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Conserved domains on  [gi|1958752027|ref|XP_038958777|]
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ATP synthase subunit C lysine N-methyltransferase isoform X2 [Rattus norvegicus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1006657)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG super family cl34436
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 9-53 1.09e-04

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


The actual alignment was detected with superfamily member COG2227:

Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 39.23  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAVGYELNPWLVWYSRYRAWREGVH 53
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD 72
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 9-105 8.83e-03

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 cd02440:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 107  Bit Score: 33.94  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAV-GYELNPWLVWYSRyRAWREGVHGSAKFYISDLWKVTFAQ-------YSNVVIFGVP 80
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVtGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEAdesfdviISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*
gi 1958752027  81 QMMPQLEKKLEFELEDGARVIACRF 105
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 9-53 1.09e-04

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: 39.23  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAVGYELNPWLVWYSRYRAWREGVH 53
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD 72
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 9-105 8.83e-03

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: 33.94  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAV-GYELNPWLVWYSRyRAWREGVHGSAKFYISDLWKVTFAQ-------YSNVVIFGVP 80
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVtGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEAdesfdviISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*
gi 1958752027  81 QMMPQLEKKLEFELEDGARVIACRF 105
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 9-53 1.09e-04

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: 39.23  E-value: 1.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAVGYELNPWLVWYSRYRAWREGVH 53
Cdd:COG2227    28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVD 72
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 9-79 5.95e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 34.91  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958752027   9 LVDIGSGDGRIVIAAAKA-GFPAVGYELNPWLVWYSRYRAWREGVHGSAKFYISDLWKVTF-AQYSNVVIFGV 79
Cdd:COG2230    55 VLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAdGQFDAIVSIGM 127
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 9-105 8.83e-03

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: 33.94  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752027   9 LVDIGSGDGRIVIAAAKAGFPAV-GYELNPWLVWYSRyRAWREGVHGSAKFYISDLWKVTFAQ-------YSNVVIFGVP 80
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVtGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEAdesfdviISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*
gi 1958752027  81 QMMPQLEKKLEFELEDGARVIACRF 105
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLV 105
 
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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