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Conserved domains on  [gi|568938322|ref|XP_006504590|]
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methyltransferase-like protein 27 isoform X1 [Mus musculus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11471966)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-184 9.34e-29

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 107.78  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976   11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938322 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPG-----SCPHqTTVTVGYSHDREAFASAL 184
Cdd:COG4976   89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGglfifSVED-ADGSGRYAHSLDYVRDLL 164
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-184 9.34e-29

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 107.78  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976   11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938322 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPG-----SCPHqTTVTVGYSHDREAFASAL 184
Cdd:COG4976   89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGglfifSVED-ADGSGRYAHSLDYVRDLL 164
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-161 1.38e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 81.07  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSlCTLGQ---EPLPDPEGTFDAVIIVGALS--EGQ 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQgdaEDLPFPDGSFDLVVSSGVLHhlPDP 79

                          90
                  ....*....|....*.
gi 568938322  146 VPCSAIPELLRVTKPG 161
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 33-161 5.14e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 64.02  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  33 DDWAPEYDQ--DVAAL----KYRapRLAVDCLsrafrGSPHDALILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLK 104
Cdd:PRK00216  18 DSIAPKYDLmnDLLSFglhrVWR--RKTIKWL-----GVRPGDKVLDLACGTGDLAIALakAVGKTGEVVGLDFSEGMLA 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938322 105 QARAR----GLYHHLSLCTLGQEPLPDPEGTFDAVII----------VGALSegqvpcsaipELLRVTKPG 161
Cdd:PRK00216  91 VGREKlrdlGLSGNVEFVQGDAEALPFPDNSFDAVTIafglrnvpdiDKALR----------EMYRVLKPG 151
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-163 5.79e-12

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 63.44  E-value: 5.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938322  104 KQARARGLYH-HLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGSC 163
Cdd:TIGR01934  78 EVAKKKSELPlNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGR 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 3.02e-10

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: 56.28  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS-EGQ 145
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKgdaeELPPEADESFDVIISDPPLHhLVE 81

                         90
                 ....*....|....*.
gi 568938322 146 VPCSAIPELLRVTKPG 161
Cdd:cd02440   82 DLARFLEEARRLLKPG 97
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-184 9.34e-29

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 107.78  E-value: 9.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  32 YDDWAPEYDQD-VAALKYRAPRLAVDCLSRAFrGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG 110
Cdd:COG4976   11 FDQYADSYDAAlVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKG 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938322 111 LYHHLSLCTLGQepLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPG-----SCPHqTTVTVGYSHDREAFASAL 184
Cdd:COG4976   89 VYDRLLVADLAD--LAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGglfifSVED-ADGSGRYAHSLDYVRDLL 164
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 32-161 4.11e-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: 4.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  32 YDDWAPEYDQDVAALKYRAPRlavdclsrafrgspHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGL 111
Cdd:COG2226    1 FDRVAARYDGREALLAALGLR--------------PGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAA 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568938322 112 YHHLSLCTLGQ--EPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPG 161
Cdd:COG2226   66 EAGLNVEFVVGdaEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPG 117
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-161 1.38e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 81.07  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSlCTLGQ---EPLPDPEGTFDAVIIVGALS--EGQ 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN-VEFVQgdaEDLPFPDGSFDLVVSSGVLHhlPDP 79

                          90
                  ....*....|....*.
gi 568938322  146 VPCSAIPELLRVTKPG 161
Cdd:pfam13649  80 DLEAALREIARVLKPG 95
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 66-161 2.81e-16

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: 73.13  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  66 PHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGLYHHLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQ 145
Cdd:COG2227   23 PAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLP 101

                         90
                 ....*....|....*.
gi 568938322 146 VPCSAIPELLRVTKPG 161
Cdd:COG2227  102 DPAALLRELARLLKPG 117
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-161 1.11e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.99  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   72 LDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARG-----LYHHLSLCTLgqePLPDpeGTFDAVIIVGALSEGQV 146
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKApreglTFVVGDAEDL---PFPD--NSFDLVLSSEVLHHVED 74

                          90
                  ....*....|....*
gi 568938322  147 PCSAIPELLRVTKPG 161
Cdd:pfam08241  75 PERALREIARVLKPG 89
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 30-161 1.28e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 67.63  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  30 RFYDDWAPEYDQDVAALkyraPRLavdclsrafrgsPHDALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR 109
Cdd:COG0500    5 YYSDELLPGLAALLALL----ERL------------PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARAR 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568938322 110 GLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS--EGQVPCSAIPELLRVTKPG 161
Cdd:COG0500   69 AAKAGLGNVEFLVadlaELDPLPAESFDLVVAFGVLHhlPPEEREALLRELARALKPG 126
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 33-161 5.14e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 64.02  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  33 DDWAPEYDQ--DVAAL----KYRapRLAVDCLsrafrGSPHDALILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLK 104
Cdd:PRK00216  18 DSIAPKYDLmnDLLSFglhrVWR--RKTIKWL-----GVRPGDKVLDLACGTGDLAIALakAVGKTGEVVGLDFSEGMLA 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938322 105 QARAR----GLYHHLSLCTLGQEPLPDPEGTFDAVII----------VGALSegqvpcsaipELLRVTKPG 161
Cdd:PRK00216  91 VGREKlrdlGLSGNVEFVQGDAEALPFPDNSFDAVTIafglrnvpdiDKALR----------EMYRVLKPG 151
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 30-163 5.79e-12

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 63.44  E-value: 5.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   30 RFYDDWAPEYDQDVAALKYRAPRL----AVDCLsRAFRGSPhdalILDVACGTGLVAVELQARG--FLQVQGVDGSPEML 103
Cdd:TIGR01934   3 EMFDRIAPKYDLLNDLLSFGLHRLwrrrAVKLI-GVFKGQK----VLDVACGTGDLAIELAKSApdRGKVTGVDFSSEML 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938322  104 KQARARGLYH-HLSLCTLGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGSC 163
Cdd:TIGR01934  78 EVAKKKSELPlNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGR 138
PRK08317 PRK08317
hypothetical protein; Provisional
 71-161 6.34e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGLVAVELQAR----GflQVQGVDGSPEMLKQARARGLYHHLSLCTL--GQEPLPDPEGTFDAVIIVGALSEG 144
Cdd:PRK08317  23 VLDVGCGPGNDARELARRvgpeG--RVVGIDRSEAMLALAKERAAGLGPNVEFVrgDADGLPFPDGSFDAVRSDRVLQHL 100

                         90
                 ....*....|....*..
gi 568938322 145 QVPCSAIPELLRVTKPG 161
Cdd:PRK08317 101 EDPARALAEIARVLRPG 117
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 36-161 1.00e-10

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 60.54  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  36 APEYDQDVAALKYRAPRLAVDCLSRAFrgsphdALILDVACGTGLVAVELQARGfLQVQGVDGSPEMLKQARARGLYHHL 115
Cdd:PRK10258  17 AAHYEQHAELQRQSADALLAMLPQRKF------THVLDAGCGPGWMSRYWRERG-SQVTALDLSPPMLAQARQKDAADHY 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568938322 116 SLCTLgqEPLPDPEGTFD------AVIIVGALSEgqvpcsAIPELLRVTKPG 161
Cdd:PRK10258  90 LAGDI--ESLPLATATFDlawsnlAVQWCGNLST------ALRELYRVVRPG 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-161 3.02e-10

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: 56.28  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARARGLYHHLSLCTLGQ----EPLPDPEGTFDAVIIVGALS-EGQ 145
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKgdaeELPPEADESFDVIISDPPLHhLVE 81

                         90
                 ....*....|....*.
gi 568938322 146 VPCSAIPELLRVTKPG 161
Cdd:cd02440   82 DLARFLEEARRLLKPG 97
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
71-161 3.12e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.99  E-value: 3.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGLVAVELQARG-FLQVQGVDGSPEMLKQARAR--GL-YHHLSLCTLgqeplpDPEGTFDAVIIVGALS--EG 144
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARlpNVrFVVADLRDL------DPPEPFDLVVSNAALHwlPD 78

                         90
                 ....*....|....*..
gi 568938322 145 QVpcSAIPELLRVTKPG 161
Cdd:COG4106   79 HA--ALLARLAAALAPG 93
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 64-136 2.78e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 56.00  E-value: 2.78e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938322  64 GSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEPLpdpEGTFDAVI 136
Cdd:PRK07580  60 GDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISPQMVEEARERapeaGLAGNITFEVGDLESL---LGRFDTVV 132
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-161 1.37e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   72 LDVACGTGLVAVEL-QARGFLQVQGVDGSPEMLKQARARGL---YHHLSLCTLGQEPLPDPEG-TFDAVIIVGALSEGQV 146
Cdd:pfam08242   1 LEIGCGTGTLLRALlEALPGLEYTGLDISPAALEAARERLAalgLLNAVRVELFQLDLGELDPgSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*
gi 568938322  147 PCSAIPELLRVTKPG 161
Cdd:pfam08242  81 PRAVLRNIRRLLKPG 95
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-161 2.30e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEPLPdPEGTFDAVIIVGALSegQV 146
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERaaeaGLADRVEVRLADYRDLP-ADGQFDAIVSIGMFE--HV 131

                         90
                 ....*....|....*....
gi 568938322 147 PCSAIPELL----RVTKPG 161
Cdd:COG2230  132 GPENYPAYFakvaRLLKPG 150
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
71-161 1.21e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 51.29  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   71 ILDVACGTGLVAVEL--QARGFLQVQGVDGSPEMLKQARAR----GLYHHLSLCTLGQEpLPDPEGTFDAVIIVGALSEG 144
Cdd:pfam01209  46 FLDVAGGTGDWTFGLsdSAGSSGKVVGLDINENMLKEGEKKakeeGKYNIEFLQGNAEE-LPFEDDSFDIVTISFGLRNF 124

                          90
                  ....*....|....*..
gi 568938322  145 QVPCSAIPELLRVTKPG 161
Cdd:pfam01209 125 PDYLKVLKEAFRVLKPG 141
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 71-175 1.43e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 48.37  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  71 ILDVACGTGL----VAVELQARGFLQVQGVDGSPEMLKQARARglYHHLSLCTLGQEPLPDPEGTFDAVIIVGAlsegqv 146
Cdd:PRK11088  89 LLDIGCGEGYythaLADALPEITTMQLFGLDISKVAIKYAAKR--YPQVTFCVASSHRLPFADQSLDAIIRIYA------ 160

                         90       100
                 ....*....|....*....|....*....
gi 568938322 147 PCSAiPELLRVTKPGScpHQTTVTVGYSH 175
Cdd:PRK11088 161 PCKA-EELARVVKPGG--IVITVTPGPRH 186
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 71-162 7.71e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 7.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   71 ILDVACGTG----LVAVELQARGflQVQGVDGSPEMLKQARARGLYHHLSLCTLGQE-----PLPDPEGTFDAVIIVGAL 141
Cdd:pfam13847   7 VLDLGCGTGhlsfELAEELGPNA--EVVGIDISEEAIEKARENAQKLGFDNVEFEQGdieelPELLEDDKFDVVISNCVL 84

                          90       100
                  ....*....|....*....|.
gi 568938322  142 SEGQVPCSAIPELLRVTKPGS 162
Cdd:pfam13847  85 NHIPDPDKVLQEILRVLKPGG 105
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-161 2.25e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.57  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   46 LKYRAPRLAVDCLSRAFRGSPHDALILDVACGTGLVAVELQARGFlQVQGVDGSPEMlkQARARGLYHHLSLCtlgQEPL 125
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVDPSPIA--IERALLNVRFDQFD---EQEA 74

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568938322  126 PDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPG 161
Cdd:pfam13489  75 AVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPG 110
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 51-161 4.66e-05

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 43.01  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  51 PRLAvDCLSRAFRGSPHDaLILDVACGTGLVAVELQARGFlQVQGVDGSPEMLKQARARGLYHHLSLCTLGQEP---LPD 127
Cdd:COG1041   12 PRLA-RALVNLAGAKEGD-TVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDardLPL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 568938322 128 PEGTFDAVII-----VGALSEGQVPC----SAIPELLRVTKPG 161
Cdd:COG1041   89 ADESVDAIVTdppygRSSKISGEELLelyeKALEEAARVLKPG 131
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 63-161 4.96e-05

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: 43.43  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   63 RGSPHDALILDVACGTGLVAVELQARgFLQVQ--GVDGSPEMLKQARarglyHHLS---LCTLGQ-EPLPDPEGTFDavI 136
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKR-FPQAEfiALDISAGMLAQAK-----TKLSenvQFICGDaEKLPLEDSSFD--L 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 568938322  137 IVGALSegqV-----PCSAIPELLRVTKPG 161
Cdd:TIGR02072 102 IVSNLA---LqwcddLSQALSELARVLKPG 128
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 52-185 7.08e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.49  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  52 RLAV--DCLSRAFRGSPHDAL------ILDVACGTGLVAVELqARGFLQVQGVDGSPEMLKQARARG----LYHHLSLCT 119
Cdd:PLN02396 108 RLAFirSTLCRHFSKDPSSAKpfeglkFIDIGCGGGLLSEPL-ARMGATVTGVDAVDKNVKIARLHAdmdpVTSTIEYLC 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938322 120 LGQEPLPDPEGTFDAVIIVGALSEGQVPCSAIPELLRVTKPGScphqTTVTVGYSHDREAFASALV 185
Cdd:PLN02396 187 TTAEKLADEGRKFDAVLSLEVIEHVANPAEFCKSLSALTIPNG----ATVLSTINRTMRAYASTIV 248
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 35-111 1.41e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 1.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938322  35 WAPeyDQDVAALKYRApRLAVDCLSRAfrGSPHDALILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQARARGL 111
Cdd:PRK14103   2 WDP--DVYLAFADHRG-RPFYDLLARV--GAERARRVVDLGCGPGNLTRYLARRwPGAVIEALDSSPEMVAAARERGV 74
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 34-109 1.47e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 39.16  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322  34 DWAPE-YdqdvaaLKYRAPRL--AVDCLSRAfrgsPHDAL--ILDVACGTGLVAVELQAR-GFLQVQGVDGSPEMLKQAR 107
Cdd:PRK01683   3 DWNPSlY------LKFEDERTrpARDLLARV----PLENPryVVDLGCGPGNSTELLVERwPAARITGIDSSPAMLAEAR 72


                 ..
gi 568938322 108 AR 109
Cdd:PRK01683  73 SR 74
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 71-159 1.97e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 38.21  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   71 ILDVACGTG----LVAVELQARGflqvQGVDGSPEMLKQARARGLYHHLSLCTLGQEPLPDpeGTFDAVIIVGALSEGQV 146
Cdd:pfam07021  17 VLDLGCGDGtllyLLKEEKGVDG----YGIELDAAGVAECVAKGLYVIQGDLDEGLEHFPD--KSFDYVILSQTLQATRN 90

                          90
                  ....*....|...
gi 568938322  147 PCSAIPELLRVTK 159
Cdd:pfam07021  91 PREVLDEMLRIGR 103
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 63-161 9.90e-03

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 36.61  E-value: 9.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938322   63 RGSPH-----DALILDVACGTGLVAVELQARGFLQVQGVDGSPEMLKQARA----RGLYHHLSLCTLGQEPLPDPEGtFD 133
Cdd:pfam08003 106 RVLPHlsplkGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLCQFEAvrklLGNDQRAHLLPLGIEQLPALAA-FD 184

                          90       100
                  ....*....|....*....|....*...
gi 568938322  134 AVIIVGALSEGQVPCSAIPELLRVTKPG 161
Cdd:pfam08003 185 TVFSMGVLYHRRSPLDHLLQLKDQLVKG 212
 
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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