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Conserved domains on  [gi|8567354|ref|NP_058780|]
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glycine N-methyltransferase [Rattus norvegicus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

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 ...
 37-173 8.72e-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: 88.15  E-value: 8.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   37 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567354  115 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
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 ...
 37-173 8.72e-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: 88.15  E-value: 8.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   37 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567354  115 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:COG2227  71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 61-169 2.01e-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: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     61 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 139
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 8567354    140 SFAHLPDskgdqSEHRLALKNIASMVRPGG 169
Cdd:pfam13649  72 VLHHLPD-----PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-173 2.32e-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: 62.45  E-value: 2.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   60 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 138
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73

                        90       100       110
                ....*....|....*....|....*....|....*
gi 8567354  139 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 22-166 9.63e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.46  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    22 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 100
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8567354   101 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 166
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 59-173 5.81e-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: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     59 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 134
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8567354    135 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 173
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 ...
 37-173 8.72e-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: 88.15  E-value: 8.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   37 DTRSRTAEYKAWLLGLLRQHGCH--RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvie 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA------RERAAELN----- 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567354  115 eANWLTLD-KDVPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:COG2227  71 -VDFVQGDlEDLPLEDGsFDLVICS-EVLEHLPD-------PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 37-173 1.72e-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: 1.72e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   37 DTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWV-IEE 115
Cdd:COG2226   2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA------RERAAEAGLNVeFVV 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 8567354  116 ANWLTLdkdvPAGDG-FDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:COG2226  76 GDAEDL----PFPDGsFDLVISS-FVLHHLPD-------PERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 61-169 2.01e-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: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     61 VLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkERWNRRKEPAFDkwvIEEANWLTLDkdvPAGDGFDAVICLGn 139
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA--RERAAEAGLNVE---FVQGDAEDLP---FPDGSFDLVVSSG- 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 8567354    140 SFAHLPDskgdqSEHRLALKNIASMVRPGG 169
Cdd:pfam13649  72 VLHHLPD-----PDLEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 47-173 6.88e-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: 6.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   47 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlKERWNRRKEPafDKWVIEEANWLtldkDV 125
Cdd:COG2230  41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYA-RERAAEAGLA--DRVEVRLADYR----DL 113

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 8567354  126 PAGDGFDAVICLGnSFAHLPDskgdqSEHRLALKNIASMVRPGGLLVI 173
Cdd:COG2230 114 PADGQFDAIVSIG-MFEHVGP-----ENYPAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
20-179 8.48e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.80  E-value: 8.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   20 DQYADgeaarVWQLYIGDTR--SRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlk 97
Cdd:COG4976  12 DQYAD-----SYDAALVEDLgyEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   98 erwnrRKEPAFDKWVIEEanwltLDKDVPAGDGFDAVICLGnSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDHRN 177
Cdd:COG4976  85 -----REKGVYDRLLVAD-----LADLAEPDGRFDLIVAAD-VLTYLGD-------LAAVFAGVARALKPGGLFIFSVED 146


                ..
gi 8567354  178 YD 179
Cdd:COG4976 147 AD 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
60-175 1.64e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 65.23  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   60 RVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDkwvIEEANWLTLDKDVPagdgFDAVICl 137
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA------RARLPNVR---FVVADLRDLDPPEP----FDLVVS- 69

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 8567354  138 GNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVIDH 175
Cdd:COG4106  70 NAALHWLPD-------HAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 62-173 8.76e-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: 8.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     62 LDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwNRRKEPAFDKWVIEEANwltldkDVPAGDG-FDAVICLgNS 140
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAE------DLPFPDNsFDLVLSS-EV 68

                          90       100       110
                  ....*....|....*....|....*....|...
gi 8567354    141 FAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:pfam08241  69 LHHVED-------PERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-173 2.32e-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: 62.45  E-value: 2.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   60 RVLDVACGTGVDSIMLVE-EGFSVTSVDASDKMLKYAlKERWNRRKEpafDKWVIEEANWLTLDKDvpAGDGFDAVIClG 138
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE--ADESFDVIIS-D 73

                        90       100       110
                ....*....|....*....|....*....|....*
gi 8567354  139 NSFAHLPDSkgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:cd02440  74 PPLHHLVED------LARFLEEARRLLKPGGVLVL 102
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 62-171 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 8567354     62 LDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLgN 139
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAA------RERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS-N 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 8567354    140 SFAHLPDSKGdqsehrlALKNIASMVRPGGLL 171
Cdd:pfam08242  74 VLHHLADPRA-------VLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 60-175 3.47e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     60 RVLDVACGTGVDSIMLVEEGFS---VTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEANWLTLDKDVpAGDGFDAVIC 136
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARE----NAQKLGFDNVEFEQGDIEELPELL-EDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 8567354    137 LGnSFAHLPDSkgdqsehRLALKNIASMVRPGGLLVIDH 175
Cdd:pfam13847  81 NC-VLNHIPDP-------DKVLQEILRVLKPGGRLIISD 111
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 31-179 1.57e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.46  E-value: 1.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   31 WQLYIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEE-GFSVTSVDASDKMLKYAlkerwnRRKEPAFD 109
Cdd:COG0500   2 WDSYYSDELLPGLAALLALLERLPKGG--RVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALA------RARAAKAG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8567354  110 kwvIEEANWLTLD----KDVPAGDgFDAVICLGnSFAHLPDSKGDQsehrlALKNIASMVRPGGLLVIDHRNYD 179
Cdd:COG0500  74 ---LGNVEFLVADlaelDPLPAES-FDLVVAFG-VLHHLPPEEREA-----LLRELARALKPGGVLLLSASDAA 137
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-173 2.52e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 55.13  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     34 YIGDTRSRTAEYKAWLLGLLRQHGchRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMlkyalkerwnrrKEPAFDKWVI 113
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRF 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    114 EEANwltLDKDVPAGDGFDAVICLgNSFAHLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:pfam13489  67 DQFD---EQEAAVPAGKFDVIVAR-EVLEHVPD-------PPALLRQIAALLKPGGLLLL 115
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 22-166 9.63e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.46  E-value: 9.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    22 YADGEAARVwQLYIGDTRSRT-AEYKAWLLGLLRQHGChRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlKERw 100
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTGL-RILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEA-RER- 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8567354   101 nrrkepAFDKWVIEEANWLTLDKDvPAGDGFDAVICLgNSFAHLPDSKGDQsehrlALKNIASMVR 166
Cdd:PRK07580 105 ------APEAGLAGNITFEVGDLE-SLLGRFDTVVCL-DVLIHYPQEDAAR-----MLAHLASLTR 157
PRK08317 PRK08317
hypothetical protein; Provisional
 43-179 1.24e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    43 AEYKAWLLGLLRQHGCHRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYAlKERwnRRKEPAFDKWVIEEANWL 119
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KER--AAGLGPNVEFVRGDADGL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8567354   120 tldkdvPAGDG-FDAVICLgNSFAHLPDSKGdqsehrlALKNIASMVRPGGLLVIDHRNYD 179
Cdd:PRK08317  82 ------PFPDGsFDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWD 128
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 59-173 3.60e-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: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    59 HRVLDVACGTGVDSIMLVEEG---FSVTSVDASDKMLKYAlKERWNRRKEPAFDKWVIEEANWLTLDKDVpagdgFDAV- 134
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS-----FDAVt 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 8567354   135 ICLG--NsfahLPDskgdqseHRLALKNIASMVRPGGLLVI 173
Cdd:PRK00216 127 IAFGlrN----VPD-------IDKALREMYRVLKPGGRLVI 156
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 47-175 1.70e-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: 47.10  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   47 AWLLGLLRQHGCHRVLDVACGTGVDSIMLVE---EGFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEANWLTLDK 123
Cdd:COG4122   6 RLLYLLARLLGAKRILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIA---RENFARAGLADRIRLILGDALEVLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 8567354  124 DVPAGDgFDAVIClgnsfahlpDskGDQSEHRLALKNIASMVRPGGLLVIDH 175
Cdd:COG4122  83 RLADGP-FDLVFI---------D--ADKSNYPDYLELALPLLRPGGLIVADN 122
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 59-173 5.81e-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: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354     59 HRVLDVACGTGVDSIML---VEEGFSVTSVDASDKMLKYALKerwnRRKEPAFDKWVIEEAnwltldKDVPAGDG-FDAV 134
Cdd:TIGR01934  41 QKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVAKK----KSELPLNIEFIQADA------EALPFEDNsFDAV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8567354    135 IC---LGNsFAHLPdskgdqsehrLALKNIASMVRPGGLLVI 173
Cdd:TIGR01934 111 TIafgLRN-VTDIQ----------KALREMYRVLKPGGRLVI 141
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 59-185 2.63e-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: 40.70  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   59 HRVLDVACGTGVdsiMLVEE---GFSVTSVDASDKM-------LKYALKERWNRRKEPAFDkwvieeanwLTLdkdvpAG 128
Cdd:COG1041  28 DTVLDPFCGTGT---ILIEAgllGRRVIGSDIDPKMvegarenLEHYGYEDADVIRGDARD---------LPL-----AD 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8567354  129 DGFDAVIC---LGNSFahlpDSKGDQSEHRL--ALKNIASMVRPGGLLVI--DHRNYDYILSTG 185
Cdd:COG1041  91 ESVDAIVTdppYGRSS----KISGEELLELYekALEEAARVLKPGGRVVIvtPRDIDELLEEAG 150
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 60-172 5.19e-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: 5.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   60 RVLDVACGTGvdsimlveeGFS----------VTSVDASDKMLKYA--------LKERWNRRKEPAFDkwvieeanwlTL 121
Cdd:COG1092 219 RVLNLFSYTG---------GFSvhaaaggaksVTSVDLSATALEWAkenaalngLDDRHEFVQADAFD----------WL 279

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8567354  122 DKDVPAGDGFDAVIC----LGNSFAHLPDSKGDQSE-HRLALKniasMVRPGGLLV 172
Cdd:COG1092 280 RELAREGERFDLIILdppaFAKSKKDLFDAQRDYKDlNRLALK----LLAPGGILV 331
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 39-136 7.96e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 7.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   39 RSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYAlkeRWNRRKEPAFDKWVIEEA 116
Cdd:COG2890  94 RPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVA---RRNAERLGLEDRVRFLQG 170

                        90       100
                ....*....|....*....|
gi 8567354  117 NWLTldkDVPAGDGFDAVIC 136
Cdd:COG2890 171 DLFE---PLPGDGRFDLIVS 187
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 60-173 8.16e-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: 8.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   60 RVLDVACGTGVDSI---MLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPAFDKWVIEEANWLTLD-KDVPAGDGFDAVI 135
Cdd:COG5459  83 TVLDVGAGPGTAAWaaaDAWPSLLDATLLERSAAALALG------RRLARAAANPALETAEWRLADlAAALPAPPADLVV 156

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 8567354  136 ClGNSFAHLPDSKgdqsehRLALknIASM-VRPGGLLVI 173
Cdd:COG5459 157 A-SYVLNELADAA------RAAL--VDRLwLAPDGALLI 186
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 60-177 9.07e-04

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    60 RVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkeRWNRRKEPafdkwVIEEANWL--TLDKDVPAGDGFDAVICL 137
Cdd:PLN02396 134 KFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIA---RLHADMDP-----VTSTIEYLctTAEKLADEGRKFDAVLSL 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 8567354   138 gnsfahlpdskgDQSEHRLA----LKNIASMVRPGGLLVIDHRN 177
Cdd:PLN02396 206 ------------EVIEHVANpaefCKSLSALTIPNGATVLSTIN 237
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 49-107 1.17e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 39.74  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8567354    49 LLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYAlkerwnRRKEPA 107
Cdd:PRK10258  34 LLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQA------RQKDAA 86
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 48-175 6.00e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354    48 WLLGLLRQHGCHRVLDVACGTGVDSIMLVEE--GFSVTSVDASDKMLKYALKerwNRRKEPAfDKWVIEEANWLTldkDV 125
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVARR---NAKHGLG-ARVEFLQGDWFE---PL 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8567354   126 PAGDgFDAVIClgN----SFAHLPDSKGDQSEH--RLAL--------------KNIASMVRPGGLLVIDH 175
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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