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Conserved domains on  [gi|515927906|ref|WP_017358489|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Bacillus]

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]; ...
 33-148 2.92e-17

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: 74.65  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHydDLHIDGLDASSTMKEQAHSRIKKRSKekQVRLYVGKIEKTRLPADQ 112
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGS 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515927906 113 YDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVV 123
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 33-148 2.92e-17

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: 74.65  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHydDLHIDGLDASSTMKEQAHSRIKKRSKekQVRLYVGKIEKTRLPADQ 112
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGS 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515927906 113 YDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVV 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-143 1.10e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   47 ILEIGYGPGYSIKHMLKHYDdLHIDGLDASSTMKEQAHSRIKKRSKekQVRLYVGKIEKTRLPADQYDKVLSVNNYTIWD 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 515927906  127 DPKAGAL--NLYHTLKPGG 143
Cdd:pfam13649  78 DPDLEAAlrEIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 47-146 3.92e-09

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: 54.60  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   47 ILEIGYGPGYSIKHMLKHYDDLHIDGLDASSTMKEQAHSRIKkrskeKQVRLYVGKIEKTRLPADQYDkvLSVNNYTI-W 125
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-----ENVQFICGDAEKLPLEDSSFD--LIVSNLALqW 110

                          90       100
                  ....*....|....*....|..
gi 515927906  126 -DDPKAGALNLYHTLKPGGKLV 146
Cdd:TIGR02072 111 cDDLSQALSELARVLKPGGLLA 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-148 2.71e-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: 50.12  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  46 NILEIGYGPGYSIKHMLKHYDDlHIDGLDASSTMKEQAhSRIKKRSKEKQVRLYVGKIEKTRLPAD-QYDKVLSVNNYTI 124
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*
gi 515927906 125 W-DDPKAGALNLYHTLKPGGKLVIV 148
Cdd:cd02440   79 LvEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 33-148 2.98e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.86  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHY-DDLHIDGLDASSTMKEQAHSRIKkrSKEKQVRLYVGKIEKTRLPAD 111
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGDADGLPFPDG 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515927906 112 QYDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:PRK08317  87 SFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 33-148 2.92e-17

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: 74.65  E-value: 2.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHydDLHIDGLDASSTMKEQAHSRIKKRSKekQVRLYVGKIEKTRLPADQ 112
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGS 87

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515927906 113 YDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVV 123
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
33-150 4.94e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 69.64  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHYDdlHIDGLDASSTMKEQAhsrikkRSKEKQVRLYVGKIEKTRLPADQ 112
Cdd:COG4976   36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY--RLTGVDLSEEMLAKA------REKGVYDRLLVADLADLAEPDGR 107

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515927906 113 YDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIVMQ 150
Cdd:COG4976  108 FDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVE 145
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 30-147 2.59e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 67.26  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  30 ALNQWAIQHLDLSDGENILEIGYGPGYSIKHMLKHYdDLHIDGLDASSTMKEQAHSRIKKRSKEKQVRLYVGKIEKTRLP 109
Cdd:COG2230   38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515927906 110 aDQYDKVLSVNNYTIWDDPKAGAL--NLYHTLKPGGKLVI 147
Cdd:COG2230  117 -GQFDAIVSIGMFEHVGPENYPAYfaKVARLLKPGGRLLL 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-143 1.10e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   47 ILEIGYGPGYSIKHMLKHYDdLHIDGLDASSTMKEQAHSRIKKRSKekQVRLYVGKIEKTRLPADQYDKVLSVNNYTIWD 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 515927906  127 DPKAGAL--NLYHTLKPGG 143
Cdd:pfam13649  78 DPDLEAAlrEIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-149 1.74e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.69  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  44 GENILEIGYGPGYSIKHMLKHYDDLHIDGLDASSTMKEQAhsrikkRSKEKQVRLYVGKIEKTRLPAdQYDKVLSvnNYT 123
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARA------RARLPNVRFVVADLRDLDPPE-PFDLVVS--NAA 72

                         90       100
                 ....*....|....*....|....*...
gi 515927906 124 I-W-DDPKAGALNLYHTLKPGGKLVIVM 149
Cdd:COG4106   73 LhWlPDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-147 1.51e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 58.45  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   48 LEIGYGPGYSIKHMLKHYddLHIDGLDASSTMKEQAhsriKKRSKEKQVRLYVGKIEKTRLPADQYDKVLSVNNYTIWDD 127
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELA----REKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 515927906  128 PKAGALNLYHTLKPGGKLVI 147
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-145 1.61e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.53  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   48 LEIGYGPGYSIKHMLKHYDDLHIDGLDASSTMKEQAHSRIKKRSKEKQVRLYVGKIEKTRLPADQYDKVLSVNNYTIWDD 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 515927906  128 PKAGALNLYHTLKPGGKL 145
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 28-147 3.52e-11

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: 58.11  E-value: 3.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  28 NKALNQWAIQHLDlsDGENILEIGYGPGYSIKHMLKHydDLHIDGLDASSTMKEQAhsriKKRSKEKQVRLYVGKIEKTR 107
Cdd:COG2227   11 DRRLAALLARLLP--AGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIA----RERAAELNVDFVQGDLEDLP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 515927906 108 LPADQYDKVLSvnNYTIW--DDPKAGALNLYHTLKPGGKLVI 147
Cdd:COG2227   83 LEDGSFDLVIC--SEVLEhlPDPAALLRELARLLKPGGLLLL 122
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 47-146 3.92e-09

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: 54.60  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   47 ILEIGYGPGYSIKHMLKHYDDLHIDGLDASSTMKEQAHSRIKkrskeKQVRLYVGKIEKTRLPADQYDkvLSVNNYTI-W 125
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-----ENVQFICGDAEKLPLEDSSFD--LIVSNLALqW 110

                          90       100
                  ....*....|....*....|..
gi 515927906  126 -DDPKAGALNLYHTLKPGGKLV 146
Cdd:TIGR02072 111 cDDLSQALSELARVLKPGGLLA 132
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 28-148 4.26e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 54.15  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  28 NKALNQWAIQHLDLSDGENILEIGYGPGYSIKHMLKHYDDlHIDGLDASSTMKEQAHSRIKKRsKEKQVRLYVGKIEKT- 106
Cdd:COG0500   11 LPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAKA-GLGNVEFLVADLAELd 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515927906 107 RLPADQYDKVLSVNNYTiWDDPK--AGAL-NLYHTLKPGGKLVIV 148
Cdd:COG0500   89 PLPAESFDLVVAFGVLH-HLPPEerEALLrELARALKPGGVLLLS 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-148 2.71e-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: 50.12  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  46 NILEIGYGPGYSIKHMLKHYDDlHIDGLDASSTMKEQAhSRIKKRSKEKQVRLYVGKIEKTRLPAD-QYDKVLSVNNYTI 124
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA-RVTGVDISPVALELA-RKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*
gi 515927906 125 W-DDPKAGALNLYHTLKPGGKLVIV 148
Cdd:cd02440   79 LvEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 33-148 2.98e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 51.86  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  33 QWAIQHLDLSDGENILEIGYGPGYSIKHMLKHY-DDLHIDGLDASSTMKEQAHSRIKkrSKEKQVRLYVGKIEKTRLPAD 111
Cdd:PRK08317   9 ARTFELLAVQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGDADGLPFPDG 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515927906 112 QYDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:PRK08317  87 SFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 35-148 6.29e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 51.43  E-value: 6.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  35 AIQHLDLSDGE-NILEIGYGPGYSIKHMLKHYDDLHIDGLDASStmkeqaHSRIKKRSKE--KQVRLYVGKIEKTRLPAD 111
Cdd:PLN02490 104 ALEPADLSDRNlKVVDVGGGTGFTTLGIVKHVDAKNVTILDQSP------HQLAKAKQKEplKECKIIEGDAEDLPFPTD 177

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515927906 112 QYDKVLSVNNYTIWDDPKAGALNLYHTLKPGGKLVIV 148
Cdd:PLN02490 178 YADRYVSAGSIEYWPDPQRGIKEAYRVLKIGGKACLI 214
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 41-171 3.39e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 42.48  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  41 LSDGENILEIGYGPGYSIKHMLKHY-DDLHIDGLDASSTMKEQAHSRIKKRSKEKQVRLYVGKIEKT--RLPADQYDKVL 117
Cdd:COG4122   14 LLGAKRILEIGTGTGYSTLWLARALpDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEVlpRLADGPFDLVF 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927906 118 svnnytIwDDPKAGALNLYHT----LKPGGKLVI--------VMQPREKGADANRTKEMGESILND 171
Cdd:COG4122   94 ------I-DADKSNYPDYLELalplLRPGGLIVAdnvlwhgrVADPARRDPSTRAIREFNEYLRED 152
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 35-147 1.42e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 41.29  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  35 AIQHLDLSDGENILEIGYGPGYSIKHMLKHYDDL-HIDGLDASSTMKEQAHSRIKKRSKEKQVRLYVGKIEKTRLPADQY 113
Cdd:PRK00216  43 TIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSF 122

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515927906 114 DkVLSVN----NYTiwdDPKAGALNLYHTLKPGGKLVI 147
Cdd:PRK00216 123 D-AVTIAfglrNVP---DIDKALREMYRVLKPGGRLVI 156
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 39-147 4.59e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.12  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906  39 LDLSDGENILEIGYGPGYSIKHMLKHYdDLHIDGLDASSTMKEQAHSRIKKRSkeKQVRLYVGKIEKTRLPADQYDKVLS 118
Cdd:PLN02336 262 LDLKPGQKVLDVGCGIGGGDFYMAENF-DVHVVGIDLSVNMISFALERAIGRK--CSVEFEVADCTKKTYPDNSFDVIYS 338

                         90       100
                 ....*....|....*....|....*....
gi 515927906 119 VNNYTIWDDPKAGALNLYHTLKPGGKLVI 147
Cdd:PLN02336 339 RDTILHIQDKPALFRSFFKWLKPGGKVLI 367
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 41-147 1.79e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.40  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927906   41 LSDGENILEIGYGPGY-SIKHMLKHYDDLHIDGLDASSTMKEQAHSRIKKrSKEKQVRLYVGKIEK--TRLPADQYDKVL 117
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHlSFELAEELGPNAEVVGIDISEEAIEKARENAQK-LGFDNVEFEQGDIEElpELLEDDKFDVVI 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 515927906  118 SvnNYTIWDDP-KAGALNLYHT-LKPGGKLVI 147
Cdd:pfam13847  80 S--NCVLNHIPdPDKVLQEILRvLKPGGRLII 109
 
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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