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Conserved domains on  [gi|6435572|pdb|1D2H|A]
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Chain A, Crystal Structure Of R175k Mutant Glycine N-methyltransferase Complexed With S-adenosylhomocysteine

Protein Classification

class I SAM-dependent methyltransferase (domain architecture ID 10614797)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor, such as Burkholderia thailandensis 1,6-didemethyltoxoflavin-N1-methyltransferase and 16S rRNA (adenine(1408)-N(1))-methyltransferase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
60-168 9.81e-16

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


:

Pssm-ID: 338872 [Multi-domain]  Cd Length: 97  Bit Score: 71.07  E-value: 9.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLALALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVVGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
1D2H_A        138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
60-168 9.81e-16

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


Pssm-ID: 338872 [Multi-domain]  Cd Length: 97  Bit Score: 71.07  E-value: 9.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLALALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVVGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
1D2H_A        138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
29-172 1.11e-12

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];


Pssm-ID: 225137 [Multi-domain]  Cd Length: 243  Bit Score: 66.20  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227  43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_A      109 kwvieeaNWLTLD------KDVPAGDG-FDAVICLgNSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 104 -------SGVNIDyrqatvEDLASAGGqFDVVTCM-EVLEHVPDP-------ESFLRACAKLVKPGGILFL 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
59-172 2.19e-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: 62.06  E-value: 2.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
                        90       100       110
                ....*....|....*....|....*....|....*
1D2H_A      138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
20-165 2.24e-09

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 56.35  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         20 QYADGEAARVWQLYIGDT-------------RSRTAEYKAWLLGLLRQHGcHRVLDVACGTGVDSIMLVEEGFSVTSVDA 86
Cdd:TIGR02021   7 HYFDGTAFQRWARIYGSGdpvsrvrqtvregRAAMRRKLLDWLPKDPLKG-KRVLDAGCGTGLLSIELAKRGAIVKAVDI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         87 SDKMLKYAlkerwNRRKEPAFDKWVIE-EANwltldkDVPAGDG-FDAVICLgNSFAHLPDSKGDQsehrlALKNIASMV 164
Cdd:TIGR02021  86 SEQMVQMA-----RNRAQGRDVAGNVEfEVN------DLLSLCGeFDIVVCM-DVLIHYPASDMAK-----ALGHLASLT 148

                  .
1D2H_A        165 R 165
Cdd:TIGR02021 149 K 149
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
21-165 7.14e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_A       100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
60-168 9.81e-16

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


Pssm-ID: 338872 [Multi-domain]  Cd Length: 97  Bit Score: 71.07  E-value: 9.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLALALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVVGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
1D2H_A        138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
61-172 6.51e-13

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


Pssm-ID: 336971 [Multi-domain]  Cd Length: 95  Bit Score: 63.07  E-value: 6.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         61 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerWNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 139
Cdd:pfam08241   1 LDVGCGTGLLAELLARLGARVTGVDISPEMLELA----REKAPRAGLVEFVVGDAE------DLPFPDNsFDLVLSS-EV 69
                          90       100       110
                  ....*....|....*....|....*....|...
1D2H_A        140 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam08241  70 LHHVED-------PERALREIARVLKPGGILII 95
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
29-172 1.11e-12

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];


Pssm-ID: 225137 [Multi-domain]  Cd Length: 243  Bit Score: 66.20  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227  43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_A      109 kwvieeaNWLTLD------KDVPAGDG-FDAVICLgNSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVI 172
Cdd:COG2227 104 -------SGVNIDyrqatvEDLASAGGqFDVVTCM-EVLEHVPDP-------ESFLRACAKLVKPGGILFL 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
59-172 2.19e-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: 62.06  E-value: 2.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
                        90       100       110
                ....*....|....*....|....*....|....*
1D2H_A      138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
59-174 1.20e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 316372 [Multi-domain]  Cd Length: 150  Bit Score: 61.29  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         59 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 135
Cdd:pfam13847   6 RVLDLGCGTGYLTFELAEELGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDSFDVIIS 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
1D2H_A        136 LGnSFAHLPDSKgdqsehrLALKNIASMVRPGGLLVIDH 174
Cdd:pfam13847  81 NC-VLNLIADPD-------KVLEEILRVLKPGGRLLISD 111
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
61-170 3.20e-11

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


Pssm-ID: 311936 [Multi-domain]  Cd Length: 98  Bit Score: 58.54  E-value: 3.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         61 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 138
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFVLDLIELDPGSFDVVVAS-N 73
                          90       100       110
                  ....*....|....*....|....*....|..
1D2H_A        139 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 170
Cdd:pfam08242  74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
20-165 2.24e-09

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 56.35  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         20 QYADGEAARVWQLYIGDT-------------RSRTAEYKAWLLGLLRQHGcHRVLDVACGTGVDSIMLVEEGFSVTSVDA 86
Cdd:TIGR02021   7 HYFDGTAFQRWARIYGSGdpvsrvrqtvregRAAMRRKLLDWLPKDPLKG-KRVLDAGCGTGLLSIELAKRGAIVKAVDI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         87 SDKMLKYAlkerwNRRKEPAFDKWVIE-EANwltldkDVPAGDG-FDAVICLgNSFAHLPDSKGDQsehrlALKNIASMV 164
Cdd:TIGR02021  86 SEQMVQMA-----RNRAQGRDVAGNVEfEVN------DLLSLCGeFDIVVCM-DVLIHYPASDMAK-----ALGHLASLT 148

                  .
1D2H_A        165 R 165
Cdd:TIGR02021 149 K 149
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
21-165 7.14e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 7.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_A       100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
PRK08317 PRK08317
hypothetical protein; Provisional
42-178 7.19e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.94  E-value: 7.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        42 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 118
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_A       119 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHKNYD 178
Cdd:PRK08317  82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
59-172 7.63e-09

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


Pssm-ID: 338771 [Multi-domain]  Cd Length: 162  Bit Score: 53.57  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLkyalkerwNRRKEPAFDKWVIEEANWltldkdvPAGDGFDAVICLgN 138
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRPQGFSVTGVDPSPIAI--------ERALPNVRFDQFDEEDEA-------KPQGKYDVIVAR-E 88
                          90       100       110
                  ....*....|....*....|....*....|....
1D2H_A        139 SFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam13489  89 VLEHVKD-------PPALLRQIAALLKPGGLLLL 115
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
33-172 8.92e-09

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910 [Multi-domain]  Cd Length: 224  Bit Score: 54.61  E-value: 8.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         33 YIGDTRSRTaeYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnrRKEPAFDKWVI 112
Cdd:TIGR01983  32 YIRDRIRKN--FKNPLDGL-------RVLDVGCGGGLLSEPLARLGANVTGIDASEENIEVA-------KLHAKKDPLQI 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
1D2H_A        113 E-EANwlTLDKDVPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVI 172
Cdd:TIGR01983  96 DyRCT--TVEDLAEKKAGsFDVVTCM-EVLEHVPDPQA-------FIRACAQLLKPGGILFF 147
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
33-194 4.38e-08

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


Pssm-ID: 223574 [Multi-domain]  Cd Length: 257  Bit Score: 52.98  E-value: 4.38e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       33 YIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIM--LVEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKW 110
Cdd:COG0500  25 AFLLLAEELLDLLLVLRLLRLLPGGLGVLDIGCGTGRLALLarLGGRGAYVVGVDLSPEMLALARA----RAEGAGLGLV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A      111 VIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSkgdqsehrlALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGK 190
Cdd:COG0500 101 DFVVADALGGVLPFEDSASFDLVISLLVLHLLPPAK---------ALRELLRVLKPGGRLVLSDLLRDGLLEGRLAALLG 171

                ....
1D2H_A      191 NIYY 194
Cdd:COG0500 172 FGDP 175
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];
59-172 4.88e-08

Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];


Pssm-ID: 225136 [Multi-domain]  Cd Length: 238  Bit Score: 52.27  E-value: 4.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       59 RVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLD-KDvpagDGFDAVIC 135
Cdd:COG2226  54 KVLDVACGTGDMALLLAKSVgtGEVVGLDISESMLEVARE----KLKKKGVQNVEFVVGDAENLPfPD----NSFDAVTI 125
                        90       100       110
                ....*....|....*....|....*....|....*..
1D2H_A      136 lGNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2226 126 -SFGLRNVTD-------IDKALKEMYRVLKPGGRLLV 154
ubiE PRK00216
ubiquinone/menaquinone biosynthesis methyltransferase; Reviewed
58-172 3.05e-07

ubiquinone/menaquinone biosynthesis methyltransferase; Reviewed


Pssm-ID: 234689  Cd Length: 239  Bit Score: 50.15  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        58 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 133
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
1D2H_A       134 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
46-173 9.05e-07

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 48.75  E-value: 9.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         46 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLK--YALKE----RWNRRKE----PAFDKwVIEEA 115
Cdd:TIGR04345  31 ELALAQFRNKSRKRALDIGCAVGRASFELARYFDEVDGIDFSARFIRpaVALKErgslRYALKEEgelvSFKEV-TLSDL 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1D2H_A        116 NWLTLDKDV-----------PAGDGFDAVIClGNSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVID 173
Cdd:TIGR04345 110 GLDEVRDRVsffqgdacnlkPHFTGYDLILA-ANLLDRLYDP-------AAFLSSIHERLNPGGLLVIA 170
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
58-172 4.75e-06

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  Cd Length: 223  Bit Score: 46.49  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
1D2H_A        134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
PRK05134 PRK05134
bifunctional 3-demethylubiquinone-9 3-methyltransferase/ 2-octaprenyl-6-hydroxy phenol ...
49-172 6.08e-05

bifunctional 3-demethylubiquinone-9 3-methyltransferase/ 2-octaprenyl-6-hydroxy phenol methylase; Provisional


Pssm-ID: 235350 [Multi-domain]  Cd Length: 233  Bit Score: 43.22  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        49 LGLLRQHGCH----RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLK----YALKE--RWNRRKEPAfdkwviEEanwl 118
Cdd:PRK05134  37 LNYIREHAGGlfgkRVLDVGCGGGILSESMARLGADVTGIDASEENIEvarlHALESglKIDYRQTTA------EE---- 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
1D2H_A       119 tLDKDVPAgdGFDAVICLgNSFAHLPDSKgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:PRK05134 107 -LAAEHPG--QFDVVTCM-EMLEHVPDPA-------SFVRACAKLVKPGGLVFF 149
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
59-176 7.03e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.49  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 136
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
1D2H_A       137 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHKN 176
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
60-149 9.08e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.84  E-value: 9.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        60 VLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkERwnRRKEPAFDKWVIEEANWLTLDKDVPAGDgFDAVICLgNS 139
Cdd:PLN02585 148 VCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEA--ER--RAKEALAALPPEVLPKFEANDLESLSGK-YDTVTCL-DV 221
                         90
                 ....*....|
1D2H_A       140 FAHLPDSKGD 149
Cdd:PLN02585 222 LIHYPQDKAD 231
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
48-106 9.35e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340  Cd Length: 251  Bit Score: 39.74  E-value: 9.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
1D2H_A        48 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 106
Cdd:PRK10258  34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
MenG_heptapren TIGR02752
demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that ...
59-171 1.42e-03

demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131799  Cd Length: 231  Bit Score: 39.02  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         59 RVLDVACGTGVDSIMLVE----EGfSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDvpaGDGFDAVI 134
Cdd:TIGR02752  48 SALDVCCGTADWSIALAEavgpEG-HVIGLDFSENMLSVGRQ----KVKDAGLHNVELVHGNAMELPFD---DNSFDYVT 119
                          90       100       110
                  ....*....|....*....|....*....|....*..
1D2H_A        135 cLGNSFAHLPDskgdqseHRLALKNIASMVRPGGLLV 171
Cdd:TIGR02752 120 -IGFGLRNVPD-------YMQVLREMYRVVKPGGKVV 148
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
35-172 1.43e-03

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


Pssm-ID: 225139 [Multi-domain]  Cd Length: 283  Bit Score: 39.15  E-value: 1.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       35 GDTRSRTAEYKAW--LLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYALKErwnRRKEPAFDKWV 111
Cdd:COG2230  49 PDMTLEEAQRAKLdlILEKLGLKPGMTLLDIGCGWGGLAIYAAEEyGVTVVGVTLSEEQLAYAEKR---IAARGLEDNVE 125
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_A      112 IEEANWLTLDKDvpagdgFDAVICLGnSFAHLpdskGDQSEHRLaLKNIASMVRPGGLLVI 172
Cdd:COG2230 126 VRLQDYRDFEEP------FDRIVSVG-MFEHV----GKENYDDF-FKKVYALLKPGGRMLL 174
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
43-173 4.96e-03

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 36.15  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         43 EYKAWLLGLLRQHGCHRVLDVACGTGVDSI--MLVEEGFSVTSVDASDKMLKyaLKERwNRRKEPAFDKWVIEEANWLTL 120
Cdd:TIGR02469   6 EVRALTLAKLRLRPGDVLWDIGAGTGSVTIeaARLVPNGRVYAIERNPEALD--LIER-NLRRFGVSNIVIVEGDAPEAP 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
1D2H_A        121 DKDVPAgdgFDAvICLGNSFAHLpdskgdqseHRLaLKNIASMVRPGGLLVID 173
Cdd:TIGR02469  83 EALLPD---PDA-VFVGGSGGLL---------QEI-LEAVERRLRPGGRIVLN 121
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
47-174 5.09e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467  Cd Length: 275  Bit Score: 37.45  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A        47 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 124
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       125 PAGDgFDAVIClgN----SFAHLPDSKGDQSEH--RLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:PRK09328 172 PGGR-FDLIVS--NppyiPEADIHLLQPEVRDHepHLALfggedgldfyrriiEQAPRYLKPGGWLLLEI 238
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
47-174 5.94e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 225443 [Multi-domain]  Cd Length: 280  Bit Score: 37.32  E-value: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A       47 WLLGLLRQHGCHrVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkeRWNRRKEpAFDKWVIEEANWLTldkdv 124
Cdd:COG2890 102 AALALLLQLDKR-ILDLGTGSGAIAIALAKEGpdAEVIAVDISPDALALA---RENAERN-GLVRVLVVQSDLFE----- 171
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1D2H_A      125 PAGDGFDAVIC----LGNSFAHLPDSKGDqSEHRLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:COG2890 172 PLRGKFDLIVSnppyIPAEDPELLPEVVR-YEPLLALvgggdglevyrrilGEAPDILKPGGVLILEI 238
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
48-171 9.12e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 36.50  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_A         48 LLGLLRQHGCH---RVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEAnwltlDK 122
Cdd:TIGR02072  23 LLALLKEKGIFipaSVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQA------KTKLSENVQFICGDA-----EK 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
1D2H_A        123 DVPAGDGFDAVIClgNS---FAHLPDSkgdqsehrlALKNIASMVRPGGLLV 171
Cdd:TIGR02072  92 LPLEDSSFDLIVS--NLalqWCDDLSQ---------ALSELARVLKPGGLLA 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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