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Conserved domains on  [gi|398365095|ref|NP_011102|]
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trans-aconitate 3-methyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11423066)

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 Saccharomyces cerevisiae trans-aconitate 3-methyltransferase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 25-147 3.18e-12

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


:

Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.17  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  25 FYKMIDEYHDGERKLL---------VDVGCGPGTATLQMAQelKPFEQIIGSDLSATMIKTAEviKEGSPDTYKNVSFKI 95
Cdd:COG0500    6 YSDELLPGLAALLALLerlpkggrvLDLGCGTGRNLLALAA--RFGGRVIGIDLSPEAIALAR--ARAAKAGLGNVEFLV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 398365095  96 SSSDDFKFLGADSVdkqkiDMITAVECAHWFDFE---KFQRSAYANLRKDGTIAI 147
Cdd:COG0500   82 ADLAELDPLPAESF-----DLVVAFGVLHHLPPEereALLRELARALKPGGVLLL 131
 
Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 25-147 3.18e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.17  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  25 FYKMIDEYHDGERKLL---------VDVGCGPGTATLQMAQelKPFEQIIGSDLSATMIKTAEviKEGSPDTYKNVSFKI 95
Cdd:COG0500    6 YSDELLPGLAALLALLerlpkggrvLDLGCGTGRNLLALAA--RFGGRVIGIDLSPEAIALAR--ARAAKAGLGNVEFLV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 398365095  96 SSSDDFKFLGADSVdkqkiDMITAVECAHWFDFE---KFQRSAYANLRKDGTIAI 147
Cdd:COG0500   82 ADLAELDPLPAESF-----DLVVAFGVLHHLPPEereALLRELARALKPGGVLLL 131
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 42-143 1.48e-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: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   42 DVGCGPGTATLQMAQELKpfEQIIGSDLSATMIKTAeviKEGSPDTYKNVSFKISSSDDFKFLGAdsvdkqKIDMITAVE 121
Cdd:pfam13649   3 DLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERA---RERAAEAGLNVEFVQGDAEDLPFPDG------SFDLVVSSG 71

                          90       100
                  ....*....|....*....|....*
gi 398365095  122 CAHWF---DFEKFQRSAYANLRKDG 143
Cdd:pfam13649  72 VLHHLpdpDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-150 3.84e-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: 47.81  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  40 LVDVGCGPGTATLQMAQelKPFEQIIGSDLSATMIKTAEVIKEGSPdtYKNVSFKISSSDDFKFLGADSVdkqkiDMITA 119
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALL--ADNVEVLKGDAEELPPEADESF-----DVIIS 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365095 120 VECAHWF--DFEKFQRSAYANLRKDGTIAIWGY 150
Cdd:cd02440   73 DPPLHHLveDLARFLEEARRLLKPGGVLVLTLV 105
PRK08317 PRK08317
hypothetical protein; Provisional
 34-110 6.04e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.39  E-value: 6.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365095  34 DGERKLlvDVGCGPGTATLQMAQELKPFEQIIGSDLSATMIKTAEVIKEGSPDtykNVSFKISSSDDFKFlGADSVD 110
Cdd:PRK08317  19 PGDRVL--DVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGP---NVEFVRGDADGLPF-PDGSFD 89
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 27-216 6.45e-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: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   27 KMIDEYHDGERKLLVDVGCGPGTATLQMAQELkPFEQIIGSDLSATMIKTAevikegspdtyknvsfKISSSDDFKFLGA 106
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRF-PQAEFIALDISAGMLAQA----------------KTKLSENVQFICG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  107 D----SVDKQKIDMITAVECAHWF-DFEKFQRSAYANLRKDGTIAIWGYADPIFpdyPEFDDLmievpYGKQGLgPYweq 181
Cdd:TIGR02072  88 DaeklPLEDSSFDLIVSNLALQWCdDLSQALSELARVLKPGGLLAFSTFGPGTL---HELRQS-----FGQHGL-RY--- 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 398365095  182 PGRSRLRNMLKDSHLDPELFHDIQVSYFcaEDVRD 216
Cdd:TIGR02072 156 LSLDELKALLKNSFELLTLEEELITLSF--DDPLD 188
 
Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 25-147 3.18e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.17  E-value: 3.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  25 FYKMIDEYHDGERKLL---------VDVGCGPGTATLQMAQelKPFEQIIGSDLSATMIKTAEviKEGSPDTYKNVSFKI 95
Cdd:COG0500    6 YSDELLPGLAALLALLerlpkggrvLDLGCGTGRNLLALAA--RFGGRVIGIDLSPEAIALAR--ARAAKAGLGNVEFLV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 398365095  96 SSSDDFKFLGADSVdkqkiDMITAVECAHWFDFE---KFQRSAYANLRKDGTIAI 147
Cdd:COG0500   82 ADLAELDPLPAESF-----DLVVAFGVLHHLPPEereALLRELARALKPGGVLLL 131
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 27-168 1.48e-11

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: 61.16  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  27 KMIDEYHDGERKLLVDVGCGPGTATLQMAQElkpFEQIIGSDLSATMIKTAeviKEGSPDTYKNVSFKISSSDDFKFlGA 106
Cdd:COG2226   13 ALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELA---RERAAEAGLNVEFVVGDAEDLPF-PD 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365095 107 DSVdkqkiDMITAVECAHWF-DFEKFQRSAYANLRKDGTIAIwgyADPIFPDYPEFDDLMIEV 168
Cdd:COG2226   86 GSF-----DLVISSFVLHHLpDPERALAEIARVLKPGGRLVV---VDFSPPDLAELEELLAEA 140
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 42-143 1.48e-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: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   42 DVGCGPGTATLQMAQELKpfEQIIGSDLSATMIKTAeviKEGSPDTYKNVSFKISSSDDFKFLGAdsvdkqKIDMITAVE 121
Cdd:pfam13649   3 DLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERA---RERAAEAGLNVEFVQGDAEDLPFPDG------SFDLVVSSG 71

                          90       100
                  ....*....|....*....|....*
gi 398365095  122 CAHWF---DFEKFQRSAYANLRKDG 143
Cdd:pfam13649  72 VLHHLpdpDLEAALREIARVLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 40-147 4.33e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.04  E-value: 4.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   40 LVDVGCGPGTATLQMAQELKPFEQIIGSDLSATMIKTAEVIKEGSPdtYKNVSFKISSSDDFKFLGADsvdkQKIDMITA 119
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLG--FDNVEFEQGDIEELPELLED----DKFDVVIS 80

                          90       100
                  ....*....|....*....|....*....
gi 398365095  120 VE-CAHWFDFEKFQRSAYANLRKDGTIAI 147
Cdd:pfam13847  81 NCvLNHIPDPDKVLQEILRVLKPGGRLII 109
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-148 7.39e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.21  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  41 VDVGCGPGTATLQMAQELkPFEQIIGSDLSATMIKTAEvikegspDTYKNVSFKISSSDDFKFlgadsvdKQKIDMITAV 120
Cdd:COG4106    6 LDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARAR-------ARLPNVRFVVADLRDLDP-------PEPFDLVVSN 70

                         90       100
                 ....*....|....*....|....*....
gi 398365095 121 ECAHWF-DFEKFQRSAYANLRKDGTIAIW 148
Cdd:COG4106   71 AALHWLpDHAALLARLAAALAPGGVLAVQ 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 24-147 1.12e-09

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: 55.41  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  24 DFYKMIDEYHDGERKLLvDVGCGPGTATLQMAQElkpFEQIIGSDLSATMIKTAeviKEGSPDTykNVSFKISSSDDFKF 103
Cdd:COG2227   13 RLAALLARLLPAGGRVL-DVGCGTGRLALALARR---GADVTGVDISPEALEIA---RERAAEL--NVDFVQGDLEDLPL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 398365095 104 LGadsvdkQKIDMITAVECAHWF-DFEKFQRSAYANLRKDGTIAI 147
Cdd:COG2227   84 ED------GSFDLVICSEVLEHLpDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-150 3.84e-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: 47.81  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  40 LVDVGCGPGTATLQMAQelKPFEQIIGSDLSATMIKTAEVIKEGSPdtYKNVSFKISSSDDFKFLGADSVdkqkiDMITA 119
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALL--ADNVEVLKGDAEELPPEADESF-----DVIIS 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 398365095 120 VECAHWF--DFEKFQRSAYANLRKDGTIAIWGY 150
Cdd:cd02440   73 DPPLHHLveDLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-147 5.69e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.89  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   41 VDVGCGPGTATLQMAQelkPFEQIIGSDLSATMIKTAEVIKEGSPdtyknVSFKISSSDDFKFlgADSvdkqKIDMITAV 120
Cdd:pfam08241   1 LDVGCGTGLLTELLAR---LGARVTGVDISPEMLELAREKAPREG-----LTFVVGDAEDLPF--PDN----SFDLVLSS 66

                          90       100
                  ....*....|....*....|....*...
gi 398365095  121 ECAHWF-DFEKFQRSAYANLRKDGTIAI 147
Cdd:pfam08241  67 EVLHHVeDPERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
27-147 6.90e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  27 KMIDEYHDGERKLLVDVGCGPGTATLQMAQElkpFEQIIGSDLSATMIKTAEvikegspdtYKNVSFKISSSDdfkfLGA 106
Cdd:COG4976   37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPR---GYRLTGVDLSEEMLAKAR---------EKGVYDRLLVAD----LAD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 398365095 107 DSVDKQKIDMITAVECAHWF-DFEKFQRSAYANLRKDGTIAI 147
Cdd:COG4976  101 LAEPDGRFDLIVAADVLTYLgDLAAVFAGVARALKPGGLFIF 142
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-145 1.90e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.74  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   41 VDVGCGPGTaTLQMAQELKPFEQIIGSDLSATMI-KTAEVIKEGSPDTYKNVsfkisssdDFKFLGADSVDKQKIDMITA 119
Cdd:pfam08242   1 LEIGCGTGT-LLRALLEALPGLEYTGLDISPAALeAARERLAALGLLNAVRV--------ELFQLDLGELDPGSFDVVVA 71

                          90       100
                  ....*....|....*....|....*..
gi 398365095  120 VECAHWF-DFEKFQRSAYANLRKDGTI 145
Cdd:pfam08242  72 SNVLHHLaDPRAVLRNIRRLLKPGGVL 98
PRK08317 PRK08317
hypothetical protein; Provisional
 34-110 6.04e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.39  E-value: 6.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365095  34 DGERKLlvDVGCGPGTATLQMAQELKPFEQIIGSDLSATMIKTAEVIKEGSPDtykNVSFKISSSDDFKFlGADSVD 110
Cdd:PRK08317  19 PGDRVL--DVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGP---NVEFVRGDADGLPF-PDGSFD 89
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 27-216 6.45e-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: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095   27 KMIDEYHDGERKLLVDVGCGPGTATLQMAQELkPFEQIIGSDLSATMIKTAevikegspdtyknvsfKISSSDDFKFLGA 106
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRF-PQAEFIALDISAGMLAQA----------------KTKLSENVQFICG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  107 D----SVDKQKIDMITAVECAHWF-DFEKFQRSAYANLRKDGTIAIWGYADPIFpdyPEFDDLmievpYGKQGLgPYweq 181
Cdd:TIGR02072  88 DaeklPLEDSSFDLIVSNLALQWCdDLSQALSELARVLKPGGLLAFSTFGPGTL---HELRQS-----FGQHGL-RY--- 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 398365095  182 PGRSRLRNMLKDSHLDPELFHDIQVSYFcaEDVRD 216
Cdd:TIGR02072 156 LSLDELKALLKNSFELLTLEEELITLSF--DDPLD 188
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 34-147 1.25e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.45  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  34 DGERklLVDVGCGPGTATLQMAQELKpfEQIIGSDLSATMIKTAE--VIKEGSPDtykNVSFKISSSDDFKFlgadsvdK 111
Cdd:COG2230   51 PGMR--VLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARerAAEAGLAD---RVEVRLADYRDLPA-------D 116

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 398365095 112 QKIDMITAVECAHWFDFEKFQ---RSAYANLRKDGTIAI 147
Cdd:COG2230  117 GQFDAIVSIGMFEHVGPENYPayfAKVARLLKPGGRLLL 155
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 30-110 3.93e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 41.05  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365095  30 DEYHDGERKLLVDVGCGPGTATLQMAQEL--KPFEQIIGSDLSATMIKTAEviKEgspdtYKNVSFKISSSDDFKFlgAD 107
Cdd:PRK11088  79 AERLDEKATALLDIGCGEGYYTHALADALpeITTMQLFGLDISKVAIKYAA--KR-----YPQVTFCVASSHRLPF--AD 149


                 ....
gi 398365095 108 -SVD 110
Cdd:PRK11088 150 qSLD 153
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 41-77 4.10e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 38.00  E-value: 4.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 398365095  41 VDVGCGPGTATlQMAQELKPFEQIIGSDLSATMIKTA 77
Cdd:PRK01683  36 VDLGCGPGNST-ELLVERWPAARITGIDSSPAMLAEA 71
 
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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