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Conserved domains on  [gi|1964337157|gb|KAG2193473|]
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hypothetical protein INT46_002385 [Mucor plumbeus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

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

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 294-391 3.33e-11

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKLFpNWLVVGIDdksggPSPD-----QRKVPK---NFKYIRCfyDILKTlkDIPADSFDFVYAR 365
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVD-----LSPEmleraRERAAEaglNVEFVQG--DAEDL--PFPDGSFDLVVSS 70

                          90       100
                  ....*....|....*....|....*.
gi 1964337157 366 FLLDAYGDDCYQDLAQECHRICKPKG 391
Cdd:pfam13649  71 GVLHHLPDPDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 294-391 3.33e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKLFpNWLVVGIDdksggPSPD-----QRKVPK---NFKYIRCfyDILKTlkDIPADSFDFVYAR 365
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVD-----LSPEmleraRERAAEaglNVEFVQG--DAEDL--PFPDGSFDLVVSS 70

                          90       100
                  ....*....|....*....|....*.
gi 1964337157 366 FLLDAYGDDCYQDLAQECHRICKPKG 391
Cdd:pfam13649  71 GVLHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 286-393 1.54e-07

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: 50.76  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 286 IHIESKQHILHVGCGDGSWCTDIAKLfpNWLVVGIDdksggPSPD-----QRKVPK---NFKYIRCfyDILKTlkDIPAD 357
Cdd:COG2226    18 LGLRPGARVLDLGCGTGRLALALAER--GARVTGVD-----ISPEmlelaRERAAEaglNVEFVVG--DAEDL--PFPDG 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1964337157 358 SFDFVYARFLLDAYGDDcyQDLAQECHRICKPKGYV 393
Cdd:COG2226    87 SFDLVISSFVLHHLPDP--ERALAEIARVLKPGGRL 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 294-393 8.09e-07

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 47.81  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKlFPNWLVVGIDdksggPSPDQ---------RKVPKNFKYIRCfyDILKtLKDIPADSFDFVYA 364
Cdd:cd02440     2 VLDLGCGTGALALALAS-GPGARVTGVD-----ISPVAlelarkaaaALLADNVEVLKG--DAEE-LPPEADESFDVIIS 72

                          90       100
                  ....*....|....*....|....*....
gi 1964337157 365 RFLLDAYGDDcYQDLAQECHRICKPKGYV 393
Cdd:cd02440    73 DPPLHHLVED-LARFLEEARRLLKPGGVL 100
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 284-391 8.04e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 284 SPIHIESKQHILHVGCGDGSWCTDIAKLFpNWLVVGIDDKSGGPSPDQRKVPKNFKYIRCFYDILKtlKDIPADSFDFVY 363
Cdd:PTZ00098   46 SDIELNENSKVLDIGSGLGGGCKYINEKY-GAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILK--KDFPENTFDMIY 122

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1964337157 364 ARfllDAYGDDCYQD---LAQECHRICKPKG 391
Cdd:PTZ00098  123 SR---DAILHLSYADkkkLFEKCYKWLKPNG 150
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 294-391 3.33e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKLFpNWLVVGIDdksggPSPD-----QRKVPK---NFKYIRCfyDILKTlkDIPADSFDFVYAR 365
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVD-----LSPEmleraRERAAEaglNVEFVQG--DAEDL--PFPDGSFDLVVSS 70

                          90       100
                  ....*....|....*....|....*.
gi 1964337157 366 FLLDAYGDDCYQDLAQECHRICKPKG 391
Cdd:pfam13649  71 GVLHHLPDPDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 295-393 3.82e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.82  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 295 LHVGCGDGSWCTDIAKLFPNwlVVGIDdksggPSPDQRKVPKNFKYIRCFYDILKTLKDIP--ADSFDFVYARFLLDAYG 372
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVD-----ISPEMLELAREKAPREGLTFVVGDAEDLPfpDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 1964337157 373 DDcyQDLAQECHRICKPKGYV 393
Cdd:pfam08241  74 DP--ERALREIARVLKPGGIL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 286-393 1.54e-07

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: 50.76  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 286 IHIESKQHILHVGCGDGSWCTDIAKLfpNWLVVGIDdksggPSPD-----QRKVPK---NFKYIRCfyDILKTlkDIPAD 357
Cdd:COG2226    18 LGLRPGARVLDLGCGTGRLALALAER--GARVTGVD-----ISPEmlelaRERAAEaglNVEFVVG--DAEDL--PFPDG 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1964337157 358 SFDFVYARFLLDAYGDDcyQDLAQECHRICKPKGYV 393
Cdd:COG2226    87 SFDLVISSFVLHHLPDP--ERALAEIARVLKPGGRL 120
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 287-393 7.09e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 287 HIESKQHILHVGCGDGSWCTDIAKLFpNWLVVGIDdksggPSPD-----QRKVPK----NFKYIRCfyDILKtLKDIPAD 357
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGID-----LSPEaialaRARAAKaglgNVEFLVA--DLAE-LDPLPAE 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1964337157 358 SFDFVYARFLLDAYGDDCYQDLAQECHRICKPKGYV 393
Cdd:COG0500    94 SFDLVVAFGVLHHLPPEEREALLRELARALKPGGVL 129
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 294-393 8.09e-07

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 47.81  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKlFPNWLVVGIDdksggPSPDQ---------RKVPKNFKYIRCfyDILKtLKDIPADSFDFVYA 364
Cdd:cd02440     2 VLDLGCGTGALALALAS-GPGARVTGVD-----ISPVAlelarkaaaALLADNVEVLKG--DAEE-LPPEADESFDVIIS 72

                          90       100
                  ....*....|....*....|....*....
gi 1964337157 365 RFLLDAYGDDcYQDLAQECHRICKPKGYV 393
Cdd:cd02440    73 DPPLHHLVED-LARFLEEARRLLKPGGVL 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 287-393 3.10e-06

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: 46.55  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 287 HIESKQHILHVGCGDGSWCTDIAKLfpNWLVVGIDdksggPSPD-----QRKVPK-NFKYIRC-FYDIlktlkDIPADSF 359
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARR--GADVTGVD-----ISPEaleiaRERAAElNVDFVQGdLEDL-----PLEDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1964337157 360 DFVYARFLLDAYGDDcyQDLAQECHRICKPKGYV 393
Cdd:COG2227    89 DLVICSEVLEHLPDP--AALLRELARLLKPGGLL 120
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 295-393 1.03e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.28  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 295 LHVGCGDGSWCTDIAKLFPNWLVVGIDdksggPSPD------QRKVPKNFKYIRCFYDILKTLKDIPADSFDFVYARFLL 368
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLD-----ISPAaleaarERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVL 75

                          90       100
                  ....*....|....*....|....*
gi 1964337157 369 DAYGDDcyQDLAQECHRICKPKGYV 393
Cdd:pfam08242  76 HHLADP--RAVLRNIRRLLKPGGVL 98
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
295-393 1.41e-04

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 42.55  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 295 LHVGCGDgswctdiaKLFPNWLVVgidDKSGGPSPDQrkvpknfkyircfYDILKTLKDIPADSFDFVYARFLLDAYGDD 374
Cdd:COG4627     7 LNIGCGP--------KRLPGWLNV---DIVPAPGVDI-------------VGDLTDPLPFPDNSVDAIYSSHVLEHLDYE 62

                          90
                  ....*....|....*....
gi 1964337157 375 CYQDLAQECHRICKPKGYV 393
Cdd:COG4627    63 EAPLALKECYRVLKPGGIL 81
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
293-368 1.52e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.96  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 293 HILHVGCGDGSWCTDIAKLFPNWLVVGIDdksggPSPD-----QRKVPkNFKYIRCfyDILkTLKdiPADSFDFVYARFL 367
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVTGVD-----LSPEmlaraRARLP-NVRFVVA--DLR-DLD--PPEPFDLVVSNAA 72


                  .
gi 1964337157 368 L 368
Cdd:COG4106    73 L 73
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 294-395 3.00e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 294 ILHVGCGDGSWCTDIAKLFPNwlVVGIDdksggPSPDQRKVPKNFKYIRCFYDIlktLKDIPADSFDFVYARFLLDAYGD 373
Cdd:pfam13489  26 VLDFGCGTGIFLRLLRAQGFS--VTGVD-----PSPIAIERALLNVRFDQFDEQ---EAAVPAGKFDVIVAREVLEHVPD 95

                          90       100
                  ....*....|....*....|..
gi 1964337157 374 dcYQDLAQECHRICKPKGYVEL 395
Cdd:pfam13489  96 --PPALLRQIAALLKPGGLLLL 115
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 288-393 3.86e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 288 IESKQHILHVGCGDGSWCTDIA-KLFPNWLVVGIDDksggpSPD---------QRKVPKNFKYIRCfyDILKTLKDIPAD 357
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDI-----SEEaiekarenaQKLGFDNVEFEQG--DIEELPELLEDD 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1964337157 358 SFDFVYARFLLDAYGD--DCYqdlaQECHRICKPKGYV 393
Cdd:pfam13847  74 KFDVVISNCVLNHIPDpdKVL----QEILRVLKPGGRL 107
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 284-391 8.04e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 284 SPIHIESKQHILHVGCGDGSWCTDIAKLFpNWLVVGIDDKSGGPSPDQRKVPKNFKYIRCFYDILKtlKDIPADSFDFVY 363
Cdd:PTZ00098   46 SDIELNENSKVLDIGSGLGGGCKYINEKY-GAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILK--KDFPENTFDMIY 122

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1964337157 364 ARfllDAYGDDCYQD---LAQECHRICKPKG 391
Cdd:PTZ00098  123 SR---DAILHLSYADkkkLFEKCYKWLKPNG 150
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 283-366 8.77e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 37.27  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 283 QSPIHIEskqhilhVGCGDGSWCTDIAKLFPNWLVVGIDDKSggPSPDQ------RKVPKNFKYIRcfYDILKTL-KDIP 355
Cdd:pfam02390   1 DAPVFLE-------IGCGMGGFLVAMAKANPDKNFIGIEIRV--PGVAKalkkidALGLQNLRILC--GNALDVLpNYFP 69

                          90
                  ....*....|.
gi 1964337157 356 ADSFDFVYARF 366
Cdd:pfam02390  70 PGSLQKIFINF 80
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 285-363 9.79e-03

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 37.42  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1964337157 285 PIHIEskqhilhVGCGDGSWCTDIAKLFPNWLVVGIDdksggPSPD-----QRKV----PKNFKYIRCfyDILKTLKDIP 355
Cdd:COG0220    34 PLVLE-------IGFGKGEFLVELAAANPDINFIGIE-----VHEPgvakaLKKAeeegLTNVRLLRG--DAVELLELFP 99


                  ....*...
gi 1964337157 356 ADSFDFVY 363
Cdd:COG0220   100 DGSLDRIY 107
 
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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