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Conserved domains on  [gi|501219093|ref|WP_012262111|]
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class I SAM-dependent methyltransferase [Escherichia coli]

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]; ...
48-156 6.01e-18

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: 78.11  E-value: 6.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  48 INKKSHLLDLACSTGFSSREcFKKEGASAEGIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLGGCN 127
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFV 96
                         90       100
                 ....*....|....*....|....*....
gi 501219093 128 FAFIQNRLIALNETHRCLNHMGSMCISNF 156
Cdd:COG2226   97 LHHLPDPERALAEIARVLKPGGRLVVVDF 125
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
48-156 6.01e-18

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: 78.11  E-value: 6.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  48 INKKSHLLDLACSTGFSSREcFKKEGASAEGIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLGGCN 127
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFV 96
                         90       100
                 ....*....|....*....|....*....
gi 501219093 128 FAFIQNRLIALNETHRCLNHMGSMCISNF 156
Cdd:COG2226   97 LHHLPDPERALAEIARVLKPGGRLVVVDF 125
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
55-145 9.70e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 9.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   55 LDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLggCNFAF---- 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVV--SSGVLhhlp 77
                          90
                  ....*....|....*
gi 501219093  131 IQNRLIALNETHRCL 145
Cdd:pfam13649  78 DPDLEAALREIARVL 92
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
50-149 6.64e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 63.63  E-value: 6.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  50 KKSHLLDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKAKKLKANNLLKYYVADACDLPFEDNTFTHVlggcN 127
Cdd:PRK00216  51 PGDKVLDLACGTGDLAIALAKAVGKTGEvvGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAV----T 126
                         90       100
                 ....*....|....*....|....*.
gi 501219093 128 FAF----IQNRLIALNETHRCLNHMG 149
Cdd:PRK00216 127 IAFglrnVPDIDKALREMYRVLKPGG 152
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-154 8.53e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 46.65  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  54 LLDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNlLKYYVADACDLPF-EDNTFTHVLggCNFAFI- 131
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPeADESFDVII--SDPPLHh 78
                         90       100
                 ....*....|....*....|....*
gi 501219093 132 --QNRLIALNETHRCLNHMGSMCIS 154
Cdd:cd02440   79 lvEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
48-156 6.01e-18

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: 78.11  E-value: 6.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  48 INKKSHLLDLACSTGFSSREcFKKEGASAEGIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLGGCN 127
Cdd:COG2226   20 LRPGARVLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFV 96
                         90       100
                 ....*....|....*....|....*....
gi 501219093 128 FAFIQNRLIALNETHRCLNHMGSMCISNF 156
Cdd:COG2226   97 LHHLPDPERALAEIARVLKPGGRLVVVDF 125
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
55-145 9.70e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 9.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   55 LDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLggCNFAF---- 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVV--SSGVLhhlp 77
                          90
                  ....*....|....*
gi 501219093  131 IQNRLIALNETHRCL 145
Cdd:pfam13649  78 DPDLEAALREIARVL 92
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
26-154 4.70e-15

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 69.66  E-value: 4.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  26 MQQDNTPPGAEYTIDYWIKHgCINKKSHLLDLACSTGFSSREcFKKEGASAEGIDISESAVMVANEKAKKLKANnllkYY 105
Cdd:COG2227    1 MSDPDARDFWDRRLAALLAR-LLPAGGRVLDVGCGTGRLALA-LARRGADVTGVDISPEALEIARERAAELNVD----FV 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501219093 106 VADACDLPFEDNTFTHVLggCNFAF--IQNRLIALNETHRCLNHMGSMCIS 154
Cdd:COG2227   75 QGDLEDLPLEDGSFDLVI--CSEVLehLPDPAALLRELARLLKPGGLLLLS 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
55-145 6.66e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 68.46  E-value: 6.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   55 LDLACSTGFSSREcFKKEGASAEGIDISESAVmvanEKAKKLKANNLLKYYVADACDLPFEDNTFTHVLggCNFAF--IQ 132
Cdd:pfam08241   1 LDVGCGTGLLTEL-LARLGARVTGVDISPEML----ELAREKAPREGLTFVVGDAEDLPFPDNSFDLVL--SSEVLhhVE 73
                          90
                  ....*....|...
gi 501219093  133 NRLIALNETHRCL 145
Cdd:pfam08241  74 DPERALREIARVL 86
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
50-149 6.64e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 63.63  E-value: 6.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  50 KKSHLLDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKAKKLKANNLLKYYVADACDLPFEDNTFTHVlggcN 127
Cdd:PRK00216  51 PGDKVLDLACGTGDLAIALAKAVGKTGEvvGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAV----T 126
                         90       100
                 ....*....|....*....|....*.
gi 501219093 128 FAF----IQNRLIALNETHRCLNHMG 149
Cdd:PRK00216 127 IAFglrnVPDIDKALREMYRVLKPGG 152
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
48-156 8.47e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.89  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   48 INKKSHLLDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKAKKLKANNlLKYYVADACDLP--FEDNTFTHVL 123
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEvvGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPelLEDDKFDVVI 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 501219093  124 GGCNFAFIQNRLIALNETHRCLNHMGSMCISNF 156
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDP 112
PLN02244 PLN02244
tocopherol O-methyltransferase
55-119 3.44e-09

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 56.68  E-value: 3.44e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501219093  55 LDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNLLKYYVADACDLPFEDNTF 119
Cdd:PLN02244 123 VDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQF 187
PRK08317 PRK08317
hypothetical protein; Provisional
55-145 8.21e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  55 LDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKAKKLKANnlLKYYVADACDLPFEDNTFTHVLGGCNFAFIQ 132
Cdd:PRK08317  24 LDVGCGPGNDARELARRVGPEGRvvGIDRSEAMLALAKERAAGLGPN--VEFVRGDADGLPFPDGSFDAVRSDRVLQHLE 101
                         90
                 ....*....|...
gi 501219093 133 NRLIALNETHRCL 145
Cdd:PRK08317 102 DPARALAEIARVL 114
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
39-123 4.04e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.47  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  39 IDYWIKHGCINKKSHLLDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNLLKYYVADACDLPFeDNT 118
Cdd:COG2230   40 LDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPA-DGQ 118

                 ....*
gi 501219093 119 FTHVL 123
Cdd:COG2230  119 FDAIV 123
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
47-119 6.23e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 6.23e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501219093  47 CINKKSHLLDLACSTGFSSrECFKKEGASAEGIDISESAVMVAneKAKKLKANnllkYYVADACDLPFEDNTF 119
Cdd:COG4976   43 PPGPFGRVLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKA--REKGVYDR----LLVADLADLAEPDGRF 108
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
39-123 6.78e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.46  E-value: 6.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  39 IDYWIKHGCINKKSHLLDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNlLKYYVADACDL-PFEDN 117
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELdPLPAE 93

                 ....*.
gi 501219093 118 TFTHVL 123
Cdd:COG0500   94 SFDLVV 99
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
54-154 8.53e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 46.65  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  54 LLDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNlLKYYVADACDLPF-EDNTFTHVLggCNFAFI- 131
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPeADESFDVII--SDPPLHh 78
                         90       100
                 ....*....|....*....|....*
gi 501219093 132 --QNRLIALNETHRCLNHMGSMCIS 154
Cdd:cd02440   79 lvEDLARFLEEARRLLKPGGVLVLT 103
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-145 3.95e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 46.66  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   40 DYWIKHGCINKKSHLLDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKAKKLKANNLlKYYVADACDLPFEDN 117
Cdd:pfam01209  32 DFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKvvGLDINENMLKEGEKKAKEEGKYNI-EFLQGNAEELPFEDD 110
                          90       100
                  ....*....|....*....|....*...
gi 501219093  118 TFTHVLGGCNFAFIQNRLIALNETHRCL 145
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVL 138
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-154 2.74e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  52 SHLLDLACSTGFSSRE-CFKKEGASAEGIDISESAVmvanEKAKKLKANnlLKYYVADACDLPFEDnTFTHVLggCNFAF 130
Cdd:COG4106    3 RRVLDLGCGTGRLTALlAERFPGARVTGVDLSPEML----ARARARLPN--VRFVVADLRDLDPPE-PFDLVV--SNAAL 73
                         90       100
                 ....*....|....*....|....*.
gi 501219093 131 --IQNRLIALNETHRCLNHMGSMCIS 154
Cdd:COG4106   74 hwLPDHAALLARLAAALAPGGVLAVQ 99
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
55-146 5.27e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.20  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093   55 LDLACSTGFSSRECFKK-EGASAEGIDISESAVMVANEK--AKKLKANNLLKYYVADACDLPFEdnTFTHVLGGCNFAFI 131
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlPGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDLGELDPG--SFDVVVASNVLHHL 78
                          90
                  ....*....|....*
gi 501219093  132 QNRLIALNETHRCLN 146
Cdd:pfam08242  79 ADPRAVLRNIRRLLK 93
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
78-156 2.08e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 37.75  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  78 GIDISESAVMVANEKaKKLKANNLLK---YYVADACDLPFEDNTFTHVLGGCNFAFIQNRLIALNETHRCLNHMGSMCIS 154
Cdd:PLN02232   2 GLDFSSEQLAVAATR-QSLKARSCYKcieWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSIL 80

                 ..
gi 501219093 155 NF 156
Cdd:PLN02232  81 DF 82
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
42-110 3.16e-03

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 38.18  E-value: 3.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501219093   42 WIKHGCINK----------KSHLLDLACSTGFSSRECFKKEGASAEGIDISESAVMVANEKAKKLKANNLLKYYVADAC 110
Cdd:pfam03291  45 WIKSLLISLyasktfqnsnKRKVLDLGCGKGGDLEKWFKGGISQLIGTDIAEVSIEQCRERYNKLRSGNKSKYYKFDAE 123
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
54-145 9.15e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 36.79  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501219093  54 LLDLACSTGFSSRECFKKEGASAE--GIDISESAVMVANEKaKKLKANNLLK---YYVADACDLPFEDNTFTHVLGGCNF 128
Cdd:PLN02233  77 VLDLCCGSGDLAFLLSEKVGSDGKvmGLDFSSEQLAVAASR-QELKAKSCYKnieWIEGDATDLPFDDCYFDAITMGYGL 155
                         90
                 ....*....|....*..
gi 501219093 129 AFIQNRLIALNETHRCL 145
Cdd:PLN02233 156 RNVVDRLKAMQEMYRVL 172
 
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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