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Conserved domains on  [gi|216548560|ref|NP_057081|]
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methyltransferase-like protein 25B isoform 1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10616068)

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 methyltransferase-like protein 25B

CATH:  2.20.25.110
EC:  2.1.1.-
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
133-293 3.68e-31

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


:

Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 116.90  E-value: 3.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  133 KKQHEIRRLGELVKKLSDF----TGCTQVVDVGSGQGHLSRFMA-LGLGLMVKSIEGDQRLVERAQRLDQElLQALEKEE 207
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKElldeNGPITIVDHGAGKGYLGFILYyLKYGVRVYGIDTRAELVEKANALAQK-LGFNKRMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  208 KRNPQVVQTSPRHSPhhvvrwvdptalceelllplenpcqgRARLLLTGLHACGDLSVALLRHFScCPEVVALASVGCCY 287
Cdd:pfam13679  80 FLEGTIAGSTPVELP--------------------------DRVDVVTALHACDTATDDALRFAL-AKQARAIVLVPCCY 132

                  ....*.
gi 216548560  288 MKLSDP 293
Cdd:pfam13679 133 HELAEQ 138
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
133-293 3.68e-31

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 116.90  E-value: 3.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  133 KKQHEIRRLGELVKKLSDF----TGCTQVVDVGSGQGHLSRFMA-LGLGLMVKSIEGDQRLVERAQRLDQElLQALEKEE 207
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKElldeNGPITIVDHGAGKGYLGFILYyLKYGVRVYGIDTRAELVEKANALAQK-LGFNKRMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  208 KRNPQVVQTSPRHSPhhvvrwvdptalceelllplenpcqgRARLLLTGLHACGDLSVALLRHFScCPEVVALASVGCCY 287
Cdd:pfam13679  80 FLEGTIAGSTPVELP--------------------------DRVDVVTALHACDTATDDALRFAL-AKQARAIVLVPCCY 132

                  ....*.
gi 216548560  288 MKLSDP 293
Cdd:pfam13679 133 HELAEQ 138
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
139-199 7.80e-03

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: 36.53  E-value: 7.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 216548560 139 RRLGELVKKLSDFTGctQVVDVGSGQGHLSRFMAlGLGLMVKSIEGDQRLVERAQRLDQEL 199
Cdd:COG2227   12 RRLAALLARLLPAGG--RVLDVGCGTGRLALALA-RRGADVTGVDISPEALEIARERAAEL 69
 
Name Accession Description Interval E-value
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
133-293 3.68e-31

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 116.90  E-value: 3.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  133 KKQHEIRRLGELVKKLSDF----TGCTQVVDVGSGQGHLSRFMA-LGLGLMVKSIEGDQRLVERAQRLDQElLQALEKEE 207
Cdd:pfam13679   1 KKLHQVEHLAEFIAPLLKElldeNGPITIVDHGAGKGYLGFILYyLKYGVRVYGIDTRAELVEKANALAQK-LGFNKRMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 216548560  208 KRNPQVVQTSPRHSPhhvvrwvdptalceelllplenpcqgRARLLLTGLHACGDLSVALLRHFScCPEVVALASVGCCY 287
Cdd:pfam13679  80 FLEGTIAGSTPVELP--------------------------DRVDVVTALHACDTATDDALRFAL-AKQARAIVLVPCCY 132

                  ....*.
gi 216548560  288 MKLSDP 293
Cdd:pfam13679 133 HELAEQ 138
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
139-199 7.80e-03

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: 36.53  E-value: 7.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 216548560 139 RRLGELVKKLSDFTGctQVVDVGSGQGHLSRFMAlGLGLMVKSIEGDQRLVERAQRLDQEL 199
Cdd:COG2227   12 RRLAALLARLLPAGG--RVLDVGCGTGRLALALA-RRGADVTGVDISPEALEIARERAAEL 69
 
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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