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Conserved domains on  [gi|15600650|ref|NP_254144|]
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hypothetical protein PA5457 [Pseudomonas aeruginosa PAO1]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 18604756)

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; similar to Mycobacterium tuberculosis S-adenosylmethionine-dependent methyltransferase Rv3030

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

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 ...
 33-156 2.15e-17

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: 76.59  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  33 DGWFRSETGELLAGFaIGAQDTLLDLGCGEGVATLFAARQGASVIFTDSEEDKVRSLAQQVEAVarrPFTGLVSDSDPLP 112
Cdd:COG2227   7 RDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 113 LRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:COG2227  83 LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
COG4627 super family cl44094
Predicted SAM-depedendent methyltransferase [General function prediction only];
106-226 2.21e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


The actual alignment was detected with superfamily member COG4627:

Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.70  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650 106 SDSDPLPLRDACADKLVCMEVLEHVANPA--RVMAELVRLGRPGAQYLLSVPDpvGEHL-QQGIAPADYFRAPNhihIFS 182
Cdd:COG4627  35 DLTDPLPFPDNSVDAIYSSHVLEHLDYEEapLALKECYRVLKPGGILRIVVPD--LEHVaRLYLAEYDAALDVA---ELR 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 183 RDDFARLVQDAGLVIEHRQASGFFWVMGMIFFWASERAAGRELG 226
Cdd:COG4627 110 LAGPIDPLGIILGERLAGLAARHSVLFRTGFTRLALTARRSAAG 153
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 33-156 2.15e-17

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: 76.59  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  33 DGWFRSETGELLAGFaIGAQDTLLDLGCGEGVATLFAARQGASVIFTDSEEDKVRSLAQQVEAVarrPFTGLVSDSDPLP 112
Cdd:COG2227   7 RDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 113 LRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:COG2227  83 LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-152 8.41e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.16  E-value: 8.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    56 LDLGCGEGVATLFAARQGASVIFTD-SEEdkvrSLAQQVEAVARRPFTGLVSDSDPLPLRDACADKLVCMEVLEHVANPA 134
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDiSPE----MLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 15600650   135 RVMAELVRLGRPGAQYLL 152
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 36-156 2.64e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 59.18  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650   36 FRSETGELLAgfaIGAQDTLLDLGCGEGV-ATLFAARQGAS--VIFTDSEEDKVrSLAQQVEAVARRPFTGLVSDSDPLP 112
Cdd:PRK08317   7 YRARTFELLA---VQPGDRVLDVGCGPGNdARELARRVGPEgrVVGIDRSEAML-ALAKERAAGLGPNVEFVRGDADGLP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15600650  113 LRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:PRK08317  83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTD 126
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 54-153 6.37e-10

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 58.07  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    54 TLLDLGCGEGVATLFAARQGASVIFTDseedkvrsLAQQVEAVARrpftgLVSDSDPLPLRDACA-------------DK 120
Cdd:TIGR01983  49 RVLDVGCGGGLLSEPLARLGANVTGID--------ASEENIEVAK-----LHAKKDPLQIDYRCTtvedlaekkagsfDV 115

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15600650   121 LVCMEVLEHVANPARVMAELVRLGRPGAQYLLS 153
Cdd:TIGR01983 116 VTCMEVLEHVPDPQAFIRACAQLLKPGGILFFS 148
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
106-226 2.21e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.70  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650 106 SDSDPLPLRDACADKLVCMEVLEHVANPA--RVMAELVRLGRPGAQYLLSVPDpvGEHL-QQGIAPADYFRAPNhihIFS 182
Cdd:COG4627  35 DLTDPLPFPDNSVDAIYSSHVLEHLDYEEapLALKECYRVLKPGGILRIVVPD--LEHVaRLYLAEYDAALDVA---ELR 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 183 RDDFARLVQDAGLVIEHRQASGFFWVMGMIFFWASERAAGRELG 226
Cdd:COG4627 110 LAGPIDPLGIILGERLAGLAARHSVLFRTGFTRLALTARRSAAG 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-154 2.55e-04

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: 39.72  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  54 TLLDLGCGEGVATLFAARQ-GASVIFTDSEEDKVRSLAQQVEAVARRPFTGLVSDS-DPLPLRDACADKLVCMEVLEH-V 130
Cdd:cd02440   1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHHlV 80

                        90       100
                ....*....|....*....|....
gi 15600650 131 ANPARVMAELVRLGRPGAQYLLSV 154
Cdd:cd02440  81 EDLARFLEEARRLLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 33-156 2.15e-17

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: 76.59  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  33 DGWFRSETGELLAGFaIGAQDTLLDLGCGEGVATLFAARQGASVIFTDSEEDKVRSLAQQVEAVarrPFTGLVSDSDPLP 112
Cdd:COG2227   7 RDFWDRRLAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLP 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 113 LRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:COG2227  83 LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 42-157 5.02e-17

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: 75.80  E-value: 5.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  42 ELLAGFAIGAQDTLLDLGCGEGVATLFAARQGASVIFTDSEEDKVRSLAQQVEAvARRPFTGLVSDSDPLPLRDACADKL 121
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAE-AGLNVEFVVGDAEDLPFPDGSFDLV 91

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15600650 122 VCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPDP 157
Cdd:COG2226  92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-152 8.41e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.16  E-value: 8.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    56 LDLGCGEGVATLFAARQGASVIFTD-SEEdkvrSLAQQVEAVARRPFTGLVSDSDPLPLRDACADKLVCMEVLEHVANPA 134
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDiSPE----MLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 15600650   135 RVMAELVRLGRPGAQYLL 152
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-199 2.89e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 68.99  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    54 TLLDLGCGEGVATLFAARQGASVIFTDSeedkvrsLAQQVEAVARRPFTGLVSDSDPLPLRDAcADKLVCMEVLEHVANP 133
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGFSVTGVDP-------SPIAIERALLNVRFDQFDEQEAAVPAGK-FDVIVAREVLEHVPDP 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600650   134 ARVMAELVRLGRPGAQYLLSVPDPVGEHLQQgiAPADYFRAPN--HIHIFSRDDFARLVQDAGLVIEH 199
Cdd:pfam13489  97 PALLRQIAALLKPGGLLLLSTPLASDEADRL--LLEWPYLRPRngHISLFSARSLKRLLEEAGFEVVS 162
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-147 1.81e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    56 LDLGCGEGVATLFAARQ-GASVIFTDSEEDKVRsLAQQVEAVARRPFTGLVSDSDPLPLRDACADKLVCMEVLEHVANP- 133
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLE-RARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*
gi 15600650   134 -ARVMAELVRLGRPG 147
Cdd:pfam13649  81 lEAALREIARVLKPG 95
PRK08317 PRK08317
hypothetical protein; Provisional
 36-156 2.64e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 59.18  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650   36 FRSETGELLAgfaIGAQDTLLDLGCGEGV-ATLFAARQGAS--VIFTDSEEDKVrSLAQQVEAVARRPFTGLVSDSDPLP 112
Cdd:PRK08317   7 YRARTFELLA---VQPGDRVLDVGCGPGNdARELARRVGPEgrVVGIDRSEAML-ALAKERAAGLGPNVEFVRGDADGLP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15600650  113 LRDACADKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:PRK08317  83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTD 126
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 54-153 6.37e-10

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 58.07  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    54 TLLDLGCGEGVATLFAARQGASVIFTDseedkvrsLAQQVEAVARrpftgLVSDSDPLPLRDACA-------------DK 120
Cdd:TIGR01983  49 RVLDVGCGGGLLSEPLARLGANVTGID--------ASEENIEVAK-----LHAKKDPLQIDYRCTtvedlaekkagsfDV 115

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15600650   121 LVCMEVLEHVANPARVMAELVRLGRPGAQYLLS 153
Cdd:TIGR01983 116 VTCMEVLEHVPDPQAFIRACAQLLKPGGILFFS 148
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-200 7.75e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 54.23  E-value: 7.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  42 ELLAGFAIGAQDTLLDLGCGEGVATLFAARQGASVIFTD-SEE--DKVRSLAQQVEAvarrpftgLVSDSDPLPLRDACA 118
Cdd:COG4976  37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDlSEEmlAKAREKGVYDRL--------LVADLADLAEPDGRF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650 119 DKLVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPDPVGEHlqqgiapaDYFRAPNHIHifsrddfaRLVQDAGLVIE 198
Cdd:COG4976 109 DLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSG--------RYAHSLDYVR--------DLLAAAGFEVP 172


                ..
gi 15600650 199 HR 200
Cdd:COG4976 173 GL 174
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 42-155 1.14e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  42 ELLAGFAIGAQDTLLDLGCGEGVATLFAARQ-GASVI-FTDSEE--DKVRSLAQqvEAVARRPFTGLVSDSDPLPLrDAC 117
Cdd:COG2230  42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRyGVRVTgVTLSPEqlEYARERAA--EAGLADRVEVRLADYRDLPA-DGQ 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15600650 118 ADKLVCMEVLEHV--ANPARVMAELVRLGRPGAQYLLSVP 155
Cdd:COG2230 119 FDAIVSIGMFEHVgpENYPAYFAKVARLLKPGGRLLLHTP 158
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 54-194 1.72e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.72  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    54 TLLDLGCGEGVATLFAA---RQGASVIFTDSEEDKVrSLAQQVeaVARRPFTGL---VSD--SDPLPLRDACADKLVCME 125
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAeelGPNAEVVGIDISEEAI-EKAREN--AQKLGFDNVefeQGDieELPELLEDDKFDVVISNC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600650   126 VLEHVANPARVMAELVRLGRPGAQYLLSVPDPVGEHLQQGIAPADYFRApNHIHIFSRDDFARLVQDAG 194
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAG-CVGGAILKKKLYELLEEAG 150
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 55-207 3.99e-07

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 50.50  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650   55 LLDLGCGEGVATLFAARQGASVIFTDSEEDKVRslaqqveaVARrpftgLVSDSDPLP--LRDACA------------DK 120
Cdd:PLN02396 135 FIDIGCGGGLLSEPLARMGATVTGVDAVDKNVK--------IAR-----LHADMDPVTstIEYLCTtaekladegrkfDA 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  121 LVCMEVLEHVANPARVMAELVRLGRPGAQYLLSVPDPVGEHLQQGIAPADYFR--APNHIHIFSR----DDFARLVQDAG 194
Cdd:PLN02396 202 VLSLEVIEHVANPAEFCKSLSALTIPNGATVLSTINRTMRAYASTIVGAEYILrwLPKGTHQWSSfvtpEELSMILQRAS 281

                        170
                 ....*....|...
gi 15600650  195 lvIEHRQASGFFW 207
Cdd:PLN02396 282 --VDVKEMAGFVY 292
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
54-154 6.88e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.04  E-value: 6.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  54 TLLDLGCGEGVATLFAARQ--GASVIFTDSEEDKVRSLAQQVEAVarrpfTGLVSDSDPLPLRDAcADKLVCMEVLEHVA 131
Cdd:COG4106   4 RVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNV-----RFVVADLRDLDPPEP-FDLVVSNAALHWLP 77

                        90       100
                ....*....|....*....|...
gi 15600650 132 NPARVMAELVRLGRPGAQYLLSV 154
Cdd:COG4106  78 DHAALLARLAAALAPGGVLAVQV 100
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
106-226 2.21e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.70  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650 106 SDSDPLPLRDACADKLVCMEVLEHVANPA--RVMAELVRLGRPGAQYLLSVPDpvGEHL-QQGIAPADYFRAPNhihIFS 182
Cdd:COG4627  35 DLTDPLPFPDNSVDAIYSSHVLEHLDYEEapLALKECYRVLKPGGILRIVVPD--LEHVaRLYLAEYDAALDVA---ELR 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15600650 183 RDDFARLVQDAGLVIEHRQASGFFWVMGMIFFWASERAAGRELG 226
Cdd:COG4627 110 LAGPIDPLGIILGERLAGLAARHSVLFRTGFTRLALTARRSAAG 153
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 33-156 2.72e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.14  E-value: 2.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  33 DGWFRSETGELLAGFAIGAQD-----TLLDLGCGEGVATL-FAARQGASVIFTDSEEDKVRSLAQQVEAVARRPFTGLVS 106
Cdd:COG0500   3 DSYYSDELLPGLAALLALLERlpkggRVLDLGCGTGRNLLaLAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVA 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15600650 107 D-SDPLPLRDACADKLVCMEVLEHV--ANPARVMAELVRLGRPGAQYLLSVPD 156
Cdd:COG0500  83 DlAELDPLPAESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLSASD 135
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 49-202 3.26e-05

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 43.60  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    49 IGAQDTLLDLGCGEGV--ATLFAARQGASVIFTDSEEDKVRSLAQQVEAVARRPFTGLVSdsdplpLRDACADKLVCMEV 126
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTllYLLKEEKGVDGYGIELDAAGVAECVAKGLYVIQGDLDEGLEH------FPDKSFDYVILSQT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650   127 LEHVANPARVMAELVRLGRpgaQYLLSVPD----------------PVGEHLqqgiaPADYFRAPNhIHIFSRDDFARLV 190
Cdd:pfam07021  85 LQATRNPREVLDEMLRIGR---RCIVSFPNfghwrvrwsllsrgrmPVTDLL-----PYTWYNTPN-IHFCTILDFEELC 155

                         170
                  ....*....|..
gi 15600650   191 QDAGLVIEHRQA 202
Cdd:pfam07021 156 EEQNLKIEDRAA 167
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 56-148 6.38e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.20  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650    56 LDLGCGEGVAT--LFAARQGASVIFTDSEEDKVRSLAQQVEAVARRPF---TGLVSDSDPLPLRDAcaDKLVCMEVLEHV 130
Cdd:pfam08242   1 LEIGCGTGTLLraLLEALPGLEYTGLDISPAALEAARERLAALGLLNAvrvELFQLDLGELDPGSF--DVVVASNVLHHL 78

                          90
                  ....*....|....*...
gi 15600650   131 ANPARVMAELVRLGRPGA 148
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-154 2.55e-04

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: 39.72  E-value: 2.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  54 TLLDLGCGEGVATLFAARQ-GASVIFTDSEEDKVRSLAQQVEAVARRPFTGLVSDS-DPLPLRDACADKLVCMEVLEH-V 130
Cdd:cd02440   1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAeELPPEADESFDVIISDPPLHHlV 80

                        90       100
                ....*....|....*....|....
gi 15600650 131 ANPARVMAELVRLGRPGAQYLLSV 154
Cdd:cd02440  81 EDLARFLEEARRLLKPGGVLVLTL 104
PLN02244 PLN02244
tocopherol O-methyltransferase
 53-152 6.77e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 40.50  E-value: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650   53 DTLLDLGCGEGVATLFAARQ-GASVI-FTDSEEDKVRSLAQQVEAVARRPFTGLVSDSDPLPLRDACADKLVCMEVLEHV 130
Cdd:PLN02244 120 KRIVDVGCGIGGSSRYLARKyGANVKgITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHM 199

                         90       100
                 ....*....|....*....|..
gi 15600650  131 ANPARVMAELVRLGRPGAQYLL 152
Cdd:PLN02244 200 PDKRKFVQELARVAAPGGRIII 221
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 47-152 1.32e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.86  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600650  47 FAIGAQ----------DTLLDLGCGE-GVATL-FAARQGASVIFTDSEEDKVRsLAQQVEAVArrpfTGLVSDSDP-LPL 113
Cdd:cd08261 145 LAIGAHavrragvtagDTVLVVGAGPiGLGVIqVAKARGARVIVVDIDDERLE-FARELGADD----TINVGDEDVaARL 219

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15600650 114 RDACADKLVCMeVLEHVANPArVMAELVRLGRPGAQYLL 152
Cdd:cd08261 220 RELTDGEGADV-VIDATGNPA-SMEEAVELVAHGGRVVL 256
 
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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