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Conserved domains on  [gi|6435573|pdb|1D2H|B]
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Chain B, GLYCINE N-METHYLTRANSFERASE

Protein Classification

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG( domain architecture ID 11454890)

bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG UbiG is a class I SAM-dependent methyltransferase that catalyzes both methylation steps in ubiquinone biosynthesis

EC:  2.1.1.222|2.1.1.64
Gene Ontology:  GO:0102208|GO:0008425|GO:0008689|GO:0032259|GO:0006744
PubMed:  10419476|11583838

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-172 6.60e-22

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: 88.54  E-value: 6.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       36 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 113
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_B      114 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2227  71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-172 6.60e-22

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: 88.54  E-value: 6.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       36 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 113
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_B      114 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2227  71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-168 1.82e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         60 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71

                          90       100       110
                  ....*....|....*....|....*....|
1D2H_B        139 SFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  72 VLHHLPD-----PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-172 2.57e-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: 2.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73

                        90       100       110
                ....*....|....*....|....*....|....*
1D2H_B      138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 21-165 8.36e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_B       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 5.56e-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: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
1D2H_B        134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 36-172 6.60e-22

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: 88.54  E-value: 6.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       36 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 113
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_B      114 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2227  71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-172 1.45e-18

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: 80.04  E-value: 1.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       36 DTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWV-IEE 114
Cdd:COG2226   2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA------RERAAEAGLNVeFVV 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
1D2H_B      115 ANWLTLdkdvPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:COG2226  76 GDAEDL----PFPDGsFDLVISS-FVLHHLPD-------PERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-168 1.82e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.98  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         60 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71

                          90       100       110
                  ....*....|....*....|....*....|
1D2H_B        139 SFAHLPDskgdqSEHRLALKNIASMVRPGG 168
Cdd:pfam13649  72 VLHHLPD-----PDLEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 46-172 5.72e-15

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 70.73  E-value: 5.72e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       46 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlKERWNRRKEPafDKWVIEEANWLtldkDV 124
Cdd:COG2230  41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYA-RERAAEAGLA--DRVEVRLADYR----DL 113

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1D2H_B      125 PAGDGFDAVICLGnSFAHLPDskgdqSEHRLALKNIASMVRPGGLLVI 172
Cdd:COG2230 114 PADGQFDAIVSIG-MFEHVGP-----ENYPAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-178 8.13e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.80  E-value: 8.13e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       19 DQYADgeaarVWQLYIGDTR--SRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlk 96
Cdd:COG4976  12 DQYAD-----SYDAALVEDLgyEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       97 erwnrRKEPAFDKWVIEEanwltLDKDVPAGDGFDAVICLGnSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDHKN 176
Cdd:COG4976  85 -----REKGVYDRLLVAD-----LADLAEPDGRFDLIVAAD-VLTYLGD-------LAAVFAGVARALKPGGLFIFSVED 146


                ..
1D2H_B      177 YD 178
Cdd:COG4976 147 AD 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
59-174 1.31e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 65.62  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       59 RVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvIEEANWLTLDKDVPagdgFDAVICl 136
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA------RARLPNVR---FVVADLRDLDPPEP----FDLVVS- 69

                        90       100       110
                ....*....|....*....|....*....|....*...
1D2H_B      137 GNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDH 174
Cdd:COG4106  70 NAALHWLPD-------HAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-172 8.67e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.07  E-value: 8.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         61 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 139
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAE------DLPFPDNsFDLVLSS-EV 68

                          90       100       110
                  ....*....|....*....|....*....|...
1D2H_B        140 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam08241  69 LHHVED-------PERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 59-172 2.57e-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: 2.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       59 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 137
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73

                        90       100       110
                ....*....|....*....|....*....|....*
1D2H_B      138 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-170 1.60e-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: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         61 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 138
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS-N 73

                          90       100       110
                  ....*....|....*....|....*....|..
1D2H_B        139 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 170
Cdd:pfam08242  74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 59-174 3.51e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         59 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 135
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
1D2H_B        136 LGnSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVIDH 174
Cdd:pfam13847  81 NC-VLNHIPDP-------DKVLQEILRVLKPGGRLIISD 111
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 33-172 2.12e-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: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         33 YIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMlkyalkerwnrrKEPAFDKWVI 112
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRF 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        113 EEANwltLDKDVPAGDGFDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:pfam13489  67 DQFD---EQEAAVPAGKFDVIVAR-EVLEHVPD-------PPALLRQIAALLKPGGLLLL 115
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 30-173 3.21e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 55.69  E-value: 3.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       30 WQLYIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkerwnRRKEPAFD 108
Cdd:COG0500   2 WDSYYSDELLPGLAALLALLERLPKGG--RVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALA------RARAAKAG 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1D2H_B      109 kwvIEEANWLTLD----KDVPAGDgFDAVICLGnSFAHLPDSKGDQsehrlALKNIASMVRPGGLLVID 173
Cdd:COG0500  74 ---LGNVEFLVADlaelDPLPAES-FDLVVAFG-VLHHLPPEEREA-----LLRELARALKPGGVLLLS 132
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 21-165 8.36e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        21 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 99
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1D2H_B       100 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 165
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
PRK08317 PRK08317
hypothetical protein; Provisional
 42-178 8.43e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.94  E-value: 8.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        42 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 118
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
1D2H_B       119 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHKNYD 178
Cdd:PRK08317  82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 58-172 3.57e-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: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        58 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 133
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
1D2H_B       134 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 172
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 46-174 1.58e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 47.49  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       46 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVE---EGFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEANWLTLDK 122
Cdd:COG4122   6 RLLYLLARLLGAKRILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIA---RENFARAGLADRIRLILGDALEVLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1D2H_B      123 DVPAGDgFDAVIClgnsfahlpDskGDQSEHRLALKNIASMVRPGGLLVIDH 174
Cdd:COG4122  83 RLADGP-FDLVFI---------D--ADKSNYPDYLELALPLLRPGGLIVADN 122
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 58-172 5.56e-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: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B         58 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 133
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
1D2H_B        134 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 172
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 58-184 2.36e-04

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 41.09  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       58 HRVLDVACGTGVdsiMLVEE---GFSVTSVDASDKM-------LKYALKERWNRRKEPAFDkwvieeanwLTLdkdvpAG 127
Cdd:COG1041  28 DTVLDPFCGTGT---ILIEAgllGRRVIGSDIDPKMvegarenLEHYGYEDADVIRGDARD---------LPL-----AD 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1D2H_B      128 DGFDAVIC---LGNSFahlpDSKGDQSEHRL--ALKNIASMVRPGGLLVI--DHKNYDYILSTG 184
Cdd:COG1041  91 ESVDAIVTdppYGRSS----KISGEELLELYekALEEAARVLKPGGRVVIvtPRDIDELLEEAG 150
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 59-171 4.98e-04

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 41.32  E-value: 4.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       59 RVLDVACGTGvdsimlveeGFS----------VTSVDASDKMLKYA--------LKERWNRRKEPAFDkwvieeanwlTL 120
Cdd:COG1092 219 RVLNLFSYTG---------GFSvhaaaggaksVTSVDLSATALEWAkenaalngLDDRHEFVQADAFD----------WL 279

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
1D2H_B      121 DKDVPAGDGFDAVIC----LGNSFAHLPDSKGDQSE-HRLALKniasMVRPGGLLV 171
Cdd:COG1092 280 RELAREGERFDLIILdppaFAKSKKDLFDAQRDYKDlNRLALK----LLAPGGILV 331
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 38-135 7.30e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.52  E-value: 7.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       38 RSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEA 115
Cdd:COG2890  94 RPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVA---RRNAERLGLEDRVRFLQG 170

                        90       100
                ....*....|....*....|
1D2H_B      116 NWLTldkDVPAGDGFDAVIC 135
Cdd:COG2890 171 DLFE---PLPGDGRFDLIVS 187
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 59-172 7.34e-04

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 40.32  E-value: 7.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       59 RVLDVACGTGVDSI---MLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLD-KDVPAGDGFDAVI 134
Cdd:COG5459  83 TVLDVGAGPGTAAWaaaDAWPSLLDATLLERSAAALALG------RRLARAAANPALETAEWRLADlAAALPAPPADLVV 156

                        90       100       110
                ....*....|....*....|....*....|....*....
1D2H_B      135 ClGNSFAHLPDSKgdqsehRLALknIASM-VRPGGLLVI 172
Cdd:COG5459 157 A-SYVLNELADAA------RAAL--VDRLwLAPDGALLI 186
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 59-176 8.24e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.49  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        59 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 136
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
1D2H_B       137 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHKN 176
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 48-106 1.10e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.74  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
1D2H_B        48 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 106
Cdd:PRK10258  34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 47-174 5.97e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B        47 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 124
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1D2H_B       125 PAGDgFDAVIClgN----SFAHLPDSKGDQSEH--RLAL--------------KNIASMVRPGGLLVIDH 174
Cdd:PRK09328 172 PGGR-FDLIVS--NppyiPEADIHLLQPEVRDHepHLALfggedgldfyrriiEQAPRYLKPGGWLLLEI 238
 
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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