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Conserved domains on  [gi|1728993876|ref|XP_030334695|]
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methyltransferase-like protein 25 isoform X1 [Strigops habroptila]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614804)

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 Mus musculus tRNA N(3)-methylcytidine methyltransferase METTL6 isoform 3

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|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
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 329-420 5.16e-12

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 pfam13679:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 138  Bit Score: 63.36  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728993876 329 ELCAE--EKARRKMASLKakaskssesnlYFPLTSCITAETELSDIITDLEDC-MVVGLHTCGDLAANTLRIFTAKpEIK 405
Cdd:pfam13679  56 DTRAElvEKANALAQKLG-----------FNKRMSFLEGTIAGSTPVELPDRVdVVTALHACDTATDDALRFALAK-QAR 123

                          90
                  ....*....|....*
gi 1728993876 406 AVCSVGCCYHLLSEQ 420
Cdd:pfam13679 124 AIVLVPCCYHELAEQ 138
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 168-218 5.35e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.77  E-value: 5.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1728993876 168 VIDIGSGKGYLSSFLSMQYNLKVYGIDSSNTNTNGAHERNRKLKKHWRAYQ 218
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQ 51
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 329-420 5.16e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 63.36  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728993876 329 ELCAE--EKARRKMASLKakaskssesnlYFPLTSCITAETELSDIITDLEDC-MVVGLHTCGDLAANTLRIFTAKpEIK 405
Cdd:pfam13679  56 DTRAElvEKANALAQKLG-----------FNKRMSFLEGTIAGSTPVELPDRVdVVTALHACDTATDDALRFALAK-QAR 123

                          90
                  ....*....|....*
gi 1728993876 406 AVCSVGCCYHLLSEQ 420
Cdd:pfam13679 124 AIVLVPCCYHELAEQ 138
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 168-218 5.35e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.77  E-value: 5.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1728993876 168 VIDIGSGKGYLSSFLSMQYNLKVYGIDSSNTNTNGAHERNRKLKKHWRAYQ 218
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQ 51
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 329-420 5.16e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 63.36  E-value: 5.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728993876 329 ELCAE--EKARRKMASLKakaskssesnlYFPLTSCITAETELSDIITDLEDC-MVVGLHTCGDLAANTLRIFTAKpEIK 405
Cdd:pfam13679  56 DTRAElvEKANALAQKLG-----------FNKRMSFLEGTIAGSTPVELPDRVdVVTALHACDTATDDALRFALAK-QAR 123

                          90
                  ....*....|....*
gi 1728993876 406 AVCSVGCCYHLLSEQ 420
Cdd:pfam13679 124 AIVLVPCCYHELAEQ 138
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 168-218 5.35e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.77  E-value: 5.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1728993876 168 VIDIGSGKGYLSSFLSMQYNLKVYGIDSSNTNTNGAHERNRKLKKHWRAYQ 218
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQ 51
 
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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