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Conserved domains on  [gi|47086405|ref|NP_997981|]
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glycine N-methyltransferase [Danio rerio]

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 ...
37-174 3.06e-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: 89.69  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  37 DTRSRTEEYKSWVLALLRKHGVQ--RVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlKERWERRKETafdnwvIE 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA-RERAAELNVD------FV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405 115 EANWLTLPEdvkkPGDGFDAVICLgNSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:COG2227  75 QGDLEDLPL----EDGSFDLVICS-EVLEHLP-------DPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
37-174 3.06e-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: 89.69  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  37 DTRSRTEEYKSWVLALLRKHGVQ--RVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlKERWERRKETafdnwvIE 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA-RERAAELNVD------FV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405 115 EANWLTLPEdvkkPGDGFDAVICLgNSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:COG2227  75 QGDLEDLPL----EDGSFDLVICS-EVLEHLP-------DPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
61-170 1.25e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    61 VLDVACGTGVDSIMLVEE-GFSVVSVDASDKMLKYAlKERWERRKEtafdNWVIEEANWLTLPEdvkkPGDGFDAVICLG 139
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA-RERAAEAGL----NVEFVQGDAEDLPF----PDGSFDLVVSSG 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 47086405   140 nSFAHLPDfkgdqSDQKLALQNIGSMVKPGG 170
Cdd:pfam13649  72 -VLHHLPD-----PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
60-174 1.35e-13

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: 65.53  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  60 RVLDVACGTGVDSIMLVE-EGFSVVSVDASDKMLKYAlKERWERRKEtafDNWVIEEANWLTLPEDvkkPGDGFDAVICl 138
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE---ADESFDVIIS- 72
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 47086405 139 GNSFAHLPDfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:cd02440  73 DPPLHHLVE------DLARFLEEARRLLKPGGVLVL 102
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
22-167 8.58e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   22 YADGKAAKVwQLYIGDTRSRT-EEYKSWVLALLRKHGvQRVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYALkerw 100
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTG-LRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEAR---- 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086405  101 ERRKETAFDNWVIEEANWLtlpEDVKKPgdgFDAVICLgNSFAHLPdfkgdQSDQKLALQNIGSMVK 167
Cdd:PRK07580 103 ERAPEAGLAGNITFEVGDL---ESLLGR---FDTVVCL-DVLIHYP-----QEDAARMLAHLASLTR 157
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
52-174 7.38e-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: 46.10  E-value: 7.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    52 LLRKHGVQRVLDVACGTGVDSIML---VEEGFSVVSVDASDKMLKYAlkerweRRKETAFDNWVIEEANWLTLP-EDvkk 127
Cdd:TIGR01934  34 LIGVFKGQKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVA------KKKSELPLNIEFIQADAEALPfED--- 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 47086405   128 pgDGFDAVIClgnSFAhLPDFkgdqSDQKLALQNIGSMVKPGGILII 174
Cdd:TIGR01934 105 --NSFDAVTI---AFG-LRNV----TDIQKALREMYRVLKPGGRLVI 141
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
37-174 3.06e-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: 89.69  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  37 DTRSRTEEYKSWVLALLRKHGVQ--RVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlKERWERRKETafdnwvIE 114
Cdd:COG2227   2 SDPDARDFWDRRLAALLARLLPAggRVLDVGCGTGRLALALARRGADVTGVDISPEALEIA-RERAAELNVD------FV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405 115 EANWLTLPEdvkkPGDGFDAVICLgNSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:COG2227  75 QGDLEDLPL----EDGSFDLVICS-EVLEHLP-------DPAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
37-174 4.89e-20

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: 84.28  E-value: 4.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  37 DTRSRTEEYKSWVLALLRKHGVQRVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlkerwERRKETAFDNWVIEEA 116
Cdd:COG2226   2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA-----RERAAEAGLNVEFVVG 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47086405 117 NWLTLPEdvkkPGDGFDAVICLgNSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:COG2226  77 DAEDLPF----PDGSFDLVISS-FVLHHLP-------DPERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
61-170 1.25e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 76.06  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    61 VLDVACGTGVDSIMLVEE-GFSVVSVDASDKMLKYAlKERWERRKEtafdNWVIEEANWLTLPEdvkkPGDGFDAVICLG 139
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERA-RERAAEAGL----NVEFVQGDAEDLPF----PDGSFDLVVSSG 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 47086405   140 nSFAHLPDfkgdqSDQKLALQNIGSMVKPGG 170
Cdd:pfam13649  72 -VLHHLPD-----PDLEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
20-180 8.17e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 76.58  E-value: 8.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  20 DQYADgkaakVWQLYIGDTR--SRTEEYKSWVLALLRKHGVQRVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlk 97
Cdd:COG4976  12 DQYAD-----SYDAALVEDLgyEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA-- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  98 erweRRKEtAFDNWVIEEANwltlpeDVKKPGDGFDAVICLGnSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILIIDHR 177
Cdd:COG4976  85 ----REKG-VYDRLLVADLA------DLAEPDGRFDLIVAAD-VLTYLG-------DLAAVFAGVARALKPGGLFIFSVE 145

                ...
gi 47086405 178 NYD 180
Cdd:COG4976 146 DAD 148
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
52-174 4.89e-15

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 71.11  E-value: 4.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  52 LLRKHGV---QRVLDVACGTGVDSIMLVEE-GFSVVSVDASDKMLKYAlKERWERRKETafDNWVIEEANWLTLPEDvkk 127
Cdd:COG2230  43 ILRKLGLkpgMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYA-RERAAEAGLA--DRVEVRLADYRDLPAD--- 116
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 47086405 128 pgDGFDAVICLGnSFAHLPDfkgdqSDQKLALQNIGSMVKPGGILII 174
Cdd:COG2230 117 --GQFDAIVSIG-MFEHVGP-----ENYPAYFAKVARLLKPGGRLLL 155
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
60-174 1.35e-13

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: 65.53  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  60 RVLDVACGTGVDSIMLVE-EGFSVVSVDASDKMLKYAlKERWERRKEtafDNWVIEEANWLTLPEDvkkPGDGFDAVICl 138
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELA-RKAAAALLA---DNVEVLKGDAEELPPE---ADESFDVIIS- 72
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 47086405 139 GNSFAHLPDfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:cd02440  73 DPPLHHLVE------DLARFLEEARRLLKPGGVLVL 102
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
60-176 2.59e-13

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 66.29  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    60 RVLDVACGTGVDSIMLVEEGFS---VVSVDASDKMLKYALkerwERRKETAFDNWVIEEANWLTLPEDVKKpgDGFDAVI 136
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKAR----ENAQKLGFDNVEFEQGDIEELPELLED--DKFDVVI 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 47086405   137 CLGnSFAHLPdfkgdqsDQKLALQNIGSMVKPGGILIIDH 176
Cdd:pfam13847  80 SNC-VLNHIP-------DPDKVLQEILRVLKPGGRLIISD 111
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
60-176 6.03e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.69  E-value: 6.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  60 RVLDVACGTGVDSIMLVEE--GFSVVSVDASDKMLKYAlkerweRRKetaFDNWVIEEANWLTLPedvkkPGDGFDAVIC 137
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA------RAR---LPNVRFVVADLRDLD-----PPEPFDLVVS 69
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 47086405 138 lGNSFAHLPDFKGdqsdqklALQNIGSMVKPGGILIIDH 176
Cdd:COG4106  70 -NAALHWLPDHAA-------LLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
62-174 4.47e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.14  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    62 LDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYAlkerwERRKETAFDNWVIEEANWLTLPEDVkkpgdgFDAVICLgNS 141
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELA-----REKAPREGLTFVVGDAEDLPFPDNS------FDLVLSS-EV 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 47086405   142 FAHLPdfkgdqsDQKLALQNIGSMVKPGGILII 174
Cdd:pfam08241  69 LHHVE-------DPERALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
41-202 6.53e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 59.75  E-value: 6.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    41 RTEEYKSWVLALLRKHGVQ-RVLDVACGTGVDSIMLVEEGFSVVSVDASDKMlkyalkerwerrKETAFDNWVIEEANwl 119
Cdd:pfam13489   5 RERLLADLLLRLLPKLPSPgRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIA------------IERALLNVRFDQFD-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   120 tlPEDVKKPGDGFDAVICLgNSFAHLPDFKGdqsdqklALQNIGSMVKPGG-ILIIDHRNYDYIIE-----TGQVPQGKN 193
Cdd:pfam13489  71 --EQEAAVPAGKFDVIVAR-EVLEHVPDPPA-------LLRQIAALLKPGGlLLLSTPLASDEADRlllewPYLRPRNGH 140
                         170
                  ....*....|.
gi 47086405   194 IYYKS--DLKQ 202
Cdd:pfam13489 141 ISLFSarSLKR 151
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
50-180 1.73e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.16  E-value: 1.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  50 LALLRKHGvqRVLDVACGTGVDSIMLVEE-GFSVVSVDASDKMLKYAlkeRwERRKETAFDNWVIEEANWLTLPEDvkkP 128
Cdd:COG0500  21 LERLPKGG--RVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALA---R-ARAAKAGLGNVEFLVADLAELDPL---P 91
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 47086405 129 GDGFDAVICLGnSFAHLPdfkgdQSDQKLALQNIGSMVKPGGILIIDHRNYD 180
Cdd:COG0500  92 AESFDLVVAFG-VLHHLP-----PEEREALLRELARALKPGGVLLLSASDAA 137
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
62-172 1.88e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.61  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    62 LDVACGTGVDSIMLVEE--GFSVVSVDASDKMLKYALkerwERRKETAFDNWVIEEanwLTLPEDVKKPGDGFDAVICLg 139
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAAR----ERLAALGLLNAVRVE---LFQLDLGELDPGSFDVVVAS- 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 47086405   140 NSFAHLPDFKGdqsdqklALQNIGSMVKPGGIL 172
Cdd:pfam08242  73 NVLHHLADPRA-------VLRNIRRLLKPGGVL 98
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
22-167 8.58e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   22 YADGKAAKVwQLYIGDTRSRT-EEYKSWVLALLRKHGvQRVLDVACGTGVDSIMLVEEGFSVVSVDASDKMLKYALkerw 100
Cdd:PRK07580  29 YSDAPVSKV-RATVRAGHQRMrDTVLSWLPADGDLTG-LRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEAR---- 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47086405  101 ERRKETAFDNWVIEEANWLtlpEDVKKPgdgFDAVICLgNSFAHLPdfkgdQSDQKLALQNIGSMVK 167
Cdd:PRK07580 103 ERAPEAGLAGNITFEVGDL---ESLLGR---FDTVVCL-DVLIHYP-----QEDAARMLAHLASLTR 157
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
59-174 2.66e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 53.62  E-value: 2.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   59 QRVLDVACGTGVDSIMLVEEG---FSVVSVDASDKMLKYAlKERWERRKETAFDNWVIEEANWLTLPEDVkkpgdgFDAV 135
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVG-REKLRDLGLSGNVEFVQGDAEALPFPDNS------FDAV 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 47086405  136 -ICLG--NsfahLPDFkgdqsdqKLALQNIGSMVKPGGILII 174
Cdd:PRK00216 126 tIAFGlrN----VPDI-------DKALREMYRVLKPGGRLVI 156
PRK08317 PRK08317
hypothetical protein; Provisional
43-183 2.72e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.40  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   43 EEYKSWVLALLRKHGVQRVLDVACGTGVDSIML---VEEGFSVVSVDASDKMLKYAlKERWErrKETAFDNWVIEEANWL 119
Cdd:PRK08317   5 RRYRARTFELLAVQPGDRVLDVGCGPGNDARELarrVGPEGRVVGIDRSEAMLALA-KERAA--GLGPNVEFVRGDADGL 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086405  120 TLPEDVkkpgdgFDAVICLgNSFAHLPDFKGdqsdqklALQNIGSMVKPGGILIIDHRNYDYII 183
Cdd:PRK08317  82 PFPDGS------FDAVRSD-RVLQHLEDPAR-------ALAEIARVLRPGGRVVVLDTDWDTLV 131
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
52-174 7.38e-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: 46.10  E-value: 7.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    52 LLRKHGVQRVLDVACGTGVDSIML---VEEGFSVVSVDASDKMLKYAlkerweRRKETAFDNWVIEEANWLTLP-EDvkk 127
Cdd:TIGR01934  34 LIGVFKGQKVLDVACGTGDLAIELaksAPDRGKVTGVDFSSEMLEVA------KKKSELPLNIEFIQADAEALPfED--- 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 47086405   128 pgDGFDAVIClgnSFAhLPDFkgdqSDQKLALQNIGSMVKPGGILII 174
Cdd:TIGR01934 105 --NSFDAVTI---AFG-LRNV----TDIQKALREMYRVLKPGGRLVI 141
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
59-188 3.65e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 43.97  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    59 QRVLDVACGTGVDSIML---VEEGFSVVSVDASDKMLKYALKerweRRKETAFDNWVIEEANWLTLPEdvkkPGDGFDAV 135
Cdd:pfam01209  44 NKFLDVAGGTGDWTFGLsdsAGSSGKVVGLDINENMLKEGEK----KAKEEGKYNIEFLQGNAEELPF----EDDSFDIV 115
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 47086405   136 IClgnSFAhLPDFkgdqSDQKLALQNIGSMVKPGGILiidhrnydYIIETGQV 188
Cdd:pfam01209 116 TI---SFG-LRNF----PDYLKVLKEAFRVLKPGGRV--------VCLEFSKP 152
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
52-176 1.41e-04

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: 41.71  E-value: 1.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  52 LLRKHGVQRVLDVACGTGVDSIMLVE---EGFSVVSVDASDKMLKYAlKERWERRKETafDNWVIEEANWL-TLPEDVKK 127
Cdd:COG4122  11 LARLLGAKRILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIA-RENFARAGLA--DRIRLILGDALeVLPRLADG 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 47086405 128 PgdgFDAVIClgnsfahlpDfkGDQSDQKLALQNIGSMVKPGGILIIDH 176
Cdd:COG4122  88 P---FDLVFI---------D--ADKSNYPDYLELALPLLRPGGLIVADN 122
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
39-137 1.64e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.44  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  39 RSRTEEYKSWVLALLRKHGVQRVLDVACGTGVDSIMLVEE--GFSVVSVDASDKMLKYAlkerweRR--KETAFDNWV-I 113
Cdd:COG2890  94 RPETEELVELALALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVA------RRnaERLGLEDRVrF 167
                        90       100
                ....*....|....*....|....*
gi 47086405 114 EEANWLT-LPEDVKkpgdgFDAVIC 137
Cdd:COG2890 168 LQGDLFEpLPGDGR-----FDLIVS 187
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
60-186 2.48e-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: 2.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  60 RVLDVACGTGVdsiMLVEE---GFSVVSVDASDKMLKYAlkerweRR--KETAFDNWVIEEANWLTLPEdvkkPGDGFDA 134
Cdd:COG1041  29 TVLDPFCGTGT---ILIEAgllGRRVIGSDIDPKMVEGA------REnlEHYGYEDADVIRGDARDLPL----ADESVDA 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086405 135 VIC----------LGNSFAHLpdFKGdqsdqklALQNIGSMVKPGGILII--DHRNYDYIIETG 186
Cdd:COG1041  96 IVTdppygrsskiSGEELLEL--YEK-------ALEEAARVLKPGGRVVIvtPRDIDELLEEAG 150
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
39-137 2.77e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 41.69  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   39 RSRTEEYKSWVLALLRKHGVQRVLDVACGTGVDSIMLVEE--GFSVVSVDASDKMLKYAlkerweRR--KETAFDNWVIE 114
Cdd:PRK09328  90 RPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVA------RRnaKHGLGARVEFL 163
                         90       100
                 ....*....|....*....|...
gi 47086405  115 EANWLTlpedvKKPGDGFDAVIC 137
Cdd:PRK09328 164 QGDWFE-----PLPGGRFDLIVS 181
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
50-226 8.67e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 39.96  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405    50 LALLRKHGV---QRVLDVACGTGVDSIMLVEEgFSVVSVDA---SDKMLKYAlkerweRRKETAFDNWVIEEANWLTLPE 123
Cdd:TIGR02072  24 LALLKEKGIfipASVLDIGCGTGYLTRALLKR-FPQAEFIAldiSAGMLAQA------KTKLSENVQFICGDAEKLPLED 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   124 DVkkpgdgFDAVIClgNS-FAHLPDFKGdqsdqklALQNIGSMVKPGGILIIDHRNYDYIIETGQVPQGKNIYYKS--DL 200
Cdd:TIGR02072  97 SS------FDLIVS--NLaLQWCDDLSQ-------ALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGLRYLSldEL 161
                         170       180
                  ....*....|....*....|....*...
gi 47086405   201 KQ--DISTSVLWVNSKPhmITLDYTLVL 226
Cdd:TIGR02072 162 KAllKNSFELLTLEEEL--ITLSFDDPL 187
PRK14968 PRK14968
putative methyltransferase; Provisional
51-136 1.81e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.73  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   51 ALLRKHGvQRVLDVACGTGVDSIMLVEEGFSVVSVDASDkmlkYALKERWERRKETAFDNWVIE--EANwltLPEDVKkp 128
Cdd:PRK14968  18 NAVDKKG-DRVLEVGTGSGIVAIVAAKNGKKVVGVDINP----YAVECAKCNAKLNNIRNNGVEviRSD---LFEPFR-- 87

                 ....*...
gi 47086405  129 GDGFDAVI 136
Cdd:PRK14968  88 GDKFDVIL 95
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
47-174 3.92e-03

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: 38.40  E-value: 3.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  47 SWVLALLRKHGV----QRVLDVACGTGVDSI---MLVEEGFSVVSVDASDKMLkyalkeRWERRKETAFDNWVIEEANWl 119
Cdd:COG5459  66 RAALAELAEAGPdfapLTVLDVGAGPGTAAWaaaDAWPSLLDATLLERSAAAL------ALGRRLARAAANPALETAEW- 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47086405 120 tLPEDVKK--PGDGFDAVIClGNSFAHLPDfkgdqsDQKLALqnIGSM-VKPGGILII 174
Cdd:COG5459 139 -RLADLAAalPAPPADLVVA-SYVLNELAD------AARAAL--VDRLwLAPDGALLI 186
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
34-174 4.82e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 38.31  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405   34 YIGDTRSrTEEYKSWVLALLRKhgvQRVLDVACGTGVDSIMLVEE--GFSVVSVDASDKMLkyalkERWERRKETAFDNW 111
Cdd:PRK06922 399 YLEHMNS-SADDKRIILDYIKG---DTIVDVGAGGGVMLDMIEEEteDKRIYGIDISENVI-----DTLKKKKQNEGRSW 469
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086405  112 VIEEANWLTLPEDVKKpgDGFDAVI---CLGNSFAHLPdFKGDQSDQ---KLALQNIGSMVKPGGILII 174
Cdd:PRK06922 470 NVIKGDAINLSSSFEK--ESVDTIVyssILHELFSYIE-YEGKKFNHeviKKGLQSAYEVLKPGGRIII 535
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
59-173 7.18e-03

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: 37.47  E-value: 7.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086405  59 QRVLDVACGTGvdsimlveeGFS----------VVSVDASDKMLKYA--------LKERWERRKETAFDnwvieeanWLt 120
Cdd:COG1092 218 KRVLNLFSYTG---------GFSvhaaaggaksVTSVDLSATALEWAkenaalngLDDRHEFVQADAFD--------WL- 279
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 47086405 121 lpEDVKKPGDGFDAVIC----LGNSFAHLPDFKGDQSD-QKLALQnigsMVKPGGILI 173
Cdd:COG1092 280 --RELAREGERFDLIILdppaFAKSKKDLFDAQRDYKDlNRLALK----LLAPGGILV 331
 
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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