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Conserved domains on  [gi|6435574]
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Chain C, Glycine N-methyltransferase

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

EC:  2.1.-.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405

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 2.37e-16

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


:

Pssm-ID: 433377 [Multi-domain]  Cd Length: 97  Bit Score: 72.61  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6435574    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 2.37e-16

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


Pssm-ID: 433377 [Multi-domain]  Cd Length: 97  Bit Score: 72.61  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6435574    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 1.25e-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: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227  43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574  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 2.46e-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: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6435574  138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
21-165 8.02e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6435574   100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
58-172 5.33e-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 [Multi-domain]  Cd Length: 223  Bit Score: 46.49  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 6435574    134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
60-168 2.37e-16

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


Pssm-ID: 433377 [Multi-domain]  Cd Length: 97  Bit Score: 72.61  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     60 VLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLG 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGpnARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6435574    138 nSFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  73 -VLHHLPD-----PDLEAALREIARVLKPGG 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
61-172 7.83e-13

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


Pssm-ID: 429883 [Multi-domain]  Cd Length: 94  Bit Score: 63.07  E-value: 7.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     61 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 139
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAE------DLPFPDNsFDLVLSS-EV 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 6435574    140 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam08241  69 LHHVED-------PERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
29-172 1.25e-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: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   29 VWQLYIgdtrSRTAEYKAWLLGLlrqhgchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERWNRrkepafd 108
Cdd:COG2227  43 LRLDYI----REVARLRFDLPGL-------RVLDVGCGGGILSEPLARLGASVTGIDASEKPIEVA-KLHALE------- 103
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574  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 2.46e-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: 2.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73
                        90       100       110
                ....*....|....*....|....*....|....*
gi 6435574  138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
61-170 1.53e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.99  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     61 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 138
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS-N 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 6435574    139 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 170
Cdd:pfam08242  74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
59-174 2.54e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 433524 [Multi-domain]  Cd Length: 150  Bit Score: 57.81  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     59 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 135
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEEVGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDKFDVVIS 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6435574    136 LGnSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVIDH 174
Cdd:pfam13847  81 NC-VLNLIPDP-------DKVLQEILRVLKPGGRLIISD 111
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
33-172 2.04e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.51  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     33 YIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMlkyalkerwnrrKEPAFDKWVI 112
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRF 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    113 EEANwltLDKDVPAGDGFDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam13489  67 DQFD---EQEAAVPAGKFDVIVAR-EVLEHVPD-------PPALLRQIAALLKPGGLLLL 115
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
21-165 8.02e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6435574   100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
PRK08317 PRK08317
hypothetical protein; Provisional
42-178 8.08e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.94  E-value: 8.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    42 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 118
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574   119 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHKNYD 178
Cdd:PRK08317  82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
33-194 4.92e-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: 4.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   33 YIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIM--LVEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKW 110
Cdd:COG0500  25 AFLLLAEELLDLLLVLRLLRLLPGGLGVLDIGCGTGRLALLarLGGRGAYVVGVDLSPEMLALARA----RAEGAGLGLV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574  111 VIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSkgdqsehrlALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGK 190
Cdd:COG0500 101 DFVVADALGGVLPFEDSASFDLVISLLVLHLLPPAK---------ALRELLRVLKPGGRLVLSDLLRDGLLEGRLAALLG 171

                ....
gi 6435574  191 NIYY 194
Cdd:COG0500 172 FGDP 175
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];
59-172 5.49e-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: 5.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   59 RVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLD-KDvpagDGFDAVIC 135
Cdd:COG2226  54 KVLDVACGTGDMALLLAKSVgtGEVVGLDISESMLEVARE----KLKKKGVQNVEFVVGDAENLPfPD----NSFDAVTI 125
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6435574  136 lGNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2226 126 -SFGLRNVTD-------IDKALKEMYRVLKPGGRLLV 154
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
58-172 3.43e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 50.15  E-value: 3.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    58 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 133
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6435574   134 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
58-172 5.33e-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 [Multi-domain]  Cd Length: 223  Bit Score: 46.49  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574     58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 6435574    134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
59-176 7.90e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.49  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 136
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 6435574   137 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHKN 176
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
48-106 1.05e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.74  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6435574    48 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 106
Cdd:PRK10258  34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
35-172 1.60e-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: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   35 GDTRSRTAEYKAW--LLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYALKErwnRRKEPAFDKWV 111
Cdd:COG2230  49 PDMTLEEAQRAKLdlILEKLGLKPGMTLLDIGCGWGGLAIYAAEEyGVTVVGVTLSEEQLAYAEKR---IAARGLEDNVE 125
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6435574  112 IEEANWLTLDKDvpagdgFDAVICLGnSFAHLpdskGDQSEHRLaLKNIASMVRPGGLLVI 172
Cdd:COG2230 126 VRLQDYRDFEEP------FDRIVSVG-MFEHV----GKENYDDF-FKKVYALLKPGGRMLL 174
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
47-174 5.72e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574    47 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 124
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   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 6.68e-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: 6.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6435574   47 WLLGLLRQHGCHrVLDVACGTGVDSIMLVEEG--FSVTSVDASDKMLKYAlkeRWNRRKEpAFDKWVIEEANWLTldkdv 124
Cdd:COG2890 102 AALALLLQLDKR-ILDLGTGSGAIAIALAKEGpdAEVIAVDISPDALALA---RENAERN-GLVRVLVVQSDLFE----- 171
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6435574  125 PAGDGFDAVIC----LGNSFAHLPDSKGDqSEHRLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:COG2890 172 PLRGKFDLIVSnppyIPAEDPELLPEVVR-YEPLLALvgggdglevyrrilGEAPDILKPGGVLILEI 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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