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Conserved domains on  [gi|15595995|ref|NP_249489|]
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phospholipid methyltransferase [Pseudomonas aeruginosa PAO1]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-161 2.17e-23

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: 91.21  E-value: 2.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  40 SLLVPRAHGRVLEIGLGTGLNLgFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCT 119
Cdd:COG2226  16 AALGLRPGARVLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISS 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595995 120 FTLCSIAAPLPALGEMRRVLKRGGELLFCEHGRAPDASVLAW 161
Cdd:COG2226  95 FVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-161 2.17e-23

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: 91.21  E-value: 2.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  40 SLLVPRAHGRVLEIGLGTGLNLgFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCT 119
Cdd:COG2226  16 AALGLRPGARVLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISS 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595995 120 FTLCSIAAPLPALGEMRRVLKRGGELLFCEHGRAPDASVLAW 161
Cdd:COG2226  95 FVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
PRK08317 PRK08317
hypothetical protein; Provisional
 39-197 1.06e-21

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 89.23  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   39 RSLLVPRAHGRVLEIGLGTGlNLGFYDAAKVSA---IVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDT 115
Cdd:PRK08317  12 FELLAVQPGDRVLDVGCGPG-NDARELARRVGPegrVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  116 IVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCEhgraPDASVLAW--------QRRLTPWWKPLAGGcHLDRDMPALLR 187
Cdd:PRK08317  91 VRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD----TDWDTLVWhsgdralmRKILNFWSDHFADP-WLGRRLPGLFR 165

                        170
                 ....*....|
gi 15595995  188 EAGFRIDELE 197
Cdd:PRK08317 166 EAGLTDIEVE 175
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-143 1.11e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.91  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    50 VLEIGLGTGLNLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCTFTL--CSIAA 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLhhLPDPD 80

                          90
                  ....*....|....*.
gi 15595995   128 PLPALGEMRRVLKRGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 17-149 1.03e-10

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: 59.20  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    17 YDRyvLPRLIDFacGMGDVMKQR--SLLVPRAHGRVLEIGLGTGlnlgfyD--------AAKVSAIVGVDPAAQMQALAR 86
Cdd:TIGR01934  12 YDL--LNDLLSF--GLHRLWRRRavKLIGVFKGQKVLDVACGTG------DlaielaksAPDRGKVTGVDFSSEMLEVAK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595995    87 ERAAQIGiPVEMV---ALELgeiRAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCE 149
Cdd:TIGR01934  82 KKSELPL-NIEFIqadAEAL---PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILE 143
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-148 7.56e-07

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: 46.27  E-value: 7.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  49 RVLEIGLGTGLNLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVemVALELGEIRA----EAESFDTIVCTFTLCS 124
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEElppeADESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|....*
gi 15595995 125 IAA-PLPALGEMRRVLKRGGELLFC 148
Cdd:cd02440  79 LVEdLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-161 2.17e-23

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: 91.21  E-value: 2.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  40 SLLVPRAHGRVLEIGLGTGLNLgFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCT 119
Cdd:COG2226  16 AALGLRPGARVLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVISS 94

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595995 120 FTLCSIAAPLPALGEMRRVLKRGGELLFCEHGRAPDASVLAW 161
Cdd:COG2226  95 FVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
PRK08317 PRK08317
hypothetical protein; Provisional
 39-197 1.06e-21

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 89.23  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   39 RSLLVPRAHGRVLEIGLGTGlNLGFYDAAKVSA---IVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDT 115
Cdd:PRK08317  12 FELLAVQPGDRVLDVGCGPG-NDARELARRVGPegrVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  116 IVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCEhgraPDASVLAW--------QRRLTPWWKPLAGGcHLDRDMPALLR 187
Cdd:PRK08317  91 VRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD----TDWDTLVWhsgdralmRKILNFWSDHFADP-WLGRRLPGLFR 165

                        170
                 ....*....|
gi 15595995  188 EAGFRIDELE 197
Cdd:PRK08317 166 EAGLTDIEVE 175
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 50-143 1.11e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.91  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    50 VLEIGLGTGLNLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCTFTL--CSIAA 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLhhLPDPD 80

                          90
                  ....*....|....*.
gi 15595995   128 PLPALGEMRRVLKRGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 45-147 1.01e-16

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: 73.13  E-value: 1.01e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  45 RAHGRVLEIGLGTGLNLGFYdAAKVSAIVGVDPAAQMQALARERAAQIGIPVEMVALElgEIRAEAESFDTIVCTFTLCS 124
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALAL-ARRGADVTGVDISPEALEIARERAAELNVDFVQGDLE--DLPLEDGSFDLVICSEVLEH 99

                        90       100
                ....*....|....*....|...
gi 15595995 125 IAAPLPALGEMRRVLKRGGELLF 147
Cdd:COG2227 100 LPDPAALLRELARLLKPGGLLLL 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-150 3.09e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 73.49  E-value: 3.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  42 LVPRAHGRVLEIGLGTGLnLGFYDAAKVSAIVGVDPAAQMQALARERaaqiGIPVEMVALELGEIRAEAESFDTIVCTFT 121
Cdd:COG4976  42 LPPGPFGRVLDLGCGTGL-LGEALRPRGYRLTGVDLSEEMLAKAREK----GVYDRLLVADLADLAEPDGRFDLIVAADV 116

                        90       100
                ....*....|....*....|....*....
gi 15595995 122 LCSIAAPLPALGEMRRVLKRGGELLFCEH 150
Cdd:COG4976 117 LTYLGDLAAVFAGVARALKPGGLFIFSVE 145
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-147 8.95e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 69.62  E-value: 8.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    51 LEIGLGTGLNLgFYDAAKVSAIVGVDPAAQMQALARERAAQIGIP-VEMVALELGeirAEAESFDTIVCTFTLCSIAAPL 129
Cdd:pfam08241   1 LDVGCGTGLLT-ELLARLGARVTGVDISPEMLELAREKAPREGLTfVVGDAEDLP---FPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 15595995   130 PALGEMRRVLKRGGELLF 147
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 17-195 2.05e-15

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 70.53  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    17 YDRYVLPRLIDFacgmgdvmKQRSLLVPRAHGRVLEIGLGTGLNLGFYdAAKVSAIVGVDPAAQMQALARERAAQIGIPV 96
Cdd:pfam13489   1 YAHQRERLLADL--------LLRLLPKLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAIERALLNVRFDQFDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    97 EmvalelgEIRAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCEhgraPDASVLAWQRRLT-PWWKPLAGG 175
Cdd:pfam13489  72 Q-------EAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLST----PLASDEADRLLLEwPYLRPRNGH 140

                         170       180
                  ....*....|....*....|..
gi 15595995   176 CHLD--RDMPALLREAGFRIDE 195
Cdd:pfam13489 141 ISLFsaRSLKRLLEEAGFEVVS 162
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 44-190 1.35e-13

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 65.52  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    44 PRAHGRVLEIGLGTGlNLGFYDAAKV---SAIVGVDPAAQMQALARERAAQIGIpvEMVALELGEIRA-----EAESFDT 115
Cdd:pfam13847   1 IDKGMRVLDLGCGTG-HLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGF--DNVEFEQGDIEElpellEDDKFDV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595995   116 IVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCEHG--RAPDASVLAWQRRLTPWWKPLAGGCHLDRdmpaLLREAG 190
Cdd:pfam13847  78 VISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDslAELPAHVKEDSTYYAGCVGGAILKKKLYE----LLEEAG 150
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 17-148 4.69e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 62.63  E-value: 4.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  17 YDRYVLPRLIDFACGMGDVmkqrsllvpRAHGRVLEIGLGTGLNLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIP- 95
Cdd:COG0500   6 YSDELLPGLAALLALLERL---------PKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGn 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595995  96 VEMVALELGEIRA-EAESFDTIVCTFTLCSI--AAPLPALGEMRRVLKRGGELLFC 148
Cdd:COG0500  77 VEFLVADLAELDPlPAESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLS 132
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-145 3.72e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 57.76  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    51 LEIGLGTGLNLGFYDAAKV-SAIVGVDPAAQMQALARERAAQIGI--PVEMVALELGEIRAEAESFDTIVCTFTLCSIAA 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 15595995   128 PLPALGEMRRVLKRGGEL 145
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 17-149 1.03e-10

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: 59.20  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    17 YDRyvLPRLIDFacGMGDVMKQR--SLLVPRAHGRVLEIGLGTGlnlgfyD--------AAKVSAIVGVDPAAQMQALAR 86
Cdd:TIGR01934  12 YDL--LNDLLSF--GLHRLWRRRavKLIGVFKGQKVLDVACGTG------DlaielaksAPDRGKVTGVDFSSEMLEVAK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595995    87 ERAAQIGiPVEMV---ALELgeiRAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCE 149
Cdd:TIGR01934  82 KKSELPL-NIEFIqadAEAL---PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILE 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-147 1.68e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 1.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  40 SLLVPRAHGRVLEIGLGTGLNLgFYDAAKVSA-IVGVDPAAQMQALARERAAQIGIPvEMVALELGEIRA--EAESFDTI 116
Cdd:COG2230  45 RKLGLKPGMRVLDIGCGWGGLA-LYLARRYGVrVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRDlpADGQFDAI 122

                        90       100       110
                ....*....|....*....|....*....|...
gi 15595995 117 VCTFTLCSI-AAPLPA-LGEMRRVLKRGGELLF 147
Cdd:COG2230 123 VSIGMFEHVgPENYPAyFAKVARLLKPGGRLLL 155
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 13-149 3.28e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.16  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   13 FVGIYDRY-VLPRLIDFacGMGDVMKQ--RSLLVPRAHGRVLEIGLGTG-LNLGFYDAAKVSA-IVGVDPAAQMQALARE 87
Cdd:PRK00216  17 FDSIAPKYdLMNDLLSF--GLHRVWRRktIKWLGVRPGDKVLDLACGTGdLAIALAKAVGKTGeVVGLDFSEGMLAVGRE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595995   88 RAAQIGI--PVEMV---ALELGeirAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCE 149
Cdd:PRK00216  95 KLRDLGLsgNVEFVqgdAEALP---FPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILE 158
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-147 3.32e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.82  E-value: 3.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  46 AHGRVLEIGLGTG-LNLGFYDAAKVSAIVGVDPAAQMQALARERAAQigipVEMVALELGEIRAEaESFDTIVCTFTLCS 124
Cdd:COG4106   1 PPRRVLDLGCGTGrLTALLAERFPGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLDPP-EPFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|...
gi 15595995 125 IAAPLPALGEMRRVLKRGGELLF 147
Cdd:COG4106  76 LPDHAALLARLAAALAPGGVLAV 98
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
10-149 5.57e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.59  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    10 GESFVGIYDRYVLprlidfacgMGDVM----------KQRSLLVPRAHGRVLEIGLGTG-LNLGFYDAAKVSA-IVGVDP 77
Cdd:pfam01209   5 GDVFSSVASKYDL---------MNDVIsfgihrlwkdFTMKCMGVKRGNKFLDVAGGTGdWTFGLSDSAGSSGkVVGLDI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595995    78 AAQMQALARERAAQIG-IPVEMVALELGEIRAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLFCE 149
Cdd:pfam01209  76 NENMLKEGEKKAKEEGkYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLE 148
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-148 7.56e-07

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: 46.27  E-value: 7.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  49 RVLEIGLGTGLNLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPVemVALELGEIRA----EAESFDTIVCTFTLCS 124
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEElppeADESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|....*
gi 15595995 125 IAA-PLPALGEMRRVLKRGGELLFC 148
Cdd:cd02440  79 LVEdLARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 17-147 2.83e-05

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: 43.43  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    17 YDRY-VLPRLIDFAcgMGDVMKQRSLLVPRahgRVLEIGLGTG----LNLGFYDAAKVSAivgVDPAAQMQALARERaaq 91
Cdd:TIGR02072   9 YDRHaKIQREMAKR--LLALLKEKGIFIPA---SVLDIGCGTGyltrALLKRFPQAEFIA---LDISAGMLAQAKTK--- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595995    92 IGIPVEMVALELGEIRAEAESFDTIVCTFTLCSIAAPLPALGEMRRVLKRGGELLF 147
Cdd:TIGR02072  78 LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAF 133
arsM PRK11873
arsenite methyltransferase;
49-191 4.35e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 43.01  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   49 RVLEIGLGTGLNLgFYDAAKVSA---IVGVDPAAQMQALARERAAQIGIpvEMVALELGEIRA---EAESFDTIV--CTF 120
Cdd:PRK11873  80 TVLDLGSGGGFDC-FLAARRVGPtgkVIGVDMTPEMLAKARANARKAGY--TNVEFRLGEIEAlpvADNSVDVIIsnCVI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  121 TLcsiaAP--LPALGEMRRVLKRGGELLFCE---HGRAPDA---SVLAWqrrltpwwkplAG---GCHLDRDMPALLREA 189
Cdd:PRK11873 157 NL----SPdkERVFKEAFRVLKPGGRFAISDvvlRGELPEEirnDAELY-----------AGcvaGALQEEEYLAMLAEA 221


                 ..
gi 15595995  190 GF 191
Cdd:PRK11873 222 GF 223
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 44-118 1.11e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 41.67  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  44 PRAHGRVLEIGLGTGLnLGFYDAAKVSA--IVGVDPAAQMQALARERAAQIGIP--VEMVALELGEIRAE--AESFDTIV 117
Cdd:COG4123  35 VKKGGRVLDLGTGTGV-IALMLAQRSPGarITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFAAElpPGSFDLVV 113


                .
gi 15595995 118 C 118
Cdd:COG4123 114 S 114
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 49-135 2.17e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 40.98  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   49 RVLEIGLGTGLnLGFYDAAKVSAIVGVDPAAQMQALARERAAQIGIPvEMVALELGEIRAEAESFDTIVCTFTLcsIAAP 128
Cdd:PRK07580  66 RILDAGCGVGS-LSIPLARRGAKVVASDISPQMVEEARERAPEAGLA-GNITFEVGDLESLLGRFDTVVCLDVL--IHYP 141


                 ....*..
gi 15595995  129 LPALGEM 135
Cdd:PRK07580 142 QEDAARM 148
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 41-147 2.80e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.38  E-value: 2.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995  41 LLVPRAHGRVLEIGLGTGlnlgfYDAAKVSAIVG----VDPAAQMQALARERAAQIGIP-VEMVALELGEIRAEAESFDT 115
Cdd:COG2518  61 ALDLKPGDRVLEIGTGSG-----YQAAVLARLAGrvysVERDPELAERARERLAALGYDnVTVRVGDGALGWPEHAPFDR 135

                        90       100       110
                ....*....|....*....|....*....|..
gi 15595995 116 IVCTftlCSIAAPLPALGEMrrvLKRGGELLF 147
Cdd:COG2518 136 IIVT---AAAPEVPEALLEQ---LAPGGRLVA 161
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 42-137 4.02e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995    42 LVPRAHGRVLEIGLGTGLnLGFYDAAKVSAIVGVD--PAAQMqaLARERAAQIGIPVEMValelgeiraEAESFDTIVCT 119
Cdd:TIGR00537  15 LRELKPDDVLEIGAGTGL-VAIRLKGKGKCILTTDinPFAVK--ELRENAKLNNVGLDVV---------MTDLFKGVRGK 82

                          90
                  ....*....|....*....
gi 15595995   120 FTLCSIAAP-LPALGEMRR 137
Cdd:TIGR00537  83 FDVILFNPPyLPLEDDLRR 101
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 49-155 6.07e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.04  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595995   49 RVLEIGLGTGLNlGFYDAAKVSA-IVGVDPAAQMQALARERAAQIGIPVEMVALELGEIRAEAESFDTIVCTFTLCSIAA 127
Cdd:PLN02336 269 KVLDVGCGIGGG-DFYMAENFDVhVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQD 347

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15595995  128 PlPALgeMRRV---LKRGGELLFCEHGRAPD 155
Cdd:PLN02336 348 K-PAL--FRSFfkwLKPGGKVLISDYCRSPG 375
 
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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