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Conserved domains on  [gi|1801329872|ref|WP_160979747|]
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class I SAM-dependent methyltransferase [Deinococcus xianganensis]

Protein Classification

class I SAM-dependent DNA 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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047
PubMed:  23180741|12504684|12826405
SCOP:  3000118

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];
3-143 4.22e-31

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


:

Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.17  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872   3 RQPFTALAAVYDA-IMADVEYDHWADFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVR 81
Cdd:COG4976     8 EALFDQYADSYDAaLVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801329872  82 LPGVPFVQGDLRTF-ELGERFGLVTCvFDSLNNLltpGDLGAALRRARAHLSPGGLLAFDVNT 143
Cdd:COG4976    88 GVYDRLLVADLADLaEPDGRFDLIVA-ADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-143 4.22e-31

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.17  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872   3 RQPFTALAAVYDA-IMADVEYDHWADFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVR 81
Cdd:COG4976     8 EALFDQYADSYDAaLVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801329872  82 LPGVPFVQGDLRTF-ELGERFGLVTCvFDSLNNLltpGDLGAALRRARAHLSPGGLLAFDVNT 143
Cdd:COG4976    88 GVYDRLLVADLADLaEPDGRFDLIVA-ADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-135 1.12e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.38  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  45 LDLACGTGGFTREL-RAAGWDVTGLDFSEAMLAEARVRL----PGVPFVQGDLRTFEL-GERFGLVTCVFdsLNNLLTPG 118
Cdd:pfam13649   2 LDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFpDGSFDLVVSSG--VLHHLPDP 79

                          90
                  ....*....|....*..
gi 1801329872 119 DLGAALRRARAHLSPGG 135
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 26-139 3.89e-14

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: 69.62  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  26 ADFVLSFARDGGLVGPGRALDLACGTGGFTRELRA--AGWDVTGLDFSEAMLAEARVRLPG-VPFVQGDLRTFELGER-F 101
Cdd:TIGR02072  20 AKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKrfPQAEFIALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSsF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1801329872 102 GLVTC--VFDSLNnlltpgDLGAALRRARAHLSPGGLLAF 139
Cdd:TIGR02072 100 DLIVSnlALQWCD------DLSQALSELARVLKPGGLLAF 133
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 41-192 4.78e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 63.81  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  41 PGRALDLACGTGGFTrELRAAGW---DVTGLDFSEAMLAEARVRLPGVPFVQGDLRTFELGERFGLV--TCVFDSLNNLL 115
Cdd:PRK01683   32 PRYVVDLGCGPGNST-ELLVERWpaaRITGIDSSPAMLAEARSRLPDCQFVEADIASWQPPQALDLIfaNASLQWLPDHL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872 116 TpgdlgaALRRARAHLSPGGLLA------FDVNTRLGVREL-----WE---GDAIEGLAPLPdggevhyHWSHHYDAEAD 181
Cdd:PRK01683  111 E------LFPRLVSLLAPGGVLAvqmpdnLDEPSHVLMREVaengpWEqnlPDRGARRAPLP-------PPHAYYDALAP 177

                         170
                  ....*....|.
gi 1801329872 182 VGvvqafCRVD 192
Cdd:PRK01683  178 AA-----CRVD 183
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-141 1.29e-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: 57.05  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  43 RALDLACGTGGFTREL-RAAGWDVTGLDFSEAMLAEARV-----RLPGVPFVQGDLRTFEL--GERFGLVTC--VFDSLn 112
Cdd:cd02440     1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaalLADNVEVLKGDAEELPPeaDESFDVIISdpPLHHL- 79

                          90       100
                  ....*....|....*....|....*....
gi 1801329872 113 nlltPGDLGAALRRARAHLSPGGLLAFDV 141
Cdd:cd02440    80 ----VEDLARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-143 4.22e-31

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 113.17  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872   3 RQPFTALAAVYDA-IMADVEYDHWADFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVR 81
Cdd:COG4976     8 EALFDQYADSYDAaLVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801329872  82 LPGVPFVQGDLRTF-ELGERFGLVTCvFDSLNNLltpGDLGAALRRARAHLSPGGLLAFDVNT 143
Cdd:COG4976    88 GVYDRLLVADLADLaEPDGRFDLIVA-ADVLTYL---GDLAAVFAGVARALKPGGLFIFSVED 146
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
40-141 5.71e-28

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 102.59  E-value: 5.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  40 GPGRALDLACGTGGFTRELRAA--GWDVTGLDFSEAMLAEARVRLPGVPFVQGDLRTFELGERFGLVTCvFDSLNNLltp 117
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLVVS-NAALHWL--- 76

                          90       100
                  ....*....|....*....|....
gi 1801329872 118 GDLGAALRRARAHLSPGGLLAFDV 141
Cdd:COG4106    77 PDHAALLARLAAALAPGGVLAVQV 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 17-141 3.78e-25

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: 96.24  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  17 MADVEYDHWADFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLP--GVPFVQGDLRT 94
Cdd:COG2227     1 MSDPDARDFWDRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAelNVDFVQGDLED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1801329872  95 FEL-GERFGLVTCvFDSLNNLltpGDLGAALRRARAHLSPGGLLAFDV 141
Cdd:COG2227    81 LPLeDGSFDLVIC-SEVLEHL---PDPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 45-135 1.12e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.38  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  45 LDLACGTGGFTREL-RAAGWDVTGLDFSEAMLAEARVRL----PGVPFVQGDLRTFEL-GERFGLVTCVFdsLNNLLTPG 118
Cdd:pfam13649   2 LDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFpDGSFDLVVSSG--VLHHLPDP 79

                          90
                  ....*....|....*..
gi 1801329872 119 DLGAALRRARAHLSPGG 135
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 22-152 4.96e-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: 83.12  E-value: 4.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  22 YDHWA---DFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLP----GVPFVQGDLRT 94
Cdd:COG2226     1 FDRVAaryDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAeaglNVEFVVGDAED 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1801329872  95 FELG-ERFGLVTCVFdSLNNLltpGDLGAALRRARAHLSPGGLLAFDVNTRLGVRELWE 152
Cdd:COG2226    81 LPFPdGSFDLVISSF-VLHHL---PDPERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 38-140 7.40e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.72  E-value: 7.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  38 LVGPGRALDLACGTGGFTRELRAA-GWDVTGLDFSEAMLAEARVR-----LPGVPFVQGDLRTFE--LGERFGLVTCvFD 109
Cdd:COG0500    24 LPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARaakagLGNVEFLVADLAELDplPAESFDLVVA-FG 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1801329872 110 SLnNLLTPGDLGAALRRARAHLSPGGLLAFD 140
Cdd:COG0500   103 VL-HHLPPEEREALLRELARALKPGGVLLLS 132
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 26-139 3.89e-14

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: 69.62  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  26 ADFVLSFARDGGLVGPGRALDLACGTGGFTRELRA--AGWDVTGLDFSEAMLAEARVRLPG-VPFVQGDLRTFELGER-F 101
Cdd:TIGR02072  20 AKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKrfPQAEFIALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSsF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1801329872 102 GLVTC--VFDSLNnlltpgDLGAALRRARAHLSPGGLLAF 139
Cdd:TIGR02072 100 DLIVSnlALQWCD------DLSQALSELARVLKPGGLLAF 133
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-139 1.95e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.22  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  45 LDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLP--GVPFVQGDLRTFELG-ERFGLVTCVFdSLNNLLtpgDLG 121
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPreGLTFVVGDAEDLPFPdNSFDLVLSSE-VLHHVE---DPE 76

                          90
                  ....*....|....*...
gi 1801329872 122 AALRRARAHLSPGGLLAF 139
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-171 6.71e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 64.76  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  41 PGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLPGVPFVQGDLRtfELGERFGLVTCvFDSLNNLLtpgDL 120
Cdd:pfam13489  23 PGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAA--VPAGKFDVIVA-REVLEHVP---DP 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1801329872 121 GAALRRARAHLSPGGLLAF-DVNTRLGVRELWEgdaiEGLAPLPDGGEVHYH 171
Cdd:pfam13489  97 PALLRQIAALLKPGGLLLLsTPLASDEADRLLL----EWPYLRPRNGHISLF 144
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-137 2.71e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 61.23  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  45 LDLACGTGGFTRELRAA--GWDVTGLDFSEAMLAEARVRLPGVPFVQGDLRTFELGERFGLVTCVFD---SLNNLLTPGD 119
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDvvvASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1801329872 120 LGAALRRARAHLSPGGLL 137
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 39-139 3.65e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 62.64  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  39 VGPG-RALDLACGTGGFTREL-RAAGWDVTGLDFSEAML--AEARVRLPGVP----FVQGDLRTFELGERFGLVTCVfDS 110
Cdd:COG2230    49 LKPGmRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLeyARERAAEAGLAdrveVRLADYRDLPADGQFDAIVSI-GM 127

                          90       100
                  ....*....|....*....|....*....
gi 1801329872 111 LnNLLTPGDLGAALRRARAHLSPGGLLAF 139
Cdd:COG2230   128 F-EHVGPENYPAYFAKVARLLKPGGRLLL 155
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 41-192 4.78e-12

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 63.81  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  41 PGRALDLACGTGGFTrELRAAGW---DVTGLDFSEAMLAEARVRLPGVPFVQGDLRTFELGERFGLV--TCVFDSLNNLL 115
Cdd:PRK01683   32 PRYVVDLGCGPGNST-ELLVERWpaaRITGIDSSPAMLAEARSRLPDCQFVEADIASWQPPQALDLIfaNASLQWLPDHL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872 116 TpgdlgaALRRARAHLSPGGLLA------FDVNTRLGVREL-----WE---GDAIEGLAPLPdggevhyHWSHHYDAEAD 181
Cdd:PRK01683  111 E------LFPRLVSLLAPGGVLAvqmpdnLDEPSHVLMREVaengpWEqnlPDRGARRAPLP-------PPHAYYDALAP 177

                         170
                  ....*....|.
gi 1801329872 182 VGvvqafCRVD 192
Cdd:PRK01683  178 AA-----CRVD 183
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 6-91 5.72e-12

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 63.25  E-value: 5.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872   6 FTALAAVYDaIMADVeydhwadfvLSF---------ARDGGLVGPG-RALDLACGTGGFTREL-RAAGW--DVTGLDFSE 72
Cdd:PRK00216   17 FDSIAPKYD-LMNDL---------LSFglhrvwrrkTIKWLGVRPGdKVLDLACGTGDLAIALaKAVGKtgEVVGLDFSE 86

                          90       100
                  ....*....|....*....|....*
gi 1801329872  73 AMLAEARVRL------PGVPFVQGD 91
Cdd:PRK00216   87 GMLAVGREKLrdlglsGNVEFVQGD 111
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-141 1.29e-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: 57.05  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  43 RALDLACGTGGFTREL-RAAGWDVTGLDFSEAMLAEARV-----RLPGVPFVQGDLRTFEL--GERFGLVTC--VFDSLn 112
Cdd:cd02440     1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaalLADNVEVLKGDAEELPPeaDESFDVIISdpPLHHL- 79

                          90       100
                  ....*....|....*....|....*....
gi 1801329872 113 nlltPGDLGAALRRARAHLSPGGLLAFDV 141
Cdd:cd02440    80 ----VEDLARFLEEARRLLKPGGVLVLTL 104
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 45-139 3.61e-10

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 58.62  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  45 LDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLPGVPFVQGDLrtfelgERFGLVTCVFD-SLNNLLTP--GDLG 121
Cdd:PRK10258   47 LDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYLAGDI------ESLPLATATFDlAWSNLAVQwcGNLS 120

                          90
                  ....*....|....*...
gi 1801329872 122 AALRRARAHLSPGGLLAF 139
Cdd:PRK10258  121 TALRELYRVVRPGGVVAF 138
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 27-111 2.27e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 56.00  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  27 DFVLSFARDGGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRLP--GVP----FVQGDLRtfELGER 100
Cdd:PRK07580   50 DTVLSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPeaGLAgnitFEVGDLE--SLLGR 127

                          90
                  ....*....|.
gi 1801329872 101 FGLVTCvFDSL 111
Cdd:PRK07580  128 FDTVVC-LDVL 137
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
6-137 1.63e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 53.60  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872   6 FTALAAVYDaIMADV----EYDHWADFVLSfaRDGGLVGpGRALDLACGTG----GFTRELRAAGwDVTGLDFSEAMLAE 77
Cdd:pfam01209   8 FSSVASKYD-LMNDVisfgIHRLWKDFTMK--CMGVKRG-NKFLDVAGGTGdwtfGLSDSAGSSG-KVVGLDINENMLKE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801329872  78 ARVRLP-----GVPFVQGDLRTFELGE-RFGLVTCVFDSLNnllTPgDLGAALRRARAHLSPGGLL 137
Cdd:pfam01209  83 GEKKAKeegkyNIEFLQGNAEELPFEDdSFDIVTISFGLRN---FP-DYLKVLKEAFRVLKPGGRV 144
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-138 9.58e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.11  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  43 RALDLACGTGGFTRELR---AAGWDVTGLDFSEAMLAEARVR-----LPGVPFVQGDLRTFEL---GERFGLVTCvFDSL 111
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAeelGPNAEVVGIDISEEAIEKARENaqklgFDNVEFEQGDIEELPElleDDKFDVVIS-NCVL 84

                          90       100
                  ....*....|....*....|....*..
gi 1801329872 112 NNLltpGDLGAALRRARAHLSPGGLLA 138
Cdd:pfam13847  85 NHI---PDPDKVLQEILRVLKPGGRLI 108
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 41-141 3.67e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 46.61  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  41 PGRALDLACGTGGFTREL--RAAGWDVTGLDFSEAMLAEARVRlpGVPFVQGDLRTFELGERFGLVTCvfdslNNLL--T 116
Cdd:PRK14103   30 ARRVVDLGCGPGNLTRYLarRWPGAVIEALDSSPEMVAAARER--GVDARTGDVRDWKPKPDTDVVVS-----NAALqwV 102

                          90       100
                  ....*....|....*....|....*..
gi 1801329872 117 PG--DLgaaLRRARAHLSPGGLLAFDV 141
Cdd:PRK14103  103 PEhaDL---LVRWVDELAPGSWIAVQV 126
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 37-135 2.07e-05

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 43.73  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  37 GLVGPG-RALDLACGTGGFTRELRAAG-WDVTGLDFSEAMLAEARVRlPGVPFVQGDLRTFE--------LGERFGLVTC 106
Cdd:pfam01728  17 GLLKPGkTVLDLGAAPGGWSQVALQRGaGKVVGVDLGPMQLWKPRND-PGVTFIQGDIRDPEtldlleelLGRKVDLVLS 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1801329872 107 ---VFDSLNNLL---TPGDLG-AALRRARAHLSPGG 135
Cdd:pfam01728  96 dgsPFISGNKVLdhlRSLDLVkAALEVALELLRKGG 131
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
 26-78 2.81e-05

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 44.13  E-value: 2.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1801329872  26 ADFVLSFARDGGLvgpGRALDLACGTGGFTRELrAAGWD-VTGLDFSEAMLAEA 78
Cdd:TIGR04345  30 AELALAQFRNKSR---KRALDIGCAVGRASFEL-ARYFDeVDGIDFSARFIRPA 79
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 30-139 7.42e-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: 42.24  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  30 LSFARDGGLVgpgraLDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARVRL-----PGVPFVQGDLRTFEL-GERFGL 103
Cdd:COG1041    21 LAGAKEGDTV-----LDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLehygyEDADVIRGDARDLPLaDESVDA 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1801329872 104 VtcVFD------------SLNNLLTpgdlgAALRRARAHLSPGGLLAF 139
Cdd:COG1041    96 I--VTDppygrsskisgeELLELYE-----KALEEAARVLKPGGRVVI 136
PRK08317 PRK08317
hypothetical protein; Provisional
 39-91 8.50e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.62  E-value: 8.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801329872  39 VGPG-RALDLACGTGGFTREL-RAAGWD--VTGLDFSEAMLAEARVR----LPGVPFVQGD 91
Cdd:PRK08317   17 VQPGdRVLDVGCGPGNDARELaRRVGPEgrVVGIDRSEAMLALAKERaaglGPNVEFVRGD 77
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 43-160 1.73e-04

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 42.09  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  43 RALDLACGTGGFTreLRAAGW---DVTGLDFSEAMLAEAR--VRLPGVP----FVQGD----LRTF-ELGERFGLVtcVF 108
Cdd:COG1092   219 RVLNLFSYTGGFS--VHAAAGgakSVTSVDLSATALEWAKenAALNGLDdrheFVQADafdwLRELaREGERFDLI--IL 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801329872 109 D--SLNNllTPGDLGAALR-------RARAHLSPGGLLAFDVNTRLGVRELWEgDAIEGLA 160
Cdd:COG1092   295 DppAFAK--SKKDLFDAQRdykdlnrLALKLLAPGGILVTSSCSRHFSLDLFL-EILARAA 352
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
39-106 5.98e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 39.72  E-value: 5.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801329872  39 VGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAE-----ARVRLPGVPFVQGDLRTFELGERFGLVTC 106
Cdd:PRK11207   29 VKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANlerikAAENLDNLHTAVVDLNNLTFDGEYDFILS 101
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 26-109 6.12e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 40.54  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  26 ADFVLSFArdgGLVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLAEARV-----RLPGVPFVQGDLRTF----E 96
Cdd:COG2265   222 YAAALEWL---DLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDAREnarlnGLKNVEFVAGDLEEVlpelL 298

                          90
                  ....*....|...
gi 1801329872  97 LGERFGLVtcVFD 109
Cdd:COG2265   299 WGGRPDVV--VLD 309
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
26-104 1.26e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.73  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  26 ADFVLSFARDGGLVGPGRALDLACGTGGFTR--ELRAAGwDVTGLDFSEAMLAEARVRLPG----VPFVQGDLRTFELGE 99
Cdd:COG2263    31 AAELLHLAYLRGDIEGKTVLDLGCGTGMLAIgaALLGAK-KVVGVDIDPEALEIARENAERlgvrVDFIRADVTRIPLGG 109


                  ....*
gi 1801329872 100 RFGLV 104
Cdd:COG2263   110 SVDTV 114
PRK06202 PRK06202
hypothetical protein; Provisional
 40-106 6.04e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 36.90  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  40 GPGRALDLACGTGGFTRELraAGW--------DVTGLDFSE-AM-LAEARVRLPGV---PFVQGDLrtFELGERFGLVTC 106
Cdd:PRK06202   60 RPLTLLDIGCGGGDLAIDL--ARWarrdglrlEVTAIDPDPrAVaFARANPRRPGVtfrQAVSDEL--VAEGERFDVVTS 135
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
51-109 6.14e-03

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 37.27  E-value: 6.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801329872  51 TGG-------FTRELRAAGWDVTGLDFSEAMLAEARvRLPGVPFVQGDLRTFE-LGERFGLVTCVFD 109
Cdd:COG0451     5 TGGagfigshLARRLLARGHEVVGLDRSPPGAANLA-ALPGVEFVRGDLRDPEaLAAALAGVDAVVH 70
TehB pfam03848
Tellurite resistance protein TehB;
38-135 6.59e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 36.75  E-value: 6.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329872  38 LVGPGRALDLACGTGGFTRELRAAGWDVTGLDFSEAMLA-----EARVRLPGVPFVQGDLRTFELGER--FGLVTCVFDS 110
Cdd:pfam03848  28 IVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIAnlqriKEKENLDNIHTALYDINNATIDENydFILSTVVLMF 107

                          90       100
                  ....*....|....*....|....*
gi 1801329872 111 LNNLLTPGdlgaALRRARAHLSPGG 135
Cdd:pfam03848 108 LEPERIPG----IIANMQECTNPGG 128
 
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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