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Conserved domains on  [gi|74048545|ref|NP_001027563|]
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leucine carboxyl methyltransferase 1 isoform b [Homo sapiens]

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.-. ...
26-162 3.27e-30

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: 111.94  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    26 VRGTCEDASLCKRFAVsiGYWHDPYIQHFVR---------------------LSKERKAPEINRGYFARVHGVSQLIKAF 84
Cdd:pfam04072   2 LGVAAARALESRRPAD--PLIDDPFAEPLVRaagldlltrradgeldpakddPGKWARFPGLNDGIAVRTRFFDDFLLAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    85 LrKTECHCQIVNLGAGMDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIK----------------------------- 135
Cdd:pfam04072  80 L-AAAGIRQVVILGAGLDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAelgalppahrryvpvdlrdddwpealraa 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 74048545   136 -----LPTLLIAECVLVYMTPEQSANLLKWAA 162
Cdd:pfam04072 157 gfdpeQPTAWLAEGLLYYLPPEAQDALLDTIA 188
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
26-162 3.27e-30

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: 111.94  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    26 VRGTCEDASLCKRFAVsiGYWHDPYIQHFVR---------------------LSKERKAPEINRGYFARVHGVSQLIKAF 84
Cdd:pfam04072   2 LGVAAARALESRRPAD--PLIDDPFAEPLVRaagldlltrradgeldpakddPGKWARFPGLNDGIAVRTRFFDDFLLAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    85 LrKTECHCQIVNLGAGMDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIK----------------------------- 135
Cdd:pfam04072  80 L-AAAGIRQVVILGAGLDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAelgalppahrryvpvdlrdddwpealraa 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 74048545   136 -----LPTLLIAECVLVYMTPEQSANLLKWAA 162
Cdd:pfam04072 157 gfdpeQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
47-165 2.59e-11

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


Pssm-ID: 442544  Cd Length: 246  Bit Score: 62.29  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545  47 HDPYIQHFVR-----LSKERKAPEINRGYFARVHGVSQLIKAFLRktECHCQIVNLGAGMDTTFWRLKDEDLLpsKYFEV 121
Cdd:COG3315  10 RDPYAARLVGaigydFSRLLAGRGLRLGVAARTRFFDDLLRAALA--AGIAQVVILGAGLDTRAYRLDNPGGV--RWFEV 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74048545 122 DFPMIVTRK------------LHSI--------------------KLPTLLIAECVLVYMTPEQSANLLKWAANSF 165
Cdd:COG3315  86 DLPEVIALKrrllpelgpparLRLVavdlrdpdwpdalpaagfdpSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
93-164 2.14e-04

methyltransferase, TIGR00027 family; This model represents a set of probable methyltransferases, about 300 amino acids long, with essentially full length homology. Members share an N-terminal region described by Pfam model pfam02409. Included are a paralogous family of 12 proteins in Mycobacterium tuberculosis, plus close homologs in related species, a family of 8 in the archaeon Methanosarcina acetivorans, and small numbers of members in other species, including plants. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272862  Cd Length: 260  Bit Score: 41.92  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    93 QIVNLGAGMDTTFWRLkdEDLLPSKYFEVDFPMIVTRKLHSIK---------------------------------LPTL 139
Cdd:TIGR00027  84 QVVILGAGLDTRAYRL--PWPDGTRVFEVDQPAVLAFKEKVLAelgaeppahrravpvdlrqdwpaalaaagfdptAPTA 161
                          90       100
                  ....*....|....*....|....*.
gi 74048545   140 LIAECVLVYMTPEQSANLLKW-AANS 164
Cdd:TIGR00027 162 WLWEGLLMYLTEEAVDALLAFiAELS 187
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
26-162 3.27e-30

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: 111.94  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    26 VRGTCEDASLCKRFAVsiGYWHDPYIQHFVR---------------------LSKERKAPEINRGYFARVHGVSQLIKAF 84
Cdd:pfam04072   2 LGVAAARALESRRPAD--PLIDDPFAEPLVRaagldlltrradgeldpakddPGKWARFPGLNDGIAVRTRFFDDFLLAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    85 LrKTECHCQIVNLGAGMDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIK----------------------------- 135
Cdd:pfam04072  80 L-AAAGIRQVVILGAGLDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAelgalppahrryvpvdlrdddwpealraa 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 74048545   136 -----LPTLLIAECVLVYMTPEQSANLLKWAA 162
Cdd:pfam04072 157 gfdpeQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
47-165 2.59e-11

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


Pssm-ID: 442544  Cd Length: 246  Bit Score: 62.29  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545  47 HDPYIQHFVR-----LSKERKAPEINRGYFARVHGVSQLIKAFLRktECHCQIVNLGAGMDTTFWRLKDEDLLpsKYFEV 121
Cdd:COG3315  10 RDPYAARLVGaigydFSRLLAGRGLRLGVAARTRFFDDLLRAALA--AGIAQVVILGAGLDTRAYRLDNPGGV--RWFEV 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74048545 122 DFPMIVTRK------------LHSI--------------------KLPTLLIAECVLVYMTPEQSANLLKWAANSF 165
Cdd:COG3315  86 DLPEVIALKrrllpelgpparLRLVavdlrdpdwpdalpaagfdpSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
93-164 2.14e-04

methyltransferase, TIGR00027 family; This model represents a set of probable methyltransferases, about 300 amino acids long, with essentially full length homology. Members share an N-terminal region described by Pfam model pfam02409. Included are a paralogous family of 12 proteins in Mycobacterium tuberculosis, plus close homologs in related species, a family of 8 in the archaeon Methanosarcina acetivorans, and small numbers of members in other species, including plants. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272862  Cd Length: 260  Bit Score: 41.92  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74048545    93 QIVNLGAGMDTTFWRLkdEDLLPSKYFEVDFPMIVTRKLHSIK---------------------------------LPTL 139
Cdd:TIGR00027  84 QVVILGAGLDTRAYRL--PWPDGTRVFEVDQPAVLAFKEKVLAelgaeppahrravpvdlrqdwpaalaaagfdptAPTA 161
                          90       100
                  ....*....|....*....|....*.
gi 74048545   140 LIAECVLVYMTPEQSANLLKW-AANS 164
Cdd:TIGR00027 162 WLWEGLLMYLTEEAVDALLAFiAELS 187
 
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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