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Conserved domains on  [gi|209447527|pdb|3EGE|A]
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Chain A, Putative methyltransferase from antibiotic biosynthesis pathway

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 5-132 3.37e-23

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: 91.98  E-value: 3.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        5 YNSIGKQYSQTRvpdirivnAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQAV-----VHPQVE 79
Cdd:COG2226   1 FDRVAARYDGRE--------ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAReraaeAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
3EGE_A       80 WFTGYAENLALPDKSVDGVISILAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD 132
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKpGGRLVVVDFS 126
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 5-132 3.37e-23

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: 91.98  E-value: 3.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        5 YNSIGKQYSQTRvpdirivnAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQAV-----VHPQVE 79
Cdd:COG2226   1 FDRVAARYDGRE--------ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAReraaeAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
3EGE_A       80 WFTGYAENLALPDKSVDGVISILAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD 132
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKpGGRLVVVDFS 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-128 4.55e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         40 DIGAGTGGYSVALANQGLFVYAVEPS---IV*RQQAVVHPQVEWFTGYAENLALPDKSVDGVISILAIHHFSHLEKSFQE 116
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISpemLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALRE 81

                          90
                  ....*....|...
3EGE_A        117 *QRIIR-DGTIVL 128
Cdd:pfam08241  82 IARVLKpGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 18-132 1.21e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.17  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        18 PDIRIVNA-IINLLNLPKGSVIADIGAGTGGYSVALANQ----GLfVYAVEPS-----IV*RQQAVVHPQVEWFTGYAEN 87
Cdd:PRK08317   2 PDFRRYRArTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSeamlaLAKERAAGLGPNVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
3EGE_A        88 LALPDKSVDGVISILAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD 132
Cdd:PRK08317  81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRpGGRVVVLDTD 126
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 30-130 1.32e-07

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: 51.13  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         30 LNLPKGSVIADIGAGTGGYSVALANQGLFV--YAVEPSIV*RQQAVVH--PQVEWFTGYAENLALPDKSVDGVISILAIH 105
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTKlsENVQFICGDAEKLPLEDSSFDLIVSNLALQ 109

                          90       100
                  ....*....|....*....|....*
3EGE_A        106 HFSHLEKSFQE*QRIIRDGTIVLLT 130
Cdd:TIGR02072 110 WCDDLSQALSELARVLKPGGLLAFS 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-133 1.36e-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: 48.58  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       38 IADIGAGTGGYSVALANQGLF-VYAVEPS------IV*RQQAVVHPQVEWFTG-YAENLALPDKSVDGVISILAIHHFSH 109
Cdd:cd02440   2 VLDLGCGTGALALALASGPGArVTGVDISpvalelARKAAAALLADNVEVLKGdAEELPPEADESFDVIISDPPLHHLVE 81

                        90       100
                ....*....|....*....|....*
3EGE_A      110 LEKSF-QE*QRIIRDGTIVLLTFDI 133
Cdd:cd02440  82 DLARFlEEARRLLKPGGVLVLTLVL 106
rADc smart00650
Ribosomal RNA adenine dimethylases;
22-63 4.44e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.80  E-value: 4.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
3EGE_A          22 IVNAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVE 63
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIE 42
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 5-132 3.37e-23

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: 91.98  E-value: 3.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        5 YNSIGKQYSQTRvpdirivnAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQAV-----VHPQVE 79
Cdd:COG2226   1 FDRVAARYDGRE--------ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAReraaeAGLNVE 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
3EGE_A       80 WFTGYAENLALPDKSVDGVISILAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD 132
Cdd:COG2226  73 FVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKpGGRLVVVDFS 126
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 19-131 7.48e-17

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: 74.67  E-value: 7.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       19 DIRIVNAIINLLnlPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQA---VVHPQVEWFTGYAENLALPDKSV 95
Cdd:COG2227  11 DRRLAALLARLL--PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIArerAAELNVDFVQGDLEDLPLEDGSF 88

                        90       100       110
                ....*....|....*....|....*....|....*.
3EGE_A       96 DGVISILAIHHFSHLEKSFQE*QRIIRDGTIVLLTF 131
Cdd:COG2227  89 DLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-128 4.55e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 4.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         40 DIGAGTGGYSVALANQGLFVYAVEPS---IV*RQQAVVHPQVEWFTGYAENLALPDKSVDGVISILAIHHFSHLEKSFQE 116
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISpemLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALRE 81

                          90
                  ....*....|...
3EGE_A        117 *QRIIR-DGTIVL 128
Cdd:pfam08241  82 IARVLKpGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 38-124 6.70e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 68.36  E-value: 6.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         38 IADIGAGTGGYSVALANQ-GLFVYAVEPS-----IV*RQQAVVHPQVEWFTGYAENLALPDKSVDGVISILAIHHFSH-- 109
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSpemleRARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDpd 80

                          90
                  ....*....|....*
3EGE_A        110 LEKSFQE*QRIIRDG 124
Cdd:pfam13649  81 LEAALREIARVLKPG 95
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
21-131 9.73e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.46  E-value: 9.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       21 RIVNAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQAVVHP-QVEWFTGYAENLALPDKSVDGVI 99
Cdd:COG4976  33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGvYDRLLVADLADLAEPDGRFDLIV 112

                        90       100       110
                ....*....|....*....|....*....|..
3EGE_A      100 SILAIHHFSHLEKSFQE*QRIIRDGTIVLLTF 131
Cdd:COG4976 113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV 144
PRK08317 PRK08317
hypothetical protein; Provisional
 18-132 1.21e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.17  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        18 PDIRIVNA-IINLLNLPKGSVIADIGAGTGGYSVALANQ----GLfVYAVEPS-----IV*RQQAVVHPQVEWFTGYAEN 87
Cdd:PRK08317   2 PDFRRYRArTFELLAVQPGDRVLDVGCGPGNDARELARRvgpeGR-VVGIDRSeamlaLAKERAAGLGPNVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
3EGE_A        88 LALPDKSVDGVISILAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD 132
Cdd:PRK08317  81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRpGGRVVVLDTD 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 24-130 2.34e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.61  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       24 NAIINLLNLPKGSVIADIGAGTGGYSVALANQGLF-VYAVEPS---IV*---RQQAVVHPQVEWFTG-YAENLALPDKSV 95
Cdd:COG0500  16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGrVIGIDLSpeaIALaraRAAKAGLGNVEFLVAdLAELDPLPAESF 95

                        90       100       110
                ....*....|....*....|....*....|....*..
3EGE_A       96 DGVISILAIHHFSH--LEKSFQE*QRIIRDGTIVLLT 130
Cdd:COG0500  96 DLVVAFGVLHHLPPeeREALLRELARALKPGGVLLLS 132
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 27-168 3.69e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 52.85  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        27 INLLNLPKGSVIADIGAGTGGYSVALANQGLF---VYAVEPSI----V*RQ---QAVVHPQVEWFTGYAENLALPDKSVD 96
Cdd:PRK00216  44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEgmlaVGREklrDLGLSGNVEFVQGDAEALPFPDNSFD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        97 GV-ISiLAIHHFSHLEKSFQE*QRIIR-DGTIVLLTFD------IRLAQRIWL-----------------YDYfpfLWED 151
Cdd:PRK00216 124 AVtIA-FGLRNVPDIDKALREMYRVLKpGGRLVILEFSkptnppLKKAYDFYLfkvlpligklisknaeaYSY---LAES 199

                        170
                 ....*....|....*..
3EGE_A       152 ALRFLPLDEQINLLQEN 168
Cdd:PRK00216 200 IRAFPDQEELAAMLEEA 216
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 30-130 1.32e-07

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: 51.13  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         30 LNLPKGSVIADIGAGTGGYSVALANQGLFV--YAVEPSIV*RQQAVVH--PQVEWFTGYAENLALPDKSVDGVISILAIH 105
Cdd:TIGR02072  30 KGIFIPASVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTKlsENVQFICGDAEKLPLEDSSFDLIVSNLALQ 109

                          90       100
                  ....*....|....*....|....*
3EGE_A        106 HFSHLEKSFQE*QRIIRDGTIVLLT 130
Cdd:TIGR02072 110 WCDDLSQALSELARVLKPGGLLAFS 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 38-133 1.36e-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: 48.58  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       38 IADIGAGTGGYSVALANQGLF-VYAVEPS------IV*RQQAVVHPQVEWFTG-YAENLALPDKSVDGVISILAIHHFSH 109
Cdd:cd02440   2 VLDLGCGTGALALALASGPGArVTGVDISpvalelARKAAAALLADNVEVLKGdAEELPPEADESFDVIISDPPLHHLVE 81

                        90       100
                ....*....|....*....|....*
3EGE_A      110 LEKSF-QE*QRIIRDGTIVLLTFDI 133
Cdd:cd02440  82 DLARFlEEARRLLKPGGVLVLTLVL 106
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 21-132 1.75e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.54  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       21 RIVNAIINLLNLPKGSVIADIGAGTGGYSVALA-NQGLFVYAVEPSIV*R-------QQAVVHPQVEWFTGYAENLAlPD 92
Cdd:COG2230  38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLeyareraAEAGLADRVEVRLADYRDLP-AD 116

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
3EGE_A       93 KSVDGVISILAIHHFS--HLEKSFQE*QRIIRDGTIVLLTFD 132
Cdd:COG2230 117 GQFDAIVSIGMFEHVGpeNYPAYFAKVARLLKPGGRLLLHTP 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
34-131 1.79e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.28  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A       34 KGSVIADIGAGTGGYSVALANQ--GLFVYAVEPSIV*RQQA-VVHPQVEWFTGYAENLAlPDKSVDGVISILAIHHFSHL 110
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARArARLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPDH 79

                        90       100
                ....*....|....*....|.
3EGE_A      111 EKSFQE*QRIIRDGTIVLLTF 131
Cdd:COG4106  80 AALLARLAAALAPGGVLAVQV 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 28-168 2.01e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 49.35  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         28 NLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVEPSIV*RQQAVVHPQVEWFtgYAENLALPDKSVDGVISILAIHHF 107
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQF--DEQEAAVPAGKFDVIVAREVLEHV 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
3EGE_A        108 SHLEKSFQE*QRIIRDGTIVLL-TFDIRLAQRIWL-YDYFPFLWEDALRFLPLDEQINLLQEN 168
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLsTPLASDEADRLLlEWPYLRPRNGHISLFSARSLKRLLEEA 156
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 18-63 5.52e-06

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 44.63  E-value: 5.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
3EGE_A         18 PDIRIVnaIINLLNLPKGSVIADIGAGTGGYSVALANQ--GLFVYAVE 63
Cdd:TIGR02469   5 REVRAL--TLAKLRLRPGDVLWDIGAGTGSVTIEAARLvpNGRVYAIE 50
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 18-64 1.32e-05

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 45.93  E-value: 1.32e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
3EGE_A       18 PDIRIVnaIINLLNLPKGSVIADIGAGTGGYSV--ALANQGLFVYAVEP 64
Cdd:COG2242 233 REVRAL--TLAKLALRPGDVLWDIGAGSGSVSIeaARLAPGGRVYAIER 279
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
19-95 5.35e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A        19 DIRIVNAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVE--PSIV*--RQQAVVHPQVEWFTGYAENLALP--D 92
Cdd:PRK14896  14 DDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIEldPRLAEflRDDEIAAGNVEIIEGDALKVDLPefN 93


                 ...
3EGE_A        93 KSV 95
Cdd:PRK14896  94 KVV 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 40-127 1.24e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.04  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         40 DIGAGTGGYSVALANQ--GLFVYAVEPS---------IV*RQQAVVHPQVEWFTGYAENLALPdkSVDGVISILAIHHFS 108
Cdd:pfam08242   2 EIGCGTGTLLRALLEAlpGLEYTGLDISpaaleaareRLAALGLLNAVRVELFQLDLGELDPG--SFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
3EGE_A        109 HLEKSFQE*QRIIRDGTIV 127
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
rADc smart00650
Ribosomal RNA adenine dimethylases;
22-63 4.44e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.80  E-value: 4.44e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
3EGE_A          22 IVNAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVE 63
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIE 42
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 34-130 1.08e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.55  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EGE_A         34 KGSVIADIGAGTGGYSVALA---NQGLFVYAVEPSIV*RQQAVVHPQ------VEWFTGYAENL--ALPDKSVDGVISIL 102
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAeelGPNAEVVGIDISEEAIEKARENAQklgfdnVEFEQGDIEELpeLLEDDKFDVVISNC 82

                          90       100
                  ....*....|....*....|....*...
3EGE_A        103 AIHHFSHLEKSFQE*QRIIRDGTIVLLT 130
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIIS 110
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 19-63 1.17e-03

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 39.34  E-value: 1.17e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
3EGE_A       19 DIRIVNAIINLLNLPKGSVIADIGAGTGGYSVALANQGLFVYAVE 63
Cdd:COG0030  22 DPNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVE 66
 
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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