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Conserved domains on  [gi|398173973|gb|EJM61785|]
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hypothetical protein PMI30_05084 [Pseudomonas sp. GM50]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-198 4.23e-18

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  40 IGNEFW---------YQYGVFDEKMDPcslpLDASGRRHMEyqfELAEQAGAdvssQSIRRAIDIGCGWGPVLSFLANRY 110
Cdd:COG2230    5 LGNDFYrlfldptmtYSCAYFEDPDDT----LEEAQEAKLD---LILRKLGL----KPGMRVLDIGCGWGGLALYLARRY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973 111 pDCeRIDGVNVSRPQLEYASQVITRKSLADRIRLYLCNAKDIgalpDPKLPYDLAIFRGSLFHFTPQVLQKTMQSLAQRM 190
Cdd:COG2230   74 -GV-RVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDL----PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLL 147


                 ....*...
gi 398173973 191 RTNGTVII 198
Cdd:COG2230  148 KPGGRLLL 155
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-198 4.23e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  40 IGNEFW---------YQYGVFDEKMDPcslpLDASGRRHMEyqfELAEQAGAdvssQSIRRAIDIGCGWGPVLSFLANRY 110
Cdd:COG2230    5 LGNDFYrlfldptmtYSCAYFEDPDDT----LEEAQEAKLD---LILRKLGL----KPGMRVLDIGCGWGGLALYLARRY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973 111 pDCeRIDGVNVSRPQLEYASQVITRKSLADRIRLYLCNAKDIgalpDPKLPYDLAIFRGSLFHFTPQVLQKTMQSLAQRM 190
Cdd:COG2230   74 -GV-RVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDL----PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLL 147


                 ....*...
gi 398173973 191 RTNGTVII 198
Cdd:COG2230  148 KPGGRLLL 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-194 6.84e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.74  E-value: 6.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   94 DIGCGWGPVLSFLANRYPdcERIDGVNVSRPQLEYASQVITRKSLadRIRLYLCnakDIGALPDPKLPYDLAIFRGSLFH 173
Cdd:pfam13649   3 DLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQG---DAEDLPFPDGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 398173973  174 FTPQVLQKTMQSLAQRMRTNG 194
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 91-199 8.74e-11

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: 58.21  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  91 RAIDIGCGWGPVLSFLANRYpdCERIDGVNVSRPQLEYASQVITRKsLADRIRLYLCNAKDIgaLPDPKLPYDLAIFRGS 170
Cdd:cd02440    1 RVLDLGCGTGALALALASGP--GARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL--PPEADESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*....
gi 398173973 171 LFHFtPQVLQKTMQSLAQRMRTNGTVIIS 199
Cdd:cd02440   76 LHHL-VEDLARFLEEARRLLKPGGVLVLT 103
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
90-304 5.85e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 55.50  E-value: 5.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973    90 RRAIDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYASQVITRKSLADRIRLYlcnAKDIGALPDPKLpYDLAIFRG 169
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQ-LHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFPDT-YDLVFGFE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   170 SLFHFTPQVLqkTMQSLAQRMRTNGTVIISESLYN----VDLATYQSFIPdkvdraasghrkTPDSLHKALEDNGFEVID 245
Cdd:smart00828  76 VIHHIKDKMD--LFSNISRHLKDGGHLVLADFIANllsaIEHEETTSYLV------------TREEWAELLARNNLRVVE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398173973   246 SrVTPSNEDVLRWY-ALVKGNLDAHYPDSSNPNFSE-LRDIAiNFSDALRKNKASSYSFIA 304
Cdd:smart00828 142 G-VDASLEIANFLYdPGFEDNLERLYQDDLDEVTKRhFRGIA-NLGKLLEKGLASYALLIV 200
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
91-131 2.20e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 42.53  E-value: 2.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 398173973  91 RAIDIGCGWGPVLSFLANRYpDCErIDGVNVSRPQLEYASQ 131
Cdd:PRK11705 170 RVLDIGCGWGGLARYAAEHY-GVS-VVGVTISAEQQKLAQE 208
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 75-145 1.00e-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: 40.03  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398173973   75 ELAEQAGADVSSQ-SIRRAIDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYASQVITRKSLADRIRLY 145
Cdd:TIGR00536 100 ELVEKALASLISQpPILHILDLGTGSGCIALALAYEFPNAE-VIAVDISPDALAVAEENAEKNQLEHRVEFI 170
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-198 4.23e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  40 IGNEFW---------YQYGVFDEKMDPcslpLDASGRRHMEyqfELAEQAGAdvssQSIRRAIDIGCGWGPVLSFLANRY 110
Cdd:COG2230    5 LGNDFYrlfldptmtYSCAYFEDPDDT----LEEAQEAKLD---LILRKLGL----KPGMRVLDIGCGWGGLALYLARRY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973 111 pDCeRIDGVNVSRPQLEYASQVITRKSLADRIRLYLCNAKDIgalpDPKLPYDLAIFRGSLFHFTPQVLQKTMQSLAQRM 190
Cdd:COG2230   74 -GV-RVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDL----PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLL 147


                 ....*...
gi 398173973 191 RTNGTVII 198
Cdd:COG2230  148 KPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 90-245 1.56e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 68.02  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  90 RRAIDIGCGWGPVLSFLANRYpdCERIDGVNVSRPQLEYASQVITRKSLaDRIRLYLCNAKDIGALPDPKlpYDLAIFRG 169
Cdd:COG0500   28 GRVLDLGCGTGRNLLALAARF--GGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELDPLPAES--FDLVVAFG 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398173973 170 SLFHFTPQVLQKTMQSLAQRMRTNGTVIISESLYNVDLATYQSFIPDKVDRAASGHRKTPDSLHKALEDNGFEVID 245
Cdd:COG0500  103 VLHHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLAAAAT 178
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-194 6.84e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.74  E-value: 6.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   94 DIGCGWGPVLSFLANRYPdcERIDGVNVSRPQLEYASQVITRKSLadRIRLYLCnakDIGALPDPKLPYDLAIFRGSLFH 173
Cdd:pfam13649   3 DLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQG---DAEDLPFPDGSFDLVVSSGVLHH 75

                          90       100
                  ....*....|....*....|.
gi 398173973  174 FTPQVLQKTMQSLAQRMRTNG 194
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 90-199 1.67e-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: 60.42  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  90 RRAIDIGCGWGPVLSFLANRypdCERIDGVNVSRPQLEYAsqvitrKSLADRIRLYLCNAkDIGALPDPKLPYDLAIFRG 169
Cdd:COG2227   26 GRVLDVGCGTGRLALALARR---GADVTGVDISPEALEIA------RERAAELNVDFVQG-DLEDLPLEDGSFDLVICSE 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 398173973 170 SLFHFTPqvLQKTMQSLAQRMRTNGTVIIS 199
Cdd:COG2227   96 VLEHLPD--PAALLRELARLLKPGGLLLLS 123
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
63-243 2.54e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 61.55  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  63 DASGRRHMEYQ--FELAEQAGADVSSQSIRRAIDIGCGWGPVLSFLANRypdCERIDGVNVSRPQLEYAsqvitrKSLAD 140
Cdd:COG4976   19 DAALVEDLGYEapALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR---GYRLTGVDLSEEMLAKA------REKGV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973 141 RIRLYLCnakDIGALPDPKLPYDLAIFRGSLFHFtpQVLQKTMQSLAQRMRTNGTVIISeslynvdlatyqsfIPDKVDR 220
Cdd:COG4976   90 YDRLLVA---DLADLAEPDGRFDLIVAADVLTYL--GDLAAVFAGVARALKPGGLFIFS--------------VEDADGS 150

                        170       180
                 ....*....|....*....|...
gi 398173973 221 AASGHrkTPDSLHKALEDNGFEV 243
Cdd:COG4976  151 GRYAH--SLDYVRDLLAAAGFEV 171
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 91-199 8.74e-11

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: 58.21  E-value: 8.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  91 RAIDIGCGWGPVLSFLANRYpdCERIDGVNVSRPQLEYASQVITRKsLADRIRLYLCNAKDIgaLPDPKLPYDLAIFRGS 170
Cdd:cd02440    1 RVLDLGCGTGALALALASGP--GARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEEL--PPEADESFDVIISDPP 75

                         90       100
                 ....*....|....*....|....*....
gi 398173973 171 LFHFtPQVLQKTMQSLAQRMRTNGTVIIS 199
Cdd:cd02440   76 LHHL-VEDLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
90-200 1.57e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 57.14  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  90 RRAIDIGCGWGPVLSFLANRYPDCeRIDGVNVSRPQLEYAsqvitrKSLADRIRLYLCNAKDIgalpDPKLPYDLAIFRG 169
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPGA-RVTGVDLSPEMLARA------RARLPNVRFVVADLRDL----DPPEPFDLVVSNA 71

                         90       100       110
                 ....*....|....*....|....*....|.
gi 398173973 170 SLFHFTPQvlQKTMQSLAQRMRTNGTVIISE 200
Cdd:COG4106   72 ALHWLPDH--AALLARLAAALAPGGVLAVQV 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 67-244 1.05e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 56.28  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   67 RRHMEYQF--ELAEQAGADVSSQSIrraIDIGCGWGPVLSFLANRYPDCERIDgvnvSRPQLEYASQVITRKSLADRIrl 144
Cdd:pfam13489   2 AHQRERLLadLLLRLLPKLPSPGRV---LDFGCGTGIFLRLLRAQGFSVTGVD----PSPIAIERALLNVRFDQFDEQ-- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  145 ylcnakdigALPDPKLPYDLAIFRGSLFHFtpQVLQKTMQSLAQRMRTNGTVIISESLYNVDLATYQSFIPDKVDRAASG 224
Cdd:pfam13489  73 ---------EAAVPAGKFDVIVAREVLEHV--PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHI 141

                         170       180
                  ....*....|....*....|
gi 398173973  225 HRKTPDSLHKALEDNGFEVI 244
Cdd:pfam13489 142 SLFSARSLKRLLEEAGFEVV 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 90-200 1.76e-09

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: 55.39  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  90 RRAIDIGCGWGPVLSFLANRypdCERIDGVNVSRPQLEYASQVITRKSLadRIRLYLCnakDIGALPDPKLPYDLAIFRG 169
Cdd:COG2226   24 ARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGL--NVEFVVG---DAEDLPFPDGSFDLVISSF 95

                         90       100       110
                 ....*....|....*....|....*....|.
gi 398173973 170 SLFHFTPqvLQKTMQSLAQRMRTNGTVIISE 200
Cdd:COG2226   96 VLHHLPD--PERALAEIARVLKPGGRLVVVD 124
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
90-304 5.85e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 55.50  E-value: 5.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973    90 RRAIDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYASQVITRKSLADRIRLYlcnAKDIGALPDPKLpYDLAIFRG 169
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPHLQ-LHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAKDPFPDT-YDLVFGFE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   170 SLFHFTPQVLqkTMQSLAQRMRTNGTVIISESLYN----VDLATYQSFIPdkvdraasghrkTPDSLHKALEDNGFEVID 245
Cdd:smart00828  76 VIHHIKDKMD--LFSNISRHLKDGGHLVLADFIANllsaIEHEETTSYLV------------TREEWAELLARNNLRVVE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398173973   246 SrVTPSNEDVLRWY-ALVKGNLDAHYPDSSNPNFSE-LRDIAiNFSDALRKNKASSYSFIA 304
Cdd:smart00828 142 G-VDASLEIANFLYdPGFEDNLERLYQDDLDEVTKRhFRGIA-NLGKLLEKGLASYALLIV 200
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-196 6.11e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 46.98  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   93 IDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYASQVITRKSLADRIRLYLcNAKDIGALPDPKlpYDLAIFRGSLf 172
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLE-YTGLDISPAALEAARERLAALGLLNAVRVEL-FQLDLGELDPGS--FDVVVASNVL- 75

                          90       100
                  ....*....|....*....|....
gi 398173973  173 HFTPQvLQKTMQSLAQRMRTNGTV 196
Cdd:pfam08242  76 HHLAD-PRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 91-240 7.34e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 7.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   91 RAIDIGCGWGpVLSFLANRY--PDCERIdGVNVSRPQLEYASQvITRKSLADRIRLYLCnakDIGALPD--PKLPYDLAI 166
Cdd:pfam13847   6 RVLDLGCGTG-HLSFELAEElgPNAEVV-GIDISEEAIEKARE-NAQKLGFDNVEFEQG---DIEELPEllEDDKFDVVI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398173973  167 FRGSLFHFTPQvlQKTMQSLAQRMRTNGTVIISE--SLYNVDLATYQSFipdKVDRAASGHRKTPDSLHKALEDNG 240
Cdd:pfam13847  80 SNCVLNHIPDP--DKVLQEILRVLKPGGRLIISDpdSLAELPAHVKEDS---TYYAGCVGGAILKKKLYELLEEAG 150
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 91-152 4.31e-06

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 47.32  E-value: 4.31e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398173973   91 RAIDIGCGWGPVLSFLANRYpDCERIdGVNVSRPQLEYASQVITRKSLADRIRLYLCNAKDI 152
Cdd:pfam02353  64 TLLDIGCGWGGLMRRAAERY-DVNVV-GLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDF 123
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-198 6.27e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.81  E-value: 6.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973   93 IDIGCGWGPVLSFLANRYPdceRIDGVNVSRPQLEYASQVITRkslaDRIRLYLCNAKDIGaLPDPKlpYDLAIFRGSLF 172
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPR----EGLTFVVGDAEDLP-FPDNS--FDLVLSSEVLH 70

                          90       100
                  ....*....|....*....|....*.
gi 398173973  173 HFtpQVLQKTMQSLAQRMRTNGTVII 198
Cdd:pfam08241  71 HV--EDPERALREIARVLKPGGILII 94
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 90-129 1.51e-04

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: 41.71  E-value: 1.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 398173973  90 RRAIDIGCGWGPVLSFLANRYPDCeRIDGVNVSRPQLEYA 129
Cdd:COG2813   51 GRVLDLGCGYGVIGLALAKRNPEA-RVTLVDVNARAVELA 89
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
91-131 2.20e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 42.53  E-value: 2.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 398173973  91 RAIDIGCGWGPVLSFLANRYpDCErIDGVNVSRPQLEYASQ 131
Cdd:PRK11705 170 RVLDIGCGWGGLARYAAEHY-GVS-VVGVTISAEQQKLAQE 208
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 81-166 5.59e-04

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: 40.51  E-value: 5.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  81 GADVSSQSIRRAIDIGCGWGPVLSFLANRYPDCeRIDGVNVsrpQLEYASQviTRKS-----LADRIRLYLCNAKDIGAL 155
Cdd:COG4123   30 AAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGA-RITGVEI---QPEAAEL--ARRNvalngLEDRITVIHGDLKEFAAE 103

                         90
                 ....*....|.
gi 398173973 156 PDPKlPYDLAI 166
Cdd:COG4123  104 LPPG-SFDLVV 113
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
87-204 8.00e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.02  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398173973  87 QSIRRAI-------DIGCGWGPvLSFLANRYpDCERIDGVNVSRPQLEYASQVITRKSLADRIRLYLCNAKDIgalpDPK 159
Cdd:COG4076   27 AAIERVVkpgdvvlDIGTGSGL-LSMLAARA-GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDL----DLP 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 398173973 160 LPYDLAIfrGSLFH---FTPQVLQkTMQSLAQRMRTNGTVIISESLYN 204
Cdd:COG4076  101 EKADVII--SEMLDtalLDEGQVP-ILNHARKRLLKPGGRIIPERITN 145
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 75-145 1.00e-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: 40.03  E-value: 1.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398173973   75 ELAEQAGADVSSQ-SIRRAIDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYASQVITRKSLADRIRLY 145
Cdd:TIGR00536 100 ELVEKALASLISQpPILHILDLGTGSGCIALALAYEFPNAE-VIAVDISPDALAVAEENAEKNQLEHRVEFI 170
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 82-131 2.71e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 38.77  E-value: 2.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 398173973  82 ADVSSQSIRRAIDIGCGWGPVLSFLANRYPDcERIDGVNVSRPQLEYASQ 131
Cdd:PRK01683  25 ARVPLENPRYVVDLGCGPGNSTELLVERWPA-ARITGIDSSPAMLAEARS 73
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 90-129 3.39e-03

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.57  E-value: 3.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 398173973   90 RRAIDIGCGWGPVLSFLANRYPDCErIDGVNVSRPQLEYA 129
Cdd:pfam05175  33 GKVLDLGCGAGVLGAALAKESPDAE-LTMVDINARALESA 71
 
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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