-15

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 74.00  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  17 KIAAQIKPGSKVLEFGPGNGRLTKHLiGAKQCEVSIVELDKELFDFVSEFAQ-DGFYGDIESFEwanyyaGQTFDYVLFA 95
Cdd:pfam13489  15 RLLPKLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAIERALLNVRfDQFDEQEAAVP------AGKFDVIVAR 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196866242  96 DVLEHLVDPGKTLKKVREFLNEEGEILITFPNLAhnsvmiDLFNNQLPWASYGLLDETHNSFYTHDGFQKVFEKAGL 172
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS------DEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGF 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 27-125 1.65e-08

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: 52.43  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  27 KVLEFGPGNGRLTKHLIGAKQCEVSIVELDKELFDFVSEFAQDGFYGDIE----SFEWANYYAGQTFDYVLFADVLEHLV 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEvlkgDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1196866242 103 -DPGKTLKKVREFLNEEGEILITF 125
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
rADc smart00650
Ribosomal RNA adenine dimethylases;
15-82 1.09e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 1.09e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196866242   15 VGKI--AAQIKPGSKVLEFGPGNGRLTKHLigAKQC-EVSIVELDKELFDFVSE-FAQDG----FYGDIESFEWAN 82
Cdd:smart00650   2 IDKIvrAANLRPGDTVLEIGPGKGALTEEL--LERAkRVTAIEIDPRLAPRLREkFAAADnltvIHGDALKFDLPK 75
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
20-76 6.16e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 41.81  E-value: 6.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1196866242  20 AQIKPGSKVLEFGPGNGRLTKHLigAKQCE-VSIVELDKELFDFVS-EFAQDGFYGDIE 76
Cdd:PRK14896   25 AEDTDGDPVLEIGPGKGALTDEL--AKRAKkVYAIELDPRLAEFLRdDEIAAGNVEIIE 81
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-127 3.05e-18

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: 80.83  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  18 IAAQIKPGSKVLEFGPGNGRLTKHLigAKQ-CEVSIVELDKELFDFVSEFAQDG----FYGDIESFEwanyYAGQTFDYV 92
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALAL--ARRgADVTGVDISPEALEIARERAAELnvdfVQGDLEDLP----LEDGSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPN 127
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 17-172 1.56e-15

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 74.00  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  17 KIAAQIKPGSKVLEFGPGNGRLTKHLiGAKQCEVSIVELDKELFDFVSEFAQ-DGFYGDIESFEwanyyaGQTFDYVLFA 95
Cdd:pfam13489  15 RLLPKLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAIERALLNVRfDQFDEQEAAVP------AGKFDVIVAR 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196866242  96 DVLEHLVDPGKTLKKVREFLNEEGEILITFPNLAhnsvmiDLFNNQLPWASYGLLDETHNSFYTHDGFQKVFEKAGL 172
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTPLAS------DEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGF 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 19-138 1.97e-11

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: 61.93  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  19 AAQIKPGSKVLEFGPGNGRLTKHLiGAKQCEVSIVELDKELFDFVSEFAQDGFY------GDIESFEWANyyagQTFDYV 92
Cdd:COG2226    17 ALGLRPGARVLDLGCGTGRLALAL-AERGARVTGVDISPEMLELARERAAEAGLnvefvvGDAEDLPFPD----GSFDLV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPNLAHNSVMIDLF 138
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 19-126 1.06e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 57.25  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  19 AAQIKPGSKVLEFGPGNGRLTKHLIGAKQCEVSIVELDKELFDFVSEFAQDGFYGDIESFEWANY---YAGQTFDYVLFA 95
Cdd:COG2230    46 KLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYrdlPADGQFDAIVSI 125

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1196866242  96 DVLEHLVDP--GKTLKKVREFLNEEGEILITFP 126
Cdd:COG2230   126 GMFEHVGPEnyPAYFAKVARLLKPGGRLLLHTP 158
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 22-127 7.65e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 54.73  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  22 IKPGSKVLEFGPGNGRLTKHLIG--AKQCEVSIVELDKELFDFVSEFAQDGFY-------GDIESFEwaNYYAGQTFDYV 92
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKARENAQKLGFdnvefeqGDIEELP--ELLEDDKFDVV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPN 127
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 18-130 1.51e-08

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: 54.77  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  18 IAAQIKPGSKVLEFGPGNGRLTKHLIGAKQCEVSIVELDKelfDFVSEFAQDGFY---GDIEsfEWANYYAGQTFDYVLF 94
Cdd:pfam07021   7 ILEWIPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDA---AGVAECVAKGLYviqGDLD--EGLEHFPDKSFDYVIL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1196866242  95 ADVLEHLVDPGKTLkkvREFLNEEGEILITFPNLAH 130
Cdd:pfam07021  82 SQTLQATRNPREVL---DEMLRIGRRCIVSFPNFGH 114
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 27-125 1.65e-08

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: 52.43  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  27 KVLEFGPGNGRLTKHLIGAKQCEVSIVELDKELFDFVSEFAQDGFYGDIE----SFEWANYYAGQTFDYVLFADVLEHLV 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEvlkgDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1196866242 103 -DPGKTLKKVREFLNEEGEILITF 125
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
24-125 7.31e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.21  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  24 PGSKVLEFGPGNGRLTKHLIGA-KQCEVSIVELDKELFdfvsEFAQDGF------YGDIESFEwanyyAGQTFDYVLFAD 96
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfPGARVTGVDLSPEML----ARARARLpnvrfvVADLRDLD-----PPEPFDLVVSNA 71

                          90       100
                  ....*....|....*....|....*....
gi 1196866242  97 VLEHLVDPGKTLKKVREFLNEEGEILITF 125
Cdd:COG4106    72 ALHWLPDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 28-119 3.08e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  28 VLEFGPGNGRLTKHLIGAKQCEVSIVELDKELFDFVSE-FAQDGFY-----GDIESFEwanyYAGQTFDYVLFADVLEHL 101
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARErAAEAGLNvefvqGDAEDLP----FPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 1196866242 102 VDPG--KTLKKVREFLNEEG 119
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 29-119 7.02e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 47.36  E-value: 7.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  29 LEFGPGNGRLTKHLIGA-KQCEVSIVELDKELFDFVSE-FAQDGFYgDIESFEWANY----YAGQTFDYVLFADVLEHLV 102
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlPGLEYTGLDISPAALEAARErLAALGLL-NAVRVELFQLdlgeLDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*..
gi 1196866242 103 DPGKTLKKVREFLNEEG 119
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-183 2.43e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.07  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  19 AAQIKPGSKVLEFGPGNGRLTKHLigAKQC-EVSIVELDKElfdFVSEFAQDGFY-----GDIESFEWAnyyaGQTFDYV 92
Cdd:COG4976    41 RLPPGPFGRVLDLGCGTGLLGEAL--RPRGyRLTGVDLSEE---MLAKAREKGVYdrllvADLADLAEP----DGRFDLI 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  93 LFADVLEHLVDPGKTLKKVREFLNEEGEILITFPNlahnsvmidlfnnqlpwasyglLDETHNSFYTHDGFQKVFEKAGL 172
Cdd:COG4976   112 VAADVLTYLGDLAAVFAGVARALKPGGLFIFSVED----------------------ADGSGRYAHSLDYVRDLLAAAGF 169

                         170
                  ....*....|.
gi 1196866242 173 fiNIEDYLYLA 183
Cdd:COG4976   170 --EVPGLLVVA 178
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 23-129 3.16e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.99  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  23 KPGSKVLEFGPGNGRLTKHLIGAKQCEVSIVELDKELFDFVSEFAQDGFYGDIE----SFEWANYYAGQTFDYVLFADVL 98
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEflvaDLAELDPLPAESFDLVVAFGVL 104

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1196866242  99 EHL--VDPGKTLKKVREFLNEEGEILITFPNLA 129
Cdd:COG0500   105 HHLppEEREALLRELARALKPGGVLLLSASDAA 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 29-123 2.10e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  29 LEFGPGNGRLTKHLigAKQCEVSI-VELDKELFDFVSEFAQDGFY----GDIESFEwanyYAGQTFDYVLFADVLEHLVD 103
Cdd:pfam08241   1 LDVGCGTGLLTELL--ARLGARVTgVDISPEMLELAREKAPREGLtfvvGDAEDLP----FPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1196866242 104 PGKTLKKVREFLNEEGEILI 123
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 15-89 6.77e-05

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 44.73  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196866242  15 VGKI--AAQIKPGSKVLEFGPGNGRLTKHLigAKQC-EVSIVELDKELFDFVSE-FAQDG----FYGDIESFEWANYYAG 86
Cdd:COG0030    26 IRRIvdAAGITPGDTVLEIGPGLGALTRAL--LERAaRVTAVEIDRRLAAILREtFAAYPnltvIEGDALKVDLPALAAG 103


                  ...
gi 1196866242  87 QTF 89
Cdd:COG0030   104 EPL 106
rADc smart00650
Ribosomal RNA adenine dimethylases;
15-82 1.09e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 1.09e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196866242   15 VGKI--AAQIKPGSKVLEFGPGNGRLTKHLigAKQC-EVSIVELDKELFDFVSE-FAQDG----FYGDIESFEWAN 82
Cdd:smart00650   2 IDKIvrAANLRPGDTVLEIGPGKGALTEEL--LERAkRVTAIEIDPRLAPRLREkFAAADnltvIHGDALKFDLPK 75
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
20-76 6.16e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 41.81  E-value: 6.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1196866242  20 AQIKPGSKVLEFGPGNGRLTKHLigAKQCE-VSIVELDKELFDFVS-EFAQDGFYGDIE 76
Cdd:PRK14896   25 AEDTDGDPVLEIGPGKGALTDEL--AKRAKkVYAIELDPRLAEFLRdDEIAAGNVEIIE 81
 
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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