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Conserved domains on  [gi|40018642|ref|NP_077025|]
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arginine-hydroxylase NDUFAF5, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

methyltransferase domain-containing protein( domain architecture ID 1002315)

methyltransferase domain-containing protein similar to vertebrate mitochondrial arginine-hydroxylase NDUFAF5 and bacterial malonyl-[acyl-carrier protein] O-methyltransferase

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
BioC super family cl37044
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-310 2.08e-32

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]


The actual alignment was detected with superfamily member TIGR02072:

Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 120.85  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   231 RAgFNTLTVDTDEIQVNYPGMFELMEDLQGMGESNCA---WNRKALLHrdtMLAAaavYREMYRNEdgSVPATYQIYYMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLER---YEQEFQPD--GLPLTYHVVYGI 237


                  ...
gi 40018642   308 GWK 310
Cdd:TIGR02072 238 AKK 240
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-310 2.08e-32

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: 120.85  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   231 RAgFNTLTVDTDEIQVNYPGMFELMEDLQGMGESNCA---WNRKALLHrdtMLAAaavYREMYRNEdgSVPATYQIYYMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLER---YEQEFQPD--GLPLTYHVVYGI 237


                  ...
gi 40018642   308 GWK 310
Cdd:TIGR02072 238 AKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 1.86e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 84.64  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 40018642   172 EQIHYILKPDGVFI 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 8.34e-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: 84.28  E-value: 8.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  94 LDLGCGRGYIAQYLNKETiGKFFQADIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226  27 LDLGCGTGRLALALAERG-ARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 40018642 170 ALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226 106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
PRK08317 PRK08317
hypothetical protein; Provisional
 93-182 1.77e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.42  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   93 ALDLGCGRG----YIAQYLNKEtiGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK08317  23 VLDVGCGPGndarELARRVGPE--GRVVGIDRSEAMLalaKERAAGLGPNVEfVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                         90
                 ....*....|....*...
gi 40018642  165 NDLPRALEQIHYILKPDG 182
Cdd:PRK08317 101 EDPARALAEIARVLRPGG 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 2.94e-10

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 56.67  E-value: 2.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSETEI----PTVSVL-AD-EEFLPFKENTFDLVVSSLSLHW-VND 166
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallaDNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                        90
                ....*....|....*....
gi 40018642 167 LPRALEQIHYILKPDGVFI 185
Cdd:cd02440  83 LARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-310 2.08e-32

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: 120.85  E-value: 2.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   231 RAgFNTLTVDTDEIQVNYPGMFELMEDLQGMGESNCA---WNRKALLHrdtMLAAaavYREMYRNEdgSVPATYQIYYMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLER---YEQEFQPD--GLPLTYHVVYGI 237


                  ...
gi 40018642   308 GWK 310
Cdd:TIGR02072 238 AKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 1.86e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 84.64  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 40018642   172 EQIHYILKPDGVFI 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 8.34e-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: 84.28  E-value: 8.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  94 LDLGCGRGYIAQYLNKETiGKFFQADIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226  27 LDLGCGTGRLALALAERG-ARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 40018642 170 ALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226 106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-182 7.44e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 80.30  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLNKETIGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWVN--DL 167
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLeraRERAAEAGLNVEfVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpDL 81

                          90
                  ....*....|....*
gi 40018642   168 PRALEQIHYILKPDG 182
Cdd:pfam13649  82 EAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 93-185 1.06e-14

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: 69.66  E-value: 1.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  93 ALDLGCGRGYIAQYLNKetigKFFQA---DIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDL 167
Cdd:COG2227  28 VLDVGCGTGRLALALAR----RGADVtgvDISPEALEIAREraAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDP 103

                        90
                ....*....|....*...
gi 40018642 168 PRALEQIHYILKPDGVFI 185
Cdd:COG2227 104 AALLRELARLLKPGGLLL 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
93-188 7.24e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 66.77  E-value: 7.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  93 ALDLGCGRGYIAQYLNKETIGKFFQA-DIAENALKNSSETeIPTVS-VLAD-EEFLPfkENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFPGARVTGvDLSPEMLARARAR-LPNVRfVVADlRDLDP--PEPFDLVVSNAALHWLPDHAA 81

                        90
                ....*....|....*....
gi 40018642 170 ALEQIHYILKPDGVFIGAM 188
Cdd:COG4106  82 LLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
87-185 1.56e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 68.10  E-value: 1.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  87 PRNFPLALDLGCGRGYIAQYLNK---ETIGkffqADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHW 163
Cdd:COG4976  44 PGPFGRVLDLGCGTGLLGEALRPrgyRLTG----VDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTY 119

                        90       100
                ....*....|....*....|..
gi 40018642 164 VNDLPRALEQIHYILKPDGVFI 185
Cdd:COG4976 120 LGDLAAVFAGVARALKPGGLFI 141
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-235 6.37e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 65.91  E-value: 6.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLNKEtigkFFQADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:pfam13489  27 LDFGCGTGIFLRLLRAQ----GFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPALLRQ 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40018642   174 IHYILKPDGVFIGAMFGGDTLYELRcsLQLAETEREggFSPHISPFTAvNDLGHLLGRAGFN 235
Cdd:pfam13489 103 IAALLKPGGLLLLSTPLASDEADRL--LLEWPYLRP--RNGHISLFSA-RSLKRLLEEAGFE 159
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 93-185 1.17e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 1.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  93 ALDLGCGRGYIAQYLNKETIGKFFQADIAENAL----KNSSETEIPTVSVLAD--EEFLPFKENTFDLVVSSLSLHWVN- 165
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIalarARAAKAGLGNVEFLVAdlAELDPLPAESFDLVVAFGVLHHLPp 109

                        90       100
                ....*....|....*....|.
gi 40018642 166 -DLPRALEQIHYILKPDGVFI 185
Cdd:COG0500 110 eEREALLRELARALKPGGVLL 130
PRK08317 PRK08317
hypothetical protein; Provisional
 93-182 1.77e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 63.42  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   93 ALDLGCGRG----YIAQYLNKEtiGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK08317  23 VLDVGCGPGndarELARRVGPE--GRVVGIDRSEAMLalaKERAAGLGPNVEfVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                         90
                 ....*....|....*...
gi 40018642  165 NDLPRALEQIHYILKPDG 182
Cdd:PRK08317 101 EDPARALAEIARVLRPGG 118
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-184 1.99e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 59.69  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLNKETIGKFFQA-DIAENALKNSSE---------TEIPTVSVLADEEFLPFKentFDLVVSSLSLHW 163
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGlDISPAALEAARErlaalgllnAVRVELFQLDLGELDPGS---FDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 40018642   164 VNDLPRALEQIHYILKPDGVF 184
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 2.94e-10

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 56.67  E-value: 2.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSETEI----PTVSVL-AD-EEFLPFKENTFDLVVSSLSLHW-VND 166
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallaDNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                        90
                ....*....|....*....
gi 40018642 167 LPRALEQIHYILKPDGVFI 185
Cdd:cd02440  83 LARFLEEARRLLKPGGVLV 101
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 88-304 9.90e-10

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 58.23  E-value: 9.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   88 RNFPLALDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDL 167
Cdd:PRK10258  41 RKFTHVLDAGCGPGWMSRYW-RERGSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  168 PRALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQlAETEReggfsPHISPFTAVNDLGHLLGRAGFntlTVDTDEIQVN 247
Cdd:PRK10258 120 STALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQ-AVDER-----PHANRFLPPDAIEQALNGWRY---QHHIQPITLW 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40018642  248 YPGMFELMEDLQGMGESNcawnrkalLH--RDTMLAAAAVYREM---YRNEDGSVPATYQIY 304
Cdd:PRK10258 191 FDDALSAMRSLKGIGATH--------LHegRDPRILTRSQLQRLqlaWPQQQGRYPLTYHLF 244
PRK05785 PRK05785
hypothetical protein; Provisional
 94-184 1.44e-09

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 57.39  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSeteIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:PRK05785  56 LDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMNL---VADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAE 132

                         90       100
                 ....*....|....*....|.
gi 40018642  174 I----HYIL------KPDGVF 184
Cdd:PRK05785 133 FtrvsRKQVgfiamgKPDNVI 153
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 94-233 2.52e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.12  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLNKETI--GKFFQADIAENALK----NSSETEIPTVSV-LADEEFLP--FKENTFDLVVSSLSLHWV 164
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEkareNAQKLGFDNVEFeQGDIEELPelLEDDKFDVVISNCVLNHI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40018642   165 NDLPRALEQIHYILKPDGVFIgaMFGGDTLYELRCSLQLAETEREGGFSPHISPftavNDLGHLLGRAG 233
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGGRLI--ISDPDSLAELPAHVKEDSTYYAGCVGGAILK----KKLYELLEEAG 150
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 93-184 7.05e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.54  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   93 ALDLGCGRGYIAQYLNKE--TIGKFFQADIAENAL-----KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAvgKTGEVVGLDFSEGMLavgreKLRDLGLSGNVEfVQGDAEALPFPDNSFDAVTIAFGLRNV 134

                         90       100
                 ....*....|....*....|
gi 40018642  165 NDLPRALEQIHYILKPDGVF 184
Cdd:PRK00216 135 PDIDKALREMYRVLKPGGRL 154
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 94-184 2.64e-08

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: 53.81  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    94 LDLGCGRGYIAQYLNK--ETIGKFFQADIAENALKNS---SETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLP 168
Cdd:TIGR01934  44 LDVACGTGDLAIELAKsaPDRGKVTGVDFSSEMLEVAkkkSELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQ 123

                          90
                  ....*....|....*.
gi 40018642   169 RALEQIHYILKPDGVF 184
Cdd:TIGR01934 124 KALREMYRVLKPGGRL 139
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
93-219 5.09e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 50.13  E-value: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    93 ALDLGCGRGYIAQYLNK--ETIGKFFQADIAENALKNS-----SETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVN 165
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDsaGSSGKVVGLDINENMLKEGekkakEEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFP 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 40018642   166 DLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLaetereggFSPHISPF 219
Cdd:pfam01209 126 DYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYEL--------YFKYVMPF 171
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 94-185 5.85e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.77  E-value: 5.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  94 LDLGCGRGYIAQYLNKE--------TIGKfFQADIAENALKNSSETEIPTVsVLADEEFLPFkENTFDLVVSSLSLHWVN 165
Cdd:COG2230  56 LDIGCGWGGLALYLARRygvrvtgvTLSP-EQLEYARERAAEAGLADRVEV-RLADYRDLPA-DGQFDAIVSIGMFEHVG 132

                        90       100
                ....*....|....*....|..
gi 40018642 166 D--LPRALEQIHYILKPDGVFI 185
Cdd:COG2230 133 PenYPAYFAKVARLLKPGGRLL 154
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 94-198 4.39e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 47.60  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   94 LDLGCGRGY----IAQYLNKETIGKFFQADIAENALKNSSEtEIPTVSV-LADEEFLPFKENTFDLVVSSLSlhwvndlP 168
Cdd:PRK11088  90 LDIGCGEGYythaLADALPEITTMQLFGLDISKVAIKYAAK-RYPQVTFcVASSHRLPFADQSLDAIIRIYA-------P 161

                         90       100       110
                 ....*....|....*....|....*....|
gi 40018642  169 RALEQIHYILKPDGVFIGAMFGGDTLYELR 198
Cdd:PRK11088 162 CKAEELARVVKPGGIVITVTPGPRHLFELK 191
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 93-203 7.37e-06

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: 45.66  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642    93 ALDLGCGRGYIAQYLNKETIGKFFQADIAENALKnsSETEIPTVSVL--------ADEEFLPFKENTFDLVVS----SLS 160
Cdd:pfam01728  25 VLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLW--KPRNDPGVTFIqgdirdpeTLDLLEELLGRKVDLVLSdgspFIS 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 40018642   161 LHWVNDLPRALE----QIHY---ILKPDGVFIGAMFGGDTLYELRCSLQL 203
Cdd:pfam01728 103 GNKVLDHLRSLDlvkaALEValeLLRKGGNFVCKVFQGEDFSELLYLLKL 152
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 93-157 4.08e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 40.94  E-value: 4.08e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642  93 ALDLGCGRGYIAQYLNKETIGKFFQA-DIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVS 157
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRNPEARVTLvDVNARAVelarANAAANGLENVEVLWSDGLSGVPDGSFDLILS 122
PRK14968 PRK14968
putative methyltransferase; Provisional
 93-156 8.36e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 8.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40018642   93 ALDLGCGRGYIAQYLNKETIgKFFQADI----AENALKNSSETEI--PTVSVLADEEFLPFKENTFDLVV 156
Cdd:PRK14968  27 VLEVGTGSGIVAIVAAKNGK-KVVGVDInpyaVECAKCNAKLNNIrnNGVEVIRSDLFEPFRGDKFDVIL 95
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
116-185 9.65e-03

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 37.20  E-value: 9.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40018642 116 FQADIAENAlKNSSETEIpTVSVLADEEFLPfkENTFDLVVSSLSLH-WVN--DLPRALEQIHYILKPDGVFI 185
Cdd:COG4798 116 FSAKLAADP-ALYGNVRV-TAFAPPDDPIAP--PGSADLVLTFRNYHnWYRagDAAAMFAAFFKALKPGGVLG 184
 
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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