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Conserved domains on  [gi|187607718|ref|NP_001119843|]
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arginine-hydroxylase NDUFAF5, mitochondrial precursor [Rattus norvegicus]

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 ...
 74-310 6.53e-33

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: 122.40  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   74 EIGSRIADR-VYDIARDFPLALDIGCGRGYIAQHLNKE-TVGKIFQTDIAEHALKNSIETDIPTVN-ILADEEFLPFPEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  151 TFDLVVSSLSLHWVNDLPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  231 RAgFNTLTVDTDEIQVNYPGMFELMEDLKGMGESNCS---WNRKALLHrdtMLAAAAVYREMysnedGSIPATYQIYHMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLERYEQEFQP-----DGLPLTYHVVYGI 237


                  ...
gi 187607718  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 6.53e-33

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: 122.40  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   74 EIGSRIADR-VYDIARDFPLALDIGCGRGYIAQHLNKE-TVGKIFQTDIAEHALKNSIETDIPTVN-ILADEEFLPFPEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  151 TFDLVVSSLSLHWVNDLPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  231 RAgFNTLTVDTDEIQVNYPGMFELMEDLKGMGESNCS---WNRKALLHrdtMLAAAAVYREMysnedGSIPATYQIYHMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLERYEQEFQP-----DGLPLTYHVVYGI 237


                  ...
gi 187607718  308 GWK 310
Cdd:TIGR02072 238 AKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 2.86e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 86.56  E-value: 2.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLnKETVGKIFQTDIAEHALKNSIE--TDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 187607718  172 EQIHYVLKPDGVFV 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 3.23e-21

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: 88.13  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGYIAQHLnKETVGKIFQTDIAEHAL----KNSIETDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226   27 LDLGCGTGRLALAL-AERGARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 187607718 170 ALEQIHYVLKPDGVFVGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226  106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 87-305 1.08e-13

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 69.79  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  87 ARDFPLALDIGCGRGYIAQHLnKETVGKIFQTDIAEHALKNSIETDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVND 166
Cdd:PRK10258  40 QRKFTHVLDAGCGPGWMSRYW-RERGSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718 167 LPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSLQlAETEReggfsPHISPFTAVNDLGHLLGRAGFntlTVDTDEIQV 246
Cdd:PRK10258 119 LSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQ-AVDER-----PHANRFLPPDAIEQALNGWRY---QHHIQPITL 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187607718 247 NYPGMFELMEDLKGMGESNcswnrkalLH--RDTMLAAAAVYREM---YSNEDGSIPATYQIYH 305
Cdd:PRK10258 190 WFDDALSAMRSLKGIGATH--------LHegRDPRILTRSQLQRLqlaWPQQQGRYPLTYHLFL 245
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 1.89e-12

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: 62.83  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGYIAQHLNKETVGKIFQTDI----AEHALKNSIETDIPTVNIL-AD-EEFLPFPENTFDLVVSSLSLHW-VND 166
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDIspvaLELARKAAAALLADNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                         90
                 ....*....|....*....
gi 187607718 167 LPRALEQIHYVLKPDGVFV 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 6.53e-33

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: 122.40  E-value: 6.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   74 EIGSRIADR-VYDIARDFPLALDIGCGRGYIAQHLNKE-TVGKIFQTDIAEHALKNSIETDIPTVN-ILADEEFLPFPEN 150
Cdd:TIGR02072  18 EMAKRLLALlKEKGIFIPASVLDIGCGTGYLTRALLKRfPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  151 TFDLVVSSLSLHWVNDLPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSlqlaetereggFSPHISPFTAVNDLGHLLG 230
Cdd:TIGR02072  98 SFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQS-----------FGQHGLRYLSLDELKALLK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  231 RAgFNTLTVDTDEIQVNYPGMFELMEDLKGMGESNCS---WNRKALLHrdtMLAAAAVYREMysnedGSIPATYQIYHMI 307
Cdd:TIGR02072 167 NS-FELLTLEEELITLSFDDPLDVLRHLKKTGANGLSsgrTSRKQLKA---FLERYEQEFQP-----DGLPLTYHVVYGI 237


                  ...
gi 187607718  308 GWK 310
Cdd:TIGR02072 238 AKK 240
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-185 2.86e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 86.56  E-value: 2.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLnKETVGKIFQTDIAEHALKNSIE--TDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPRAL 171
Cdd:pfam08241   1 LDVGCGTGLLTELL-ARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....
gi 187607718  172 EQIHYVLKPDGVFV 185
Cdd:pfam08241  80 REIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 94-213 3.23e-21

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: 88.13  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGYIAQHLnKETVGKIFQTDIAEHAL----KNSIETDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPR 169
Cdd:COG2226   27 LDLGCGTGRLALAL-AERGARVTGVDISPEMLelarERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPER 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 187607718 170 ALEQIHYVLKPDGVFVGAMFGGDTLYELRCSLQLAeteregGFS 213
Cdd:COG2226  106 ALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA------GFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-182 1.22e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.92  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLNKETVGKIFQTDIAEHAL---KNSIETDIPTVN-ILADEEFLPFPENTFDLVVSSLSLHWVN--DL 167
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLeraRERAAEAGLNVEfVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpDL 81

                          90
                  ....*....|....*
gi 187607718  168 PRALEQIHYVLKPDG 182
Cdd:pfam13649  82 EAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 66-185 1.50e-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: 71.97  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  66 MKFDYLKEEIGSRIADRVYDIARDFPLALDIGCGRGYIAQHLNK---ETVGkifqTDIAEHALKNSIETdIPTVNI---L 139
Cdd:COG2227    1 MSDPDARDFWDRRLAALLARLLPAGGRVLDVGCGTGRLALALARrgaDVTG----VDISPEALEIARER-AAELNVdfvQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 187607718 140 ADEEFLPFPENTFDLVVSSLSLHWVNDLPRALEQIHYVLKPDGVFV 185
Cdd:COG2227   76 GDLEDLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLL 121
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 94-235 9.62e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 68.22  E-value: 9.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLNKETVgKIFQTDIAEHALKNSIETDIPTVnilADEEFLPFPENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:pfam13489  27 LDFGCGTGIFLRLLRAQGF-SVTGVDPSPIAIERALLNVRFDQ---FDEQEAAVPAGKFDVIVAREVLEHVPDPPALLRQ 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 187607718  174 IHYVLKPDGVFVGAMFGGDTLYELRcsLQLAETEREggFSPHISPFTAvNDLGHLLGRAGFN 235
Cdd:pfam13489 103 IAALLKPGGLLLLSTPLASDEADRL--LLEWPYLRP--RNGHISLFSA-RSLKRLLEEAGFE 159
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 87-305 1.08e-13

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 69.79  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  87 ARDFPLALDIGCGRGYIAQHLnKETVGKIFQTDIAEHALKNSIETDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVND 166
Cdd:PRK10258  40 QRKFTHVLDAGCGPGWMSRYW-RERGSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718 167 LPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSLQlAETEReggfsPHISPFTAVNDLGHLLGRAGFntlTVDTDEIQV 246
Cdd:PRK10258 119 LSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQ-AVDER-----PHANRFLPPDAIEQALNGWRY---QHHIQPITL 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187607718 247 NYPGMFELMEDLKGMGESNcswnrkalLH--RDTMLAAAAVYREM---YSNEDGSIPATYQIYH 305
Cdd:PRK10258 190 WFDDALSAMRSLKGIGATH--------LHegRDPRILTRSQLQRLqlaWPQQQGRYPLTYHLFL 245
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
93-188 3.65e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.84  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRGYIAQHLNKETVG-KIFQTDIAEHALKNSIETdIPTVN-ILADEEFLPFPEnTFDLVVSSLSLHWVNDLPRA 170
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGaRVTGVDLSPEMLARARAR-LPNVRfVVADLRDLDPPE-PFDLVVSNAALHWLPDHAAL 82

                         90
                 ....*....|....*...
gi 187607718 171 LEQIHYVLKPDGVFVGAM 188
Cdd:COG4106   83 LARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
93-185 6.17e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.18  E-value: 6.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRGYIAQHLNKEtVGKIFQTDI----AEHALKNSIETDIptvnILADEEFLPFPENTFDLVVSSLSLHWVNDLP 168
Cdd:COG4976   50 VLDLGCGTGLLGEALRPR-GYRLTGVDLseemLAKAREKGVYDRL----LVADLADLAEPDGRFDLIVAADVLTYLGDLA 124

                         90
                 ....*....|....*..
gi 187607718 169 RALEQIHYVLKPDGVFV 185
Cdd:COG4976  125 AVFAGVARALKPGGLFI 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 94-184 1.29e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 63.16  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLNKETVG-KIFQTDIAEHALKNSIET-------DIPTVNILADEEFLPFPEnTFDLVVSSLSLHWVN 165
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERlaalgllNAVRVELFQLDLGELDPG-SFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 187607718  166 DLPRALEQIHYVLKPDGVF 184
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-185 1.89e-12

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: 62.83  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGYIAQHLNKETVGKIFQTDI----AEHALKNSIETDIPTVNIL-AD-EEFLPFPENTFDLVVSSLSLHW-VND 166
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDIspvaLELARKAAAALLADNVEVLkGDaEELPPEADESFDVIISDPPLHHlVED 82

                         90
                 ....*....|....*....
gi 187607718 167 LPRALEQIHYVLKPDGVFV 185
Cdd:cd02440   83 LARFLEEARRLLKPGGVLV 101
PRK08317 PRK08317
hypothetical protein; Provisional
 93-182 7.71e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 64.19  E-value: 7.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRG----YIAQHLNKEtvGKIFQTDIAEHAL---KNSIETDIPTV-NILADEEFLPFPENTFDLVVSSLSLHWV 164
Cdd:PRK08317  23 VLDVGCGPGndarELARRVGPE--GRVVGIDRSEAMLalaKERAAGLGPNVeFVRGDADGLPFPDGSFDAVRSDRVLQHL 100

                         90
                 ....*....|....*...
gi 187607718 165 NDLPRALEQIHYVLKPDG 182
Cdd:PRK08317 101 EDPARALAEIARVLRPGG 118
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 93-185 8.55e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.40  E-value: 8.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRGYIAQHLNKETVGKIFQTDIAEHAL----KNSIETDIPTVN-ILAD-EEFLPFPENTFDLVVSSLSLHWVN- 165
Cdd:COG0500   30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIalarARAAKAGLGNVEfLVADlAELDPLPAESFDLVVAFGVLHHLPp 109

                         90       100
                 ....*....|....*....|.
gi 187607718 166 -DLPRALEQIHYVLKPDGVFV 185
Cdd:COG0500  110 eEREALLRELARALKPGGVLL 130
PRK05785 PRK05785
hypothetical protein; Provisional
 94-185 2.15e-11

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 62.78  E-value: 2.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGYIAQHLNKETVGKIFQTDIAEHALKNSIETDiptVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPRALEQ 173
Cdd:PRK05785  56 LDVAAGKGELSYHFKKVFKYYVVALDYAENMLKMNLVAD---DKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAE 132

                         90       100
                 ....*....|....*....|..
gi 187607718 174 IHYVL----------KPDGVFV 185
Cdd:PRK05785 133 FTRVSrkqvgfiamgKPDNVIK 154
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 93-185 2.04e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 60.17  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRGYIAQHLNKEtVGKIFQ---TDI--------AEHALKNSIETDIPTVniLADEEFLPFPENTFDLVVSSLSL 161
Cdd:PRK00216  55 VLDLACGTGDLAIALAKA-VGKTGEvvgLDFsegmlavgREKLRDLGLSGNVEFV--QGDAEALPFPDNSFDAVTIAFGL 131

                         90       100
                 ....*....|....*....|....
gi 187607718 162 HWVNDLPRALEQIHYVLKPDGVFV 185
Cdd:PRK00216 132 RNVPDIDKALREMYRVLKPGGRLV 155
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 94-185 9.10e-10

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: 58.04  E-value: 9.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLNK--ETVGKIFQTDIAEHALKNSIETDIPTVNI---LADEEFLPFPENTFDLVVSSLSLHWVNDLP 168
Cdd:TIGR01934  44 LDVACGTGDLAIELAKsaPDRGKVTGVDFSSEMLEVAKKKSELPLNIefiQADAEALPFEDNSFDAVTIAFGLRNVTDIQ 123

                          90
                  ....*....|....*..
gi 187607718  169 RALEQIHYVLKPDGVFV 185
Cdd:TIGR01934 124 KALREMYRVLKPGGRLV 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 94-185 3.16e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.32  E-value: 3.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRG----YIAQHLNKETVG--------KIFQTDIAEHALKNSIETdiptvnILADEEFLPFPEnTFDLVVSSLSL 161
Cdd:COG2230   56 LDIGCGWGglalYLARRYGVRVTGvtlspeqlEYARERAAEAGLADRVEV------RLADYRDLPADG-QFDAIVSIGMF 128

                         90       100
                 ....*....|....*....|....*.
gi 187607718 162 HWVND--LPRALEQIHYVLKPDGVFV 185
Cdd:COG2230  129 EHVGPenYPAYFAKVARLLKPGGRLL 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 94-233 1.01e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 53.57  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   94 LDIGCGRGYIAQHLNKE--TVGKIFQTDIAEHALKNSIE--TDIPTVNI---LADEEFLP--FPENTFDLVVSSLSLHWV 164
Cdd:pfam13847   8 LDLGCGTGHLSFELAEElgPNAEVVGIDISEEAIEKAREnaQKLGFDNVefeQGDIEELPelLEDDKFDVVISNCVLNHI 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187607718  165 NDLPRALEQIHYVLKPDGVFVgaMFGGDTLYELRCSLQLAETEREGGFSPHISPftavNDLGHLLGRAG 233
Cdd:pfam13847  88 PDPDKVLQEILRVLKPGGRLI--ISDPDSLAELPAHVKEDSTYYAGCVGGAILK----KKLYELLEEAG 150
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
93-261 3.75e-08

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 53.21  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   93 ALDIGCGRGYIAQHLNK--ETVGKIFQTDIAEHALKNSIE--TDIPTVNI---LADEEFLPFPENTFDLVVSSLSLHWVN 165
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDsaGSSGKVVGLDINENMLKEGEKkaKEEGKYNIeflQGNAEELPFEDDSFDIVTISFGLRNFP 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  166 DLPRALEQIHYVLKPDGVFVGAMFGGDTLYELRCSLQLaetereggFSPHISPFtavndLGHLLGRagfntltvDTDEIQ 245
Cdd:pfam01209 126 DYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAYEL--------YFKYVMPF-----MGKMFAK--------SYKSYQ 184

                         170
                  ....*....|....*...
gi 187607718  246 --VNYPGMFELMEDLKGM 261
Cdd:pfam01209 185 ylQESIRDFPDQKTLASM 202
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 93-203 9.72e-08

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: 51.44  E-value: 9.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   93 ALDIGCGRGYIAQHLNKETVGKIFQTDIAEHALKNSIETDIPTV---NILADE---EFLPFPENTFDLVVS----SLSLH 162
Cdd:pfam01728  25 VLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQLWKPRNDPGVTFiqgDIRDPEtldLLEELLGRKVDLVLSdgspFISGN 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 187607718  163 WVNDLPRALE----QIHY---VLKPDGVFVGAMFGGDTLYELRCSLQL 203
Cdd:pfam01728 105 KVLDHLRSLDlvkaALEValeLLRKGGNFVCKVFQGEDFSELLYLLKL 152
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 94-198 1.48e-06

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 48.75  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGY----IAQHLNKETVGKIFQTDIAEHALKNSIETdIPTVNI-LADEEFLPFPENTFDLVVSSLSlhwvndlP 168
Cdd:PRK11088  90 LDIGCGEGYythaLADALPEITTMQLFGLDISKVAIKYAAKR-YPQVTFcVASSHRLPFADQSLDAIIRIYA-------P 161

                         90       100       110
                 ....*....|....*....|....*....|
gi 187607718 169 RALEQIHYVLKPDGVFVGAMFGGDTLYELR 198
Cdd:PRK11088 162 CKAEELARVVKPGGIVITVTPGPRHLFELK 191
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 93-157 5.65e-05

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: 43.25  E-value: 5.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  93 ALDIGCGRGYIAQHLNKET-VGKIFQTDIAEHAL----KNSIETDIPTVNILADEEFLPFPENTFDLVVS 157
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNpEARVTLVDVNARAVelarANAAANGLENVEVLWSDGLSGVPDGSFDLILS 122
PRK14968 PRK14968
putative methyltransferase; Provisional
 81-156 5.87e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 40.27  E-value: 5.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  81 DRVYDIARD-FPLA-----------LDIGCGRGYIAQHLNKETVgKIFQTDIAEHA----LKNSIETDI--PTVNILADE 142
Cdd:PRK14968   3 DEVYEPAEDsFLLAenavdkkgdrvLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAvecaKCNAKLNNIrnNGVEVIRSD 81

                         90
                 ....*....|....
gi 187607718 143 EFLPFPENTFDLVV 156
Cdd:PRK14968  82 LFEPFRGDKFDVIL 95
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
148-185 1.10e-03

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 40.29  E-value: 1.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 187607718 148 PENTFDLVVSSLSLH-WVN--DLPRALEQIHYVLKPDGVFV 185
Cdd:COG4798  144 PPGSADLVLTFRNYHnWYRagDAAAMFAAFFKALKPGGVLG 184
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 94-234 2.48e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.35  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRG----YIAQHLNKETVGKIFQTDIAEHALKNSIETDIPTVNILADEEFLPFPENTFDLVVSSLSLHWVNDLPR 169
Cdd:PLN02336 271 LDVGCGIGggdfYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPA 350

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187607718 170 ALEQIHYVLKPdgvfvgamfGGDTLYELRC------SLQLAETEREGGFSPHispftAVNDLGHLLGRAGF 234
Cdd:PLN02336 351 LFRSFFKWLKP---------GGKVLISDYCrspgtpSPEFAEYIKQRGYDLH-----DVQAYGQMLKDAGF 407
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 94-183 2.76e-03

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 39.10  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  94 LDIGCGRGY----IAQHLNKETVGKIfqtDIAEHALKNSIETD-IPTVNIL-ADEEFLPFPENTFDLVVSSLSLHWVNDL 167
Cdd:PLN02490 118 VDVGGGTGFttlgIVKHVDAKNVTIL---DQSPHQLAKAKQKEpLKECKIIeGDAEDLPFPTDYADRYVSAGSIEYWPDP 194

                         90
                 ....*....|....*.
gi 187607718 168 PRALEQIHYVLKPDGV 183
Cdd:PLN02490 195 QRGIKEAYRVLKIGGK 210
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 61-197 6.73e-03

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 37.80  E-value: 6.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718   61 RQPEPMKF-----DYLKEEIGSRIADRVYDIARDFpLALDIGCGRGyiaQHLNKETVGKIFQ---TDIAEHALK------ 126
Cdd:pfam03291  31 RQASPIIYlrnfnNWIKSLLISLYASKTFQNSNKR-KVLDLGCGKG---GDLEKWFKGGISQligTDIAEVSIEqcrery 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187607718  127 -------NSIETDIPTVNILAD------EEFLPFPENTFDLVVSSLSLHWvndlprALEQIHYV----------LKPDGV 183
Cdd:pfam03291 107 nklrsgnKSKYYKFDAEFITGDcfvsslREVFEDPFGKFDIVSCQFAIHY------SFESEEKArtmlrnvaelLASGGV 180

                         170
                  ....*....|....
gi 187607718  184 FVGAMFGGDTLYEL 197
Cdd:pfam03291 181 FIGTTPDSDFISAL 194
 
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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