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Conserved domains on  [gi|6320643|ref|NP_010723|]
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leucine carboxy methyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10513475)

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 Homo sapiens leucine carboxyl methyltransferase 1

CATH:  3.40.50.150
EC:  2.1.1.-
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
5-220 1.30e-27

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


:

Pssm-ID: 427692  Cd Length: 188  Bit Score: 106.55  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643      5 IQQTDYDALSCKLAAisVGYLPSSGLQRLSVDLSKKYteWHRSYLITLKKFsrrafgKVDKAMRSSFPVMNYGTYLRTVG 84
Cdd:pfam04072   2 LGVAAARALESRRPA--DPLIDDPFAEPLVRAAGLDL--LTRRADGELDPA------KDDPGKWARFPGLNDGIAVRTRF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643     85 IDAAILEFLVANEKVQVVNLGCGSDLRMLPLLQMfPHLAYVDIDYNESVELKNSILRESEILrislglskedtakspfLI 164
Cdd:pfam04072  72 FDDFLLAALAAAGIRQVVILGAGLDTRAYRLPWP-AGTRVFEVDQPDVLEFKRETLAELGAL----------------PP 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320643    165 DQGRYklAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHNNESQLLINTIM 220
Cdd:pfam04072 135 AHRRY--VPVDLRDDDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
5-220 1.30e-27

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 106.55  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643      5 IQQTDYDALSCKLAAisVGYLPSSGLQRLSVDLSKKYteWHRSYLITLKKFsrrafgKVDKAMRSSFPVMNYGTYLRTVG 84
Cdd:pfam04072   2 LGVAAARALESRRPA--DPLIDDPFAEPLVRAAGLDL--LTRRADGELDPA------KDDPGKWARFPGLNDGIAVRTRF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643     85 IDAAILEFLVANEKVQVVNLGCGSDLRMLPLLQMfPHLAYVDIDYNESVELKNSILRESEILrislglskedtakspfLI 164
Cdd:pfam04072  72 FDDFLLAALAAAGIRQVVILGAGLDTRAYRLPWP-AGTRVFEVDQPDVLEFKRETLAELGAL----------------PP 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320643    165 DQGRYklAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHNNESQLLINTIM 220
Cdd:pfam04072 135 AHRRY--VPVDLRDDDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
55-232 1.66e-09

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 57.28  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643   55 FSRRAFGKVDKAMR--SSFPVMNYGTYLRTVGIDAAILEFLVANEKvQVVNLGCGSD---LRmLPLLqmfPHLAYVDIDY 129
Cdd:COG3315  13 YAARLVGAIGYDFSrlLAGRGLRLGVAARTRFFDDLLRAALAAGIA-QVVILGAGLDtraYR-LDNP---GGVRWFEVDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643  130 NESVELKNSILRESEIlrislglskedtakspflidQGRYKLAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHN 209
Cdd:COG3315  88 PEVIALKRRLLPELGP--------------------PARLRLVAVDLRDPDWPDALPAAGFDPSRPTLFIAEGVLMYLTE 147
                       170       180
                ....*....|....*....|...
gi 6320643  210 NESQLLINTIMSKFSHGLWISYD 232
Cdd:COG3315 148 EAVRALLRRIAALFPPGSELAFD 170
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
5-220 1.30e-27

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 106.55  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643      5 IQQTDYDALSCKLAAisVGYLPSSGLQRLSVDLSKKYteWHRSYLITLKKFsrrafgKVDKAMRSSFPVMNYGTYLRTVG 84
Cdd:pfam04072   2 LGVAAARALESRRPA--DPLIDDPFAEPLVRAAGLDL--LTRRADGELDPA------KDDPGKWARFPGLNDGIAVRTRF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643     85 IDAAILEFLVANEKVQVVNLGCGSDLRMLPLLQMfPHLAYVDIDYNESVELKNSILRESEILrislglskedtakspfLI 164
Cdd:pfam04072  72 FDDFLLAALAAAGIRQVVILGAGLDTRAYRLPWP-AGTRVFEVDQPDVLEFKRETLAELGAL----------------PP 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320643    165 DQGRYklAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHNNESQLLINTIM 220
Cdd:pfam04072 135 AHRRY--VPVDLRDDDWPEALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
55-232 1.66e-09

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 57.28  E-value: 1.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643   55 FSRRAFGKVDKAMR--SSFPVMNYGTYLRTVGIDAAILEFLVANEKvQVVNLGCGSD---LRmLPLLqmfPHLAYVDIDY 129
Cdd:COG3315  13 YAARLVGAIGYDFSrlLAGRGLRLGVAARTRFFDDLLRAALAAGIA-QVVILGAGLDtraYR-LDNP---GGVRWFEVDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320643  130 NESVELKNSILRESEIlrislglskedtakspflidQGRYKLAACDLNDITETTRLLDVCTKREIPTIVISECLLCYMHN 209
Cdd:COG3315  88 PEVIALKRRLLPELGP--------------------PARLRLVAVDLRDPDWPDALPAAGFDPSRPTLFIAEGVLMYLTE 147
                       170       180
                ....*....|....*....|...
gi 6320643  210 NESQLLINTIMSKFSHGLWISYD 232
Cdd:COG3315 148 EAVRALLRRIAALFPPGSELAFD 170
 
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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