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Conserved domains on  [gi|2068385656|ref|WP_218470305|]
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methyltransferase domain-containing protein [Nocardia iowensis]

Protein Classification

methyltransferase domain-containing protein( domain architecture ID 1004954)

methyltransferase domain-containing protein may be a class I SAM-dependent methyltransferase that 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|GO:0008168
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08317 super family cl32293
hypothetical protein; Provisional
 19-249 1.01e-42

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK08317:

Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 145.08  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  19 MPGAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAAR---GACPIGVDPDQRMLDVARTRW----PALDFRSGSAQA 91
Cdd:PRK08317    1 LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAaglgPNVEFVRGDADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  92 LPLPDESASGYRADKVFHEIADPAAALAEAERVLVPGGRIVLLDLDWDAVVVDSDDPATTRAIVHARADAITNPQAARGC 171
Cdd:PRK08317   81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDTLVWHSGDRALMRKILNFWSDHFADPWLGRRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656 172 RNMLLASGFRDVTVAGRLSIFTD--ERMLGL-LTRLTEVAVANGELDRERTEAWLAEQTERAGSGRLMLAIPLFVAAATR 248
Cdd:PRK08317  161 PGLFREAGLTDIEVEPYTLIETDlkEADKGFgLIRAARRAVEAGGISADEADAWLADLAQLARAGEFFFSVTGFLVVGRK 240


                  .
gi 2068385656 249 P 249
Cdd:PRK08317  241 P 241
 
Name Accession Description Interval E-value
PRK08317 PRK08317
hypothetical protein; Provisional
 19-249 1.01e-42

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 145.08  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  19 MPGAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAAR---GACPIGVDPDQRMLDVARTRW----PALDFRSGSAQA 91
Cdd:PRK08317    1 LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAaglgPNVEFVRGDADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  92 LPLPDESASGYRADKVFHEIADPAAALAEAERVLVPGGRIVLLDLDWDAVVVDSDDPATTRAIVHARADAITNPQAARGC 171
Cdd:PRK08317   81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDTLVWHSGDRALMRKILNFWSDHFADPWLGRRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656 172 RNMLLASGFRDVTVAGRLSIFTD--ERMLGL-LTRLTEVAVANGELDRERTEAWLAEQTERAGSGRLMLAIPLFVAAATR 248
Cdd:PRK08317  161 PGLFREAGLTDIEVEPYTLIETDlkEADKGFgLIRAARRAVEAGGISADEADAWLADLAQLARAGEFFFSVTGFLVVGRK 240


                  .
gi 2068385656 249 P 249
Cdd:PRK08317  241 P 241
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 17-138 1.09e-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: 85.05  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  17 DAMPGAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPA----LDFRSGSAQAL 92
Cdd:COG2226     2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2068385656  93 PLPDESASGYRADKVFHEIADPAAALAEAERVLVPGGRIVLLDLDW 138
Cdd:COG2226    82 PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-129 1.16e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.59  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  41 VLDVGCGSGRAVAELAAR-GACPIGVDPDQRMLDVARTRW----PALDFRSGSAQALPLPDESASGYRADKVFHEIADPA 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 2068385656 116 AALAEAE--RVLVPGG 129
Cdd:pfam13649  81 LEAALREiaRVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 31-136 5.67e-11

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: 60.35  E-value: 5.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELA----ARGACpIGVDPDQRMLDVARTRWPA---LDFRSGSAQALPLPDES----- 98
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAksapDRGKV-TGVDFSSEMLEVAKKKSELplnIEFIQADAEALPFEDNSfdavt 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2068385656  99 -ASGYR----ADKVFHEIAdpaaalaeaeRVLVPGGRIVLLDL 136
Cdd:TIGR01934 112 iAFGLRnvtdIQKALREMY----------RVLKPGGRLVILEF 144
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 41-138 7.56e-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: 46.65  E-value: 7.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  41 VLDVGCGSGRAVAELAARGACP-IGVDPDQRMLDVARTRWPAL-----DFRSGSA-QALPLPDESasgyrADKVF----- 108
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARvTGVDISPVALELARKAAAALladnvEVLKGDAeELPPEADES-----FDVIIsdppl 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2068385656 109 -HEIADPAAALAEAERVLVPGGRIVLLDLDW 138
Cdd:cd02440    77 hHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PRK08317 PRK08317
hypothetical protein; Provisional
 19-249 1.01e-42

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 145.08  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  19 MPGAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAAR---GACPIGVDPDQRMLDVARTRW----PALDFRSGSAQA 91
Cdd:PRK08317    1 LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAaglgPNVEFVRGDADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  92 LPLPDESASGYRADKVFHEIADPAAALAEAERVLVPGGRIVLLDLDWDAVVVDSDDPATTRAIVHARADAITNPQAARGC 171
Cdd:PRK08317   81 LPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWDTLVWHSGDRALMRKILNFWSDHFADPWLGRRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656 172 RNMLLASGFRDVTVAGRLSIFTD--ERMLGL-LTRLTEVAVANGELDRERTEAWLAEQTERAGSGRLMLAIPLFVAAATR 248
Cdd:PRK08317  161 PGLFREAGLTDIEVEPYTLIETDlkEADKGFgLIRAARRAVEAGGISADEADAWLADLAQLARAGEFFFSVTGFLVVGRK 240


                  .
gi 2068385656 249 P 249
Cdd:PRK08317  241 P 241
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 17-138 1.09e-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: 85.05  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  17 DAMPGAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPA----LDFRSGSAQAL 92
Cdd:COG2226     2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2068385656  93 PLPDESASGYRADKVFHEIADPAAALAEAERVLVPGGRIVLLDLDW 138
Cdd:COG2226    82 PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 34-133 3.25e-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: 75.05  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  34 HLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPAL--DFRSGSAQALPLPDES-----ASGyradk 106
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnvDFVQGDLEDLPLEDGSfdlviCSE----- 95

                          90       100
                  ....*....|....*....|....*..
gi 2068385656 107 VFHEIADPAAALAEAERVLVPGGRIVL 133
Cdd:COG2227    96 VLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-129 1.16e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.59  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  41 VLDVGCGSGRAVAELAAR-GACPIGVDPDQRMLDVARTRW----PALDFRSGSAQALPLPDESASGYRADKVFHEIADPA 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 2068385656 116 AALAEAE--RVLVPGG 129
Cdd:pfam13649  81 LEAALREiaRVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 31-136 3.98e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 69.41  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELAARGACP---IGVDPDQRMLDVARTRWPA------LDFRSGSAQALPLPDES--- 98
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKTgevVGLDFSEGMLAVGREKLRDlglsgnVEFVQGDAEALPFPDNSfda 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2068385656  99 ---ASGYR----ADKVFHEIAdpaaalaeaeRVLVPGGRIVLLDL 136
Cdd:PRK00216  125 vtiAFGLRnvpdIDKALREMY----------RVLKPGGRLVILEF 159
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-133 3.48e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.45  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  42 LDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTR--WPALDFRSGSAQALPLPDESA----SGYradkVFHEIADPA 115
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKapREGLTFVVGDAEDLPFPDNSFdlvlSSE----VLHHVEDPE 76

                          90
                  ....*....|....*...
gi 2068385656 116 AALAEAERVLVPGGRIVL 133
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
21-133 5.95e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 62.32  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  21 GAAELRTHSYELLHLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPALDFRSGSAQALPLPDESAS 100
Cdd:COG4976    30 APALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFD 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2068385656 101 G--------YRAD--KVFHEIAdpaaalaeaeRVLVPGGRIVL 133
Cdd:COG4976   110 LivaadvltYLGDlaAVFAGVA----------RALKPGGLFIF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
37-133 6.39e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 60.22  E-value: 6.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  37 PGASVLDVGCGSGRAVAELAAR--GACPIGVDPDQRMLDVARTRWPALDFRSGSAQALPlPDESASGYRADKVFHEIADP 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPDH 79

                          90
                  ....*....|....*....
gi 2068385656 115 AAALAEAERVLVPGGRIVL 133
Cdd:COG4106    80 AALLARLAAALAPGGVLAV 98
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 31-136 5.67e-11

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: 60.35  E-value: 5.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELA----ARGACpIGVDPDQRMLDVARTRWPA---LDFRSGSAQALPLPDES----- 98
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAksapDRGKV-TGVDFSSEMLEVAKKKSELplnIEFIQADAEALPFEDNSfdavt 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2068385656  99 -ASGYR----ADKVFHEIAdpaaalaeaeRVLVPGGRIVLLDL 136
Cdd:TIGR01934 112 iAFGLRnvtdIQKALREMY----------RVLKPGGRLVILEF 144
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 32-137 3.81e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.62  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  32 LLHLPPGASVLDVGCGSGRAVAELAAR-GACPIGVDPDQRMLDVARTRWPAL-----DFRSGS-AQALPLPDESASGYRA 104
Cdd:COG0500    21 LERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAglgnvEFLVADlAELDPLPAESFDLVVA 100

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2068385656 105 DKVFHEIADPAAALAEAE--RVLVPGGRIVLLDLD 137
Cdd:COG0500   101 FGVLHHLPPEEREALLRElaRALKPGGVLLLSASD 135
arsM PRK11873
arsenite methyltransferase;
35-213 1.24e-08

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 54.18  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  35 LPPGASVLDVGCGSGRAVAeLAARGACP----IGVDPDQRMLDVARTRWPAL-----DFRSGSAQALPLPDESA------ 99
Cdd:PRK11873   75 LKPGETVLDLGSGGGFDCF-LAARRVGPtgkvIGVDMTPEMLAKARANARKAgytnvEFRLGEIEALPVADNSVdviisn 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656 100 -----SGYRaDKVFHEIAdpaaalaeaeRVLVPGGRIVLLDldwdaVVVDSDDPATTRaivharadaiTNPQAARGC--- 171
Cdd:PRK11873  154 cvinlSPDK-ERVFKEAF----------RVLKPGGRFAISD-----VVLRGELPEEIR----------NDAELYAGCvag 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2068385656 172 -------RNMLLASGFRDVTVAGRLSIFTDERmLGLLTRLTEVAVANGE 213
Cdd:PRK11873  208 alqeeeyLAMLAEAGFVDITIQPKREYRIPDA-REFLEDWGIAPGRQLD 255
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 31-133 4.48e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.39  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELAARGACPI-GVDPDQRMLDVARTRWPA------LDFRSGSAQALPLPDesasgyR 103
Cdd:COG2230    45 RKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVtGVTLSPEQLEYARERAAEagladrVEVRLADYRDLPADG------Q 118

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2068385656 104 ADKV-----FHEIADPAAALAEAE--RVLVPGGRIVL 133
Cdd:COG2230   119 FDAIvsigmFEHVGPENYPAYFAKvaRLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 41-138 7.56e-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: 46.65  E-value: 7.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  41 VLDVGCGSGRAVAELAARGACP-IGVDPDQRMLDVARTRWPAL-----DFRSGSA-QALPLPDESasgyrADKVF----- 108
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARvTGVDISPVALELARKAAAALladnvEVLKGDAeELPPEADES-----FDVIIsdppl 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2068385656 109 -HEIADPAAALAEAERVLVPGGRIVLLDLDW 138
Cdd:cd02440    77 hHLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 37-140 3.04e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  37 PGASVLDVGCGSGRAVAELAAR---GACPIGVDPDQRMLDVARTRWPALD-----FRSGSAQALP--LPDESASGYRADK 106
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGfdnveFEQGDIEELPelLEDDKFDVVISNC 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2068385656 107 VFHEIADPAAALAEAERVLVPGGRIVLLDLDWDA 140
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLA 116
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
37-135 5.79e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 45.89  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  37 PGASVLDVGCGSGR---AVAELAARGACPIGVDPDQRMLDVARTR-----WPALDFRSGSAQALPLPDES------ASGY 102
Cdd:pfam01209  42 RGNKFLDVAGGTGDwtfGLSDSAGSSGKVVGLDINENMLKEGEKKakeegKYNIEFLQGNAEELPFEDDSfdivtiSFGL 121

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2068385656 103 R----ADKVFHEIAdpaaalaeaeRVLVPGGRIVLLD 135
Cdd:pfam01209 122 RnfpdYLKVLKEAF----------RVLKPGGRVVCLE 148
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 34-146 9.08e-06

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: 44.94  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  34 HLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPALDFRS-----GSAQALPLPDES---------- 98
Cdd:COG1041    23 GAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDadvirGDARDLPLADESvdaivtdppy 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2068385656  99 --ASGYRADKVFHEIADPAAALAeaeRVLVPGGRIVLL-DLDWDAVVVDSD 146
Cdd:COG1041   103 grSSKISGEELLELYEKALEEAA---RVLKPGGRVVIVtPRDIDELLEEAG 150
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 35-92 1.73e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.44  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068385656  35 LPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPA------LDFRSGSAQAL 92
Cdd:PRK07580   61 DLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEaglagnITFEVGDLESL 124
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 23-96 5.96e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 43.21  E-value: 5.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068385656  23 AELRTHSYELLH-LPPG---ASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPALDFRSGSAQALPLPD 96
Cdd:PRK10258   24 AELQRQSADALLaMLPQrkfTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLAT 101
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 39-98 3.09e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 41.05  E-value: 3.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068385656  39 ASVLDVGCGSG----RAVAELAARGACPI-GVDPDQRMLDVARTRWPALDFRSGSAQALPLPDES 98
Cdd:PRK11088   87 TALLDIGCGEGyythALADALPEITTMQLfGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQS 151
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 31-84 5.37e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 40.31  E-value: 5.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  31 ELL----HLPPGAsVLDVGCGSGRAVAELAAR--GACPIGVDPDQRMLDVARTRWPALDF 84
Cdd:PRK01683   22 DLLarvpLENPRY-VVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLPDCQF 80
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 42-131 6.56e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.12  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  42 LDVGCGSGRAVAELAARGACP--IGVDPDQRMLDVARTRWPALDFRSGSAQALPLPDESAS-GYRAD-----KVFHEIAD 113
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELdPGSFDvvvasNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2068385656 114 PAAALAEAERVLVPGGRI 131
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 31-85 9.19e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 39.30  E-value: 9.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPALDFR 85
Cdd:COG2518    60 EALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARERLAALGYD 114
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 34-72 1.81e-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: 38.93  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2068385656  34 HLPP--GASVLDVGCGSG----RAVAELAARgacPIGVDPDQRML 72
Cdd:pfam08003 110 HLSPlkGRTILDVGCGNGyhmwRMLGEGAAM---VVGIDPSELFL 151
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-84 3.71e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.02  E-value: 3.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2068385656  35 LPPGASVLDVGCGSGRAVAELAARGACPIGVDPDQRMLDVARTRWPALDF 84
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQF 69
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
31-56 5.17e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 36.96  E-value: 5.17e-03
                          10        20
                  ....*....|....*....|....*.
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELA 56
Cdd:pfam01135  67 ELLELKPGMRVLEIGSGSGYLTACFA 92
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 39-98 5.66e-03

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: 37.27  E-value: 5.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068385656  39 ASVLDVGCGSGRAVAELAARG--ACPIGVDPDQRMLDVARTRWPA-LDFRSGSAQALPLPDES 98
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSEnVQFICGDAEKLPLEDSS 98
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
34-76 8.59e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 36.69  E-value: 8.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2068385656  34 HLPPGASVLDVGCGSG-RAVAelAAR-GACPI-GVDPDQRMLDVAR 76
Cdd:COG2264   145 LLKPGKTVLDVGCGSGiLAIA--AAKlGAKRVlAVDIDPVAVEAAR 188
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 34-134 8.76e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 36.53  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068385656  34 HLPPGASVLDVGCGS-GRAVAELA-ARGACPIGVDPDQRMLDVARtRWPALDFRSGSAQALPLPDESASGYRADKVFhEI 111
Cdd:cd05188   131 VLKPGDTVLVLGAGGvGLLAAQLAkAAGARVIVTDRSDEKLELAK-ELGADHVIDYKEEDLEEELRLTGGGGADVVI-DA 208

                          90       100
                  ....*....|....*....|...
gi 2068385656 112 ADPAAALAEAERVLVPGGRIVLL 134
Cdd:cd05188   209 VGGPETLAQALRLLRPGGRIVVV 231
PRK14968 PRK14968
putative methyltransferase; Provisional
 31-66 8.99e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.03  E-value: 8.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2068385656  31 ELLHLPPGASVLDVGCGSGRAVAELAARGACPIGVD 66
Cdd:PRK14968   17 ENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVD 52
 
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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