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Conserved domains on  [gi|428257455|gb|AFZ23405|]
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methylase involved in ubiquinone/menaquinone biosynthesis [Cylindrospermum stagnale PCC 7417]

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]; ...
 12-143 4.58e-20

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: 83.89  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  12 FEGAAEDYARYRAkyppaLFAKLAEifhfNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGAnN 91
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGL----RPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-N 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 428257455  92 ITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVLI 143
Cdd:COG2226   71 VEFVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVV 123
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 12-143 4.58e-20

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: 83.89  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  12 FEGAAEDYARYRAkyppaLFAKLAEifhfNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGAnN 91
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGL----RPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-N 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 428257455  92 ITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVLI 143
Cdd:COG2226   71 VEFVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVV 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-138 3.59e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.22  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   47 LDLGCGPGLMTIPLQSQFQ-EVVAVDPDPEMLKIAKQQASSVGAnNITWLEQGAELINSSLGVFQLVTIGRAFHWM---D 122
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdpD 80

                          90
                  ....*....|....*.
gi 428257455  123 RELVLERIYQLLSEDG 138
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-143 2.57e-12

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: 62.06  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  45 RLLDLGCGPGLMTIPLQSQ-FQEVVAVDPDPEMLKIAKQQASSVGANNITWLEQGAELINSSLGV-FQLVTIGRAFHW-- 120
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADEsFDVIISDPPLHHlv 80

                         90       100
                 ....*....|....*....|...
gi 428257455 121 MDRELVLERIYQLLSEDGGLVLI 143
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 12-142 9.90e-10

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: 57.30  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   12 FEGAAEDYARYR------AKYppaLFAKLAEIFHFNNQgRLLDLGCGPGLMTIPLQSQF--QEVVAVDPDPEMLKIAKQQ 83
Cdd:TIGR02072   2 FNKAAKTYDRHAkiqremAKR---LLALLKEKGIFIPA-SVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   84 ASSvganNITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVL 142
Cdd:TIGR02072  78 LSE----NVQFICGDAEKLPLEDSSFDLIVSNLALQWCdDLSQALSELARVLKPGGLLAF 133
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 45-112 7.51e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 7.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428257455  45 RLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVG-ANNITWLEQGAElinSSLGVFQLV 112
Cdd:PRK07580  66 RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGlAGNITFEVGDLE---SLLGRFDTV 131
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 12-143 4.58e-20

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: 83.89  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  12 FEGAAEDYARYRAkyppaLFAKLAEifhfNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGAnN 91
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGL----RPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-N 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 428257455  92 ITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVLI 143
Cdd:COG2226   71 VEFVVGDAEDLPFPDGSFDLVISSFVLHHLpDPERALAEIARVLKPGGRLVVV 123
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-145 1.51e-19

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: 81.99  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  39 HFNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVganNITWLEQGAELINSSLGVFQLVTIGRAF 118
Cdd:COG2227   21 LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLPLEDGSFDLVICSEVL 97

                         90       100
                 ....*....|....*....|....*...
gi 428257455 119 HWM-DRELVLERIYQLLSeDGGLVLIGT 145
Cdd:COG2227   98 EHLpDPAALLRELARLLK-PGGLLLLST 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 20-145 1.94e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.12  E-value: 1.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  20 ARYRAKYPPALFAKLAEIFHFNNQGRLLDLGCGPGLMTIPL-QSQFQEVVAVDPDPEMLKIAKQQASSVGANNITWLEQG 98
Cdd:COG0500    4 SYYSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVAD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 428257455  99 -AELINSSLGVFQLVTIGRAFHWMDREL---VLERIYQLLSEDGGLVLIGT 145
Cdd:COG0500   84 lAELDPLPAESFDLVVAFGVLHHLPPEEreaLLRELARALKPGGVLLLSAS 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-138 3.59e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.22  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   47 LDLGCGPGLMTIPLQSQFQ-EVVAVDPDPEMLKIAKQQASSVGAnNITWLEQGAELINSSLGVFQLVTIGRAFHWM---D 122
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdpD 80

                          90
                  ....*....|....*.
gi 428257455  123 RELVLERIYQLLSEDG 138
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-142 1.38e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  44 GRLLDLGCGPGLMTIPLQSQFQ--EVVAVDPDPEMLKIAKQQASsvganNITWLEQGAELINSSlGVFQLVTIGRAFHWM 121
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARARARLP-----NVRFVVADLRDLDPP-EPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|..
gi 428257455 122 -DRELVLERIYQLLSEDGGLVL 142
Cdd:COG4106   77 pDHAALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-140 3.31e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 69.32  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   47 LDLGCGPGLMTIPLQSQFQ--EVVAVDPDPEMLKIAKQQASSVGANNITWLEQGA-ELINSSLGVFQLVTIGRAFHWM-D 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALEAARERLAALGLLNAVRVELFQlDLGELDPGSFDVVVASNVLHHLaD 80

                          90
                  ....*....|....*...
gi 428257455  123 RELVLERIYQLLSEDGGL 140
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-142 6.16e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.80  E-value: 6.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   3 TLPTYDPTLFEGAAEDY-------ARYRAkyPPALFAKLAEIFHFNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPE 75
Cdd:COG4976    2 ALDAYVEALFDQYADSYdaalvedLGYEA--PALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 428257455  76 MLKIAKQQASSvgannITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVL 142
Cdd:COG4976   80 MLAKAREKGVY-----DRLLVADLADLAEPDGRFDLIVAADVLTYLgDLAAVFAGVARALKPGGLFIF 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-142 1.54e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.61  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   47 LDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGannITWLEQGAELI----NSslgvFQLVTIGRAFHWM- 121
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG---LTFVVGDAEDLpfpdNS----FDLVLSSEVLHHVe 73

                          90       100
                  ....*....|....*....|.
gi 428257455  122 DRELVLERIYQLLSEDGGLVL 142
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-143 2.57e-12

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: 62.06  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  45 RLLDLGCGPGLMTIPLQSQ-FQEVVAVDPDPEMLKIAKQQASSVGANNITWLEQGAELINSSLGV-FQLVTIGRAFHW-- 120
Cdd:cd02440    1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADEsFDVIISDPPLHHlv 80

                         90       100
                 ....*....|....*....|...
gi 428257455 121 MDRELVLERIYQLLSEDGGLVLI 143
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLT 103
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 19-143 5.51e-12

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 64.59  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  19 YARYRAkypPALFAK-------LAEIFHFNNQGRLLDLGCGPGLMTIPLQSQF---QEVVAVDPDPEMLKIAKQQASSVG 88
Cdd:COG5459   53 YAAYRL---PATYAAvraalaeLAEAGPDFAPLTVLDVGAGPGTAAWAAADAWpslLDATLLERSAAALALGRRLARAAA 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  89 ANNITWLEQGAELINSSLGV--FQLVTIGRAFH---WMDRELVLERIyqLLSEDGGLVLI 143
Cdd:COG5459  130 NPALETAEWRLADLAAALPAppADLVVASYVLNelaDAARAALVDRL--WLAPDGALLIV 187
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 27-145 2.81e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 57.63  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  27 PPALFAKLAEIFHFNNQGRLLDLGCGPGLMTIPLQSQFQ-EVVAVDPDPEMLKIAKQQASSVG-ANNITWLEQGAELINS 104
Cdd:COG2230   36 QEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGlADRVEVRLADYRDLPA 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 428257455 105 SlGVFQLVTIGRAFHWMDRE---LVLERIYQLLSeDGGLVLIGT 145
Cdd:COG2230  116 D-GQFDAIVSIGMFEHVGPEnypAYFAKVARLLK-PGGRLLLHT 157
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 12-142 9.90e-10

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: 57.30  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   12 FEGAAEDYARYR------AKYppaLFAKLAEIFHFNNQgRLLDLGCGPGLMTIPLQSQF--QEVVAVDPDPEMLKIAKQQ 83
Cdd:TIGR02072   2 FNKAAKTYDRHAkiqremAKR---LLALLKEKGIFIPA-SVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   84 ASSvganNITWLEQGAELINSSLGVFQLVTIGRAFHWM-DRELVLERIYQLLSEDGGLVL 142
Cdd:TIGR02072  78 LSE----NVQFICGDAEKLPLEDSSFDLIVSNLALQWCdDLSQALSELARVLKPGGLLAF 133
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 19-158 5.49e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 53.97  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   19 YARYRAKYPPALFAKLAEIFhfNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGANNITWLEQG 98
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKL--PSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPA 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 428257455   99 aelinsslGVFQLVTigrAFHWMDR----ELVLERIYQLLsEDGGLVLIGTNENPWGSPLPWKQ 158
Cdd:pfam13489  79 --------GKFDVIV---AREVLEHvpdpPALLRQIAALL-KPGGLLLLSTPLASDEADRLLLE 130
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 45-112 7.51e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 7.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 428257455  45 RLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVG-ANNITWLEQGAElinSSLGVFQLV 112
Cdd:PRK07580  66 RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGlAGNITFEVGDLE---SLLGRFDTV 131
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 45-150 7.94e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 54.77  E-value: 7.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  45 RLLDLGCGPGLMTIPLQSQ---FQEVVAVDPDPEMLKIAKQQASSVG-ANNITWLEQGAELI----NSslgvFQLVTIG- 115
Cdd:PRK00216  54 KVLDLACGTGDLAIALAKAvgkTGEVVGLDFSEGMLAVGREKLRDLGlSGNVEFVQGDAEALpfpdNS----FDAVTIAf 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 428257455 116 --RAFHwmDRELVLERIYQLLsEDGGLVLI---GTNENPW 150
Cdd:PRK00216 130 glRNVP--DIDKALREMYRVL-KPGGRLVIlefSKPTNPP 166
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 45-142 4.00e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.26  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   45 RLLDLGCGPGLMTIPLQSQFQ---EVVAVDPDPEMLKIAKQQASSVGANNITWLEQGAELINSSL--GVFQLVTIGRAFH 119
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPELLedDKFDVVISNCVLN 85

                          90       100
                  ....*....|....*....|....
gi 428257455  120 WM-DRELVLERIYQLLSEDGGLVL 142
Cdd:pfam13847  86 HIpDPDKVLQEILRVLKPGGRLII 109
PRK08317 PRK08317
hypothetical protein; Provisional
 18-152 3.67e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  18 DYARYRAKyppaLFAKLaeifHFNNQGRLLDLGCGPGLMTIPLQSQFQ---EVVAVDPDPEMLKIAKQQAssvgANNITW 94
Cdd:PRK08317   3 DFRRYRAR----TFELL----AVQPGDRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAKERA----AGLGPN 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428257455  95 LE--QG-AELINSSLGVFQLVTIGRAF-HWMDRELVLERIYQLLSEDGGLVLIgtnENPWGS 152
Cdd:PRK08317  71 VEfvRGdADGLPFPDGSFDAVRSDRVLqHLEDPARALAEIARVLRPGGRVVVL---DTDWDT 129
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
47-149 7.49e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.97  E-value: 7.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   47 LDLGCGPGLMTIPLQSQFQ---EVVAVDPDPEMLKIAKQQASSVGANNITWLEQGAELINSSLGVFQLVTIG---RAFhw 120
Cdd:pfam01209  47 LDVAGGTGDWTFGLSDSAGssgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISfglRNF-- 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 428257455  121 MDRELVLERIYQLLSEDGGLVLIGTN--ENP 149
Cdd:pfam01209 125 PDYLKVLKEAFRVLKPGGRVVCLEFSkpENP 155
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 34-140 2.89e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 41.47  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  34 LAEIFHfNNQGRLLDLGCGPGLMTIPLQSQF--QEVVAVDPDPEMLKIAKQ---QASSVGANNITWL-EQGAELINSSlG 107
Cdd:PRK01683  24 LARVPL-ENPRYVVDLGCGPGNSTELLVERWpaARITGIDSSPAMLAEARSrlpDCQFVEADIASWQpPQALDLIFAN-A 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 428257455 108 VFQLVTigrafhwmDRELVLERIYQLLSEDGGL 140
Cdd:PRK01683 102 SLQWLP--------DHLELFPRLVSLLAPGGVL 126
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
27-103 3.41e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 40.66  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  27 PPALfAklAEIFHF-----NNQGRL-LDLGCGPGLMTIPLQS-QFQEVVAVDPDPEMLKIAKQQASSVGAnNITWLEQGA 99
Cdd:COG2263   27 PAEL-A--AELLHLaylrgDIEGKTvLDLGCGTGMLAIGAALlGAKKVVGVDIDPEALEIARENAERLGV-RVDFIRADV 102


                 ....
gi 428257455 100 ELIN 103
Cdd:COG2263  103 TRIP 106
PRK14968 PRK14968
putative methyltransferase; Provisional
 26-106 9.41e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  26 YPPA----LfakLAEIFHFNNQGRLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSvgaNNITwlEQGAEL 101
Cdd:PRK14968   6 YEPAedsfL---LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKL---NNIR--NNGVEV 77


                 ....*
gi 428257455 102 INSSL 106
Cdd:PRK14968  78 IRSDL 82
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 31-98 1.43e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 39.26  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455   31 FAKLAEIFHFNNQGRLLDLGCGPGLMTIPLQSQFQ--EVVAVDPDPEMLKIAKQQASSVGANNITWLEQG 98
Cdd:TIGR00536 103 EKALASLISQPPILHILDLGTGSGCIALALAYEFPnaEVIAVDISPDALAVAEENAEKNQLEHRVEFIQS 172
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
45-93 1.43e-03

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 39.75  E-value: 1.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 428257455  45 RLLDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQASSVGANNIT 93
Cdd:PRK13168 300 RVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARRNGLDNVT 348
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
30-102 2.64e-03

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.78  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428257455  30 LFAKLAEIFHFNNQGRLLDLGCGPG--LMTIPLQSQFQ-EVVAVDPDPEMLKIAKQQASsvgannitWLEQGAELI 102
Cdd:COG0827  103 LIGYLVEKFTKKEGLRILDPAVGTGnlLTTVLNQLKKKvNAYGVEVDDLLIRLAAVLAN--------LQGHPVELF 170
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
47-93 2.87e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.09  E-value: 2.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 428257455  47 LDLGCGPGLMT-IPLQSQFQEVVAVDPDPEMLKIAKQQASSVG-ANNIT 93
Cdd:COG4076   40 LDIGTGSGLLSmLAARAGAKKVYAVEVNPDIAAVARRIIAANGlSDRIT 88
PRK05785 PRK05785
hypothetical protein; Provisional
 44-80 2.95e-03

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 38.13  E-value: 2.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 428257455  44 GRLLDLGCGPGLMTIPLQSQFQ-EVVAVDPDPEMLKIA 80
Cdd:PRK05785  53 KKVLDVAAGKGELSYHFKKVFKyYVVALDYAENMLKMN 90
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 34-93 5.30e-03

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: 37.09  E-value: 5.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 428257455  34 LAEIFHFNNQGRLLDLGCGPGLMTIPLQSQFQE--VVAVDPDPEMLKIAKQQASSVGANNIT 93
Cdd:COG2813   41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEarVTLVDVNARAVELARANAAANGLENVE 102
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 30-106 5.38e-03

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: 37.43  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257455  30 LFAKLAEIfhfNNQGRLLDLGCGPGLmtIPL----QSQFQEVVAVDPDPEMLKIAKQqasSVGANNitwLEQGAELINSS 105
Cdd:COG4123   28 LLAAFAPV---KKGGRVLDLGTGTGV--IALmlaqRSPGARITGVEIQPEAAELARR---NVALNG---LEDRITVIHGD 96


                 .
gi 428257455 106 L 106
Cdd:COG4123   97 L 97
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 47-83 6.12e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 37.43  E-value: 6.12e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 428257455  47 LDLGCGPGLMTIPLQSQFQEVVAVDPDPEMLKIAKQQ 83
Cdd:PRK10258  47 LDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQK 83
 
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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