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Conserved domains on  [gi|1206271458|ref|NP_001339337|]
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arginine-hydroxylase NDUFAF5, mitochondrial isoform 3 [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

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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 ...
 74-229 4.36e-24

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: 96.59  E-value: 4.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271458 151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLL 229
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALL 165
 
Name Accession Description Interval E-value
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-229 4.36e-24

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: 96.59  E-value: 4.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271458 151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLL 229
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALL 165
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 2.13e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 82.71  E-value: 2.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 1206271458 172 EQIHYILKPDGVFI 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 7.72e-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: 82.73  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETiGKFFQADIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226    27 LDLGCGTGRLALALAERG-ARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1206271458 170 ALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226   106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
PRK08317 PRK08317
hypothetical protein; Provisional
 93-182 1.47e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 62.26  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRG----YIAQYLNKEtiGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK08317   23 VLDVGCGPGndarELARRVGPE--GRVVGIDRSEAMLalaKERAAGLGPNVEfVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                          90
                  ....*....|....*...
gi 1206271458 165 NDLPRALEQIHYILKPDG 182
Cdd:PRK08317  101 EDPARALAEIARVLRPGG 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 9.64e-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: 54.36  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSETEI----PTVSVL-AD-EEFLPFKENTFDLVVSSLSLHW-VND 166
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallaDNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                          90
                  ....*....|....*....
gi 1206271458 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 ...
 74-229 4.36e-24

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: 96.59  E-value: 4.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  74 EVGSRIADR-VYDIPRNFPLALDLGCGRGYIAQYLNKE-TIGKFFQADIAENALKNSSETEIPTVS-VLADEEFLPFKEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271458 151 TFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLL 229
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALL 165
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 2.13e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 82.71  E-value: 2.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 1206271458 172 EQIHYILKPDGVFI 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 7.72e-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: 82.73  E-value: 7.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETiGKFFQADIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226    27 LDLGCGTGRLALALAERG-ARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1206271458 170 ALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226   106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-182 3.23e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.53  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWVN--DL 167
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLeraRERAAEAGLNVEfVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpDL 81

                          90
                  ....*....|....*
gi 1206271458 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 7.50e-15

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: 68.89  E-value: 7.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKetigKFFQA---DIAENALKNSSE--TEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDL 167
Cdd:COG2227    28 VLDVGCGTGRLALALAR----RGADVtgvDISPEALEIAREraAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDP 103

                          90
                  ....*....|....*...
gi 1206271458 168 PRALEQIHYILKPDGVFI 185
Cdd:COG2227   104 AALLRELARLLKPGGLLL 121
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
87-185 7.74e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 67.72  E-value: 7.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  87 PRNFPLALDLGCGRGYIAQYLNK---ETIGkffqADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHW 163
Cdd:COG4976    44 PGPFGRVLDLGCGTGLLGEALRPrgyRLTG----VDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTY 119

                          90       100
                  ....*....|....*....|..
gi 1206271458 164 VNDLPRALEQIHYILKPDGVFI 185
Cdd:COG4976   120 LGDLAAVFAGVARALKPGGLFI 141
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
93-188 9.46e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 65.23  E-value: 9.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKETIGKFFQA-DIAENALKNSSETeIPTVS-VLAD-EEFLPfkENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGvDLSPEMLARARAR-LPNVRfVVADlRDLDP--PEPFDLVVSNAALHWLPDHAA 81

                          90
                  ....*....|....*....
gi 1206271458 170 ALEQIHYILKPDGVFIGAM 188
Cdd:COG4106    82 LLARLAAALAPGGVLAVQV 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-235 3.96e-13

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 65.14  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKEtigkFFQADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:pfam13489  27 LDFGCGTGIFLRLLRAQ----GFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPPALLRQ 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1206271458 174 IHYILKPDGVFIGAMFGGDTLYELRcsLQLAETEREggFSPHISPFTAvNDLGHLLGRAGFN 235
Cdd:pfam13489 103 IAALLKPGGLLLLSTPLASDEADRL--LLEWPYLRP--RNGHISLFSA-RSLKRLLEEAGFE 159
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 93-185 1.42e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.86  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKETIGKFFQADIAENAL----KNSSETEIPTVSVLAD--EEFLPFKENTFDLVVSSLSLHWVN- 165
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIalarARAAKAGLGNVEFLVAdlAELDPLPAESFDLVVAFGVLHHLPp 109

                          90       100
                  ....*....|....*....|.
gi 1206271458 166 -DLPRALEQIHYILKPDGVFI 185
Cdd:COG0500   110 eEREALLRELARALKPGGVLL 130
PRK08317 PRK08317
hypothetical protein; Provisional
 93-182 1.47e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 62.26  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRG----YIAQYLNKEtiGKFFQADIAENAL---KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK08317   23 VLDVGCGPGndarELARRVGPE--GRVVGIDRSEAMLalaKERAAGLGPNVEfVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                          90
                  ....*....|....*...
gi 1206271458 165 NDLPRALEQIHYILKPDG 182
Cdd:PRK08317  101 EDPARALAEIARVLRPGG 118
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-184 6.40e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 57.38  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETIGKFFQA-DIAENALKNSSE---------TEIPTVSVLADEEFLPFKentFDLVVSSLSLHW 163
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGlDISPAALEAARErlaalgllnAVRVELFQLDLGELDPGS---FDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 1206271458 164 VNDLPRALEQIHYILKPDGVF 184
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
PRK05785 PRK05785
hypothetical protein; Provisional
 94-184 4.93e-10

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 57.78  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSeteIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:PRK05785   56 LDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMNL---VADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAE 132

                          90       100
                  ....*....|....*....|.
gi 1206271458 174 I----HYIL------KPDGVF 184
Cdd:PRK05785  133 FtrvsRKQVgfiamgKPDNVI 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 9.64e-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: 54.36  E-value: 9.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSETEI----PTVSVL-AD-EEFLPFKENTFDLVVSSLSLHW-VND 166
Cdd:cd02440     3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAallaDNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                          90
                  ....*....|....*....
gi 1206271458 167 LPRALEQIHYILKPDGVFI 185
Cdd:cd02440    83 LARFLEEARRLLKPGGVLV 101
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: 54.35  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKETI--GKFFQADIAENALK----NSSETEIPTVSV-LADEEFLP--FKENTFDLVVSSLSLHWV 164
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEkareNAQKLGFDNVEFeQGDIEELPelLEDDKFDVVISNCVLNHI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1206271458 165 NDLPRALEQIHYILKPDGVFIgaMFGGDTLYELRCSLQLAETEREGGFSPHISPftavNDLGHLLGRAG 233
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGGRLI--ISDPDSLAELPAHVKEDSTYYAGCVGGAILK----KKLYELLEEAG 150
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 93-184 3.13e-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: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKE--TIGKFFQADIAENAL-----KNSSETEIPTVS-VLADEEFLPFKENTFDLVVSSLSLHWV 164
Cdd:PRK00216   55 VLDLACGTGDLAIALAKAvgKTGEVVGLDFSEGMLavgreKLRDLGLSGNVEfVQGDAEALPFPDNSFDAVTIAFGLRNV 134

                          90       100
                  ....*....|....*....|
gi 1206271458 165 NDLPRALEQIHYILKPDGVF 184
Cdd:PRK00216  135 PDIDKALREMYRVLKPGGRL 154
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 94-184 1.31e-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: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNK--ETIGKFFQADIAENALKNS---SETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLP 168
Cdd:TIGR01934  44 LDVACGTGDLAIELAKsaPDRGKVTGVDFSSEMLEVAkkkSELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQ 123

                          90
                  ....*....|....*.
gi 1206271458 169 RALEQIHYILKPDGVF 184
Cdd:TIGR01934 124 KALREMYRVLKPGGRL 139
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 88-229 1.70e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 53.61  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  88 RNFPLALDLGCGRGYIAQYLnKETIGKFFQADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDL 167
Cdd:PRK10258   41 RKFTHVLDAGCGPGWMSRYW-RERGSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNL 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1206271458 168 PRALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQlAETEReggfsPHISPFTAVNDLGHLL 229
Cdd:PRK10258  120 STALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQ-AVDER-----PHANRFLPPDAIEQAL 175
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
93-219 1.91e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 50.52  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNK--ETIGKFFQADIAENALKNS-----SETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVN 165
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDsaGSSGKVVGLDINENMLKEGekkakEEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFP 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1206271458 166 DLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLaetereggFSPHISPF 219
Cdd:pfam01209 126 DYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYEL--------YFKYVMPF 171
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 94-185 3.56e-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: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGYIAQYLNKE--------TIGKfFQADIAENALKNSSETEIPTVsVLADEEFLPFkENTFDLVVSSLSLHWVN 165
Cdd:COG2230    56 LDIGCGWGGLALYLARRygvrvtgvTLSP-EQLEYARERAAEAGLADRVEV-RLADYRDLPA-DGQFDAIVSIGMFEHVG 132

                          90       100
                  ....*....|....*....|..
gi 1206271458 166 D--LPRALEQIHYILKPDGVFI 185
Cdd:COG2230   133 PenYPAYFAKVARLLKPGGRLL 154
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 94-198 1.85e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 47.60  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  94 LDLGCGRGY----IAQYLNKETIGKFFQADIAENALKNSSEtEIPTVSV-LADEEFLPFKENTFDLVVSSLSlhwvndlP 168
Cdd:PRK11088   90 LDIGCGEGYythaLADALPEITTMQLFGLDISKVAIKYAAK-RYPQVTFcVASSHRLPFADQSLDAIIRIYA-------P 161

                          90       100       110
                  ....*....|....*....|....*....|
gi 1206271458 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 8.87e-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: 44.89  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKETIGKFFQADIAENALKnsSETEIPTVSVL--------ADEEFLPFKENTFDLVVS----SLS 160
Cdd:pfam01728  25 VLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLW--KPRNDPGVTFIqgdirdpeTLDLLEELLGRKVDLVLSdgspFIS 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1206271458 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 5.00e-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: 39.79  E-value: 5.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKETIGKFFQA-DIAENAL----KNSSETEIPTVSVLADEEFLPFKENTFDLVVS 157
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLvDVNARAVelarANAAANGLENVEVLWSDGLSGVPDGSFDLILS 122
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
116-185 6.23e-03

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 37.20  E-value: 6.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1206271458 116 FQADIAENAlKNSSETEIpTVSVLADEEFLPfkENTFDLVVSSLSLH-WVN--DLPRALEQIHYILKPDGVFI 185
Cdd:COG4798   116 FSAKLAADP-ALYGNVRV-TAFAPPDDPIAP--PGSADLVLTFRNYHnWYRagDAAAMFAAFFKALKPGGVLG 184
PRK14968 PRK14968
putative methyltransferase; Provisional
 93-156 9.56e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.03  E-value: 9.56e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1206271458  93 ALDLGCGRGYIAQYLNKETIgKFFQADI----AENALKNSSETEI--PTVSVLADEEFLPFKENTFDLVV 156
Cdd:PRK14968   27 VLEVGTGSGIVAIVAAKNGK-KVVGVDInpyaVECAKCNAKLNNIrnNGVEVIRSDLFEPFRGDKFDVIL 95
 
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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