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Conserved domains on  [gi|530408203|ref|XP_005255411|]
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leucine carboxyl methyltransferase 1 isoform X4 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 1-117 9.75e-21

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.).


The actual alignment was detected with superfamily member pfam04072:

Pssm-ID: 473071  Cd Length: 188  Bit Score: 85.75  E-value: 9.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408203    1 MDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIKCKPPLSSpilelhsedtlqmdghilDSKRYavIGADLRDlSELEE 80
Cdd:pfam04072  95 LDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAELGALPP------------------AHRRY--VPVDLRD-DDWPE 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530408203   81 KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAA 117
Cdd:pfam04072 152 ALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
 1-117 9.75e-21

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: 85.75  E-value: 9.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408203    1 MDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIKCKPPLSSpilelhsedtlqmdghilDSKRYavIGADLRDlSELEE 80
Cdd:pfam04072  95 LDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAELGALPP------------------AHRRY--VPVDLRD-DDWPE 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530408203   81 KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAA 117
Cdd:pfam04072 152 ALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
 1-120 1.80e-07

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


Pssm-ID: 442544  Cd Length: 246  Bit Score: 50.34  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408203   1 MDTTFWRLKDEDLLpsKYFEVDFP-MIVTRKLHSIKCKPPlsspilelhsedtlqmdghildsKRYAVIGADLRDLSeLE 79
Cdd:COG3315   67 LDTRAYRLDNPGGV--RWFEVDLPeVIALKRRLLPELGPP-----------------------ARLRLVAVDLRDPD-WP 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530408203  80 EKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSF 120
Cdd:COG3315  121 DALPAAGFDPSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
 67-119 4.90e-03

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: 37.29  E-value: 4.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530408203   67 VIGADLRDlsELEEKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKW-AANS 119
Cdd:TIGR00027 136 AVPVDLRQ--DWPAALAAAGFDPTAPTAWLWEGLLMYLTEEAVDALLAFiAELS 187
 
Name Accession Description Interval E-value
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
 1-117 9.75e-21

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: 85.75  E-value: 9.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408203    1 MDTTFWRLKDEDLLpsKYFEVDFPMIVTRKLHSIKCKPPLSSpilelhsedtlqmdghilDSKRYavIGADLRDlSELEE 80
Cdd:pfam04072  95 LDTRAYRLPWPAGT--RVFEVDQPDVLEFKRETLAELGALPP------------------AHRRY--VPVDLRD-DDWPE 151

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530408203   81 KLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAA 117
Cdd:pfam04072 152 ALRAAGFDPEQPTAWLAEGLLYYLPPEAQDALLDTIA 188
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
 1-120 1.80e-07

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


Pssm-ID: 442544  Cd Length: 246  Bit Score: 50.34  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530408203   1 MDTTFWRLKDEDLLpsKYFEVDFP-MIVTRKLHSIKCKPPlsspilelhsedtlqmdghildsKRYAVIGADLRDLSeLE 79
Cdd:COG3315   67 LDTRAYRLDNPGGV--RWFEVDLPeVIALKRRLLPELGPP-----------------------ARLRLVAVDLRDPD-WP 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530408203  80 EKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKWAANSF 120
Cdd:COG3315  121 DALPAAGFDPSRPTLFIAEGVLMYLTEEAVRALLRRIAALF 161
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
 67-119 4.90e-03

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: 37.29  E-value: 4.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530408203   67 VIGADLRDlsELEEKLKKCNMNTQLPTLLIAECVLVYMTPEQSANLLKW-AANS 119
Cdd:TIGR00027 136 AVPVDLRQ--DWPAALAAAGFDPTAPTAWLWEGLLMYLTEEAVDALLAFiAELS 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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