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Conserved domains on  [gi|398365487|ref|NP_010368|]
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25S rRNA (adenine645-N1)-methyltransferase [Saccharomyces cerevisiae S288C]

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; ...
117-392 2.08e-69

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 pfam05148:

Pssm-ID: 473071  Cd Length: 214  Bit Score: 217.76  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  117 MMAKLTGSRFRWINEQLYTISSDEALKLIKEQPQLFDEYHDGFRSQVQAWPENPVDVFVDQIRYRcmkpvnapgglPGlk 196
Cdd:pfam05148   1 MKKRLDGGRFRMLNEKLYTGKGSRAGDLFKEDPDAFDLYHEGFNLQVKKWPVNPLDVIIRKLKRR-----------PG-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  197 dskEIVIADMGCGEAQLALEINNFfknynkkakkylkrrHKVHSFDLKKANERITVADIRNVPLPDESCTIVVFCLALMG 276
Cdd:pfam05148  68 ---NGVIADLGCGEARIAFRKREF---------------ENVHSFDLVAVNKRVIPCDMARVPLEDESVDVAVFCLSLMG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  277 TNFLDFIKEAYRILAPRGELWIAEIKSRFSDGKgnEFVDALKLMGFFHKKTFDENKMFTRFEFFKppaeiIEERRQKLER 356
Cdd:pfam05148 130 TNIADFLKEANRILKNGGLLKIAEVRSRFPSVG--LFERAFTKLGFEVEHVDLSNAQFVLFEFQK-----TSRVGPKRLL 202
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 398365487  357 RQKfievetekeelekkrrkiaegkwlLKPCIYKRR 392
Cdd:pfam05148 203 GLK------------------------LVPCLYKKR 214
 
Name Accession Description Interval E-value
Methyltransf_8 pfam05148
Hypothetical methyltransferase; This family consists of several uncharacterized eukaryotic ...
117-392 2.08e-69

Hypothetical methyltransferase; This family consists of several uncharacterized eukaryotic proteins which are related to methyltransferases pfam01209.


Pssm-ID: 398698  Cd Length: 214  Bit Score: 217.76  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  117 MMAKLTGSRFRWINEQLYTISSDEALKLIKEQPQLFDEYHDGFRSQVQAWPENPVDVFVDQIRYRcmkpvnapgglPGlk 196
Cdd:pfam05148   1 MKKRLDGGRFRMLNEKLYTGKGSRAGDLFKEDPDAFDLYHEGFNLQVKKWPVNPLDVIIRKLKRR-----------PG-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  197 dskEIVIADMGCGEAQLALEINNFfknynkkakkylkrrHKVHSFDLKKANERITVADIRNVPLPDESCTIVVFCLALMG 276
Cdd:pfam05148  68 ---NGVIADLGCGEARIAFRKREF---------------ENVHSFDLVAVNKRVIPCDMARVPLEDESVDVAVFCLSLMG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  277 TNFLDFIKEAYRILAPRGELWIAEIKSRFSDGKgnEFVDALKLMGFFHKKTFDENKMFTRFEFFKppaeiIEERRQKLER 356
Cdd:pfam05148 130 TNIADFLKEANRILKNGGLLKIAEVRSRFPSVG--LFERAFTKLGFEVEHVDLSNAQFVLFEFQK-----TSRVGPKRLL 202
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 398365487  357 RQKfievetekeelekkrrkiaegkwlLKPCIYKRR 392
Cdd:pfam05148 203 GLK------------------------LVPCLYKKR 214
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
195-322 3.37e-11

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 60.78  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487 195 LKDSKEIVIADMGCGEAQLALEInnffknynkkakkyLKRRHKVHSFD-----LKKANERIT---------VADIRNVPL 260
Cdd:COG2226   18 LGLRPGARVLDLGCGTGRLALAL--------------AERGARVTGVDispemLELARERAAeaglnvefvVGDAEDLPF 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365487 261 PDESCTIVVFCLALMgtNFLD---FIKEAYRILAPRGELWIAEiksrFSDGKGNEFVDALKLMGF 322
Cdd:COG2226   84 PDGSFDLVISSFVLH--HLPDperALAEIARVLKPGGRLVVVD----FSPPDLAELEELLAEAGF 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
243-298 7.20e-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: 35.87  E-value: 7.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398365487 243 LKKANERITVADIRNVPL-PDESCTIVVFCLALMG--TNFLDFIKEAYRILAPRGELWI 298
Cdd:cd02440   44 LLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlvEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
Methyltransf_8 pfam05148
Hypothetical methyltransferase; This family consists of several uncharacterized eukaryotic ...
117-392 2.08e-69

Hypothetical methyltransferase; This family consists of several uncharacterized eukaryotic proteins which are related to methyltransferases pfam01209.


Pssm-ID: 398698  Cd Length: 214  Bit Score: 217.76  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  117 MMAKLTGSRFRWINEQLYTISSDEALKLIKEQPQLFDEYHDGFRSQVQAWPENPVDVFVDQIRYRcmkpvnapgglPGlk 196
Cdd:pfam05148   1 MKKRLDGGRFRMLNEKLYTGKGSRAGDLFKEDPDAFDLYHEGFNLQVKKWPVNPLDVIIRKLKRR-----------PG-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  197 dskEIVIADMGCGEAQLALEINNFfknynkkakkylkrrHKVHSFDLKKANERITVADIRNVPLPDESCTIVVFCLALMG 276
Cdd:pfam05148  68 ---NGVIADLGCGEARIAFRKREF---------------ENVHSFDLVAVNKRVIPCDMARVPLEDESVDVAVFCLSLMG 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  277 TNFLDFIKEAYRILAPRGELWIAEIKSRFSDGKgnEFVDALKLMGFFHKKTFDENKMFTRFEFFKppaeiIEERRQKLER 356
Cdd:pfam05148 130 TNIADFLKEANRILKNGGLLKIAEVRSRFPSVG--LFERAFTKLGFEVEHVDLSNAQFVLFEFQK-----TSRVGPKRLL 202
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 398365487  357 RQKfievetekeelekkrrkiaegkwlLKPCIYKRR 392
Cdd:pfam05148 203 GLK------------------------LVPCLYKKR 214
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
195-322 3.37e-11

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 60.78  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487 195 LKDSKEIVIADMGCGEAQLALEInnffknynkkakkyLKRRHKVHSFD-----LKKANERIT---------VADIRNVPL 260
Cdd:COG2226   18 LGLRPGARVLDLGCGTGRLALAL--------------AERGARVTGVDispemLELARERAAeaglnvefvVGDAEDLPF 83
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365487 261 PDESCTIVVFCLALMgtNFLD---FIKEAYRILAPRGELWIAEiksrFSDGKGNEFVDALKLMGF 322
Cdd:COG2226   84 PDGSFDLVISSFVLH--HLPDperALAEIARVLKPGGRLVVVD----FSPPDLAELEELLAEAGF 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
205-298 3.02e-08

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 50.74  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  205 DMGCGEAQLALEInnffknynkkakkyLKRRHKVHSFD-----LKKANERIT-------VADIRNVPLPDESCTIVVFCL 272
Cdd:pfam08241   2 DVGCGTGLLTELL--------------ARLGARVTGVDispemLELAREKAPregltfvVGDAEDLPFPDNSFDLVLSSE 67
                          90       100
                  ....*....|....*....|....*..
gi 398365487  273 ALMGTNFLD-FIKEAYRILAPRGELWI 298
Cdd:pfam08241  68 VLHHVEDPErALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
203-294 4.13e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487  203 IADMGCGEAQLALEINNFFKnynkkakkylkrrHKVHSFD-----LKKANERIT---------VADIRNVPLPDESCTIV 268
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-------------ARVTGVDlspemLERARERAAeaglnvefvQGDAEDLPFPDGSFDLV 67
                          90       100
                  ....*....|....*....|....*....
gi 398365487  269 VFCLALMGTNFLD---FIKEAYRILAPRG 294
Cdd:pfam13649  68 VSSGVLHHLPDPDleaALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
203-299 2.43e-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: 40.77  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365487 203 IADMGCGEAQLALEinnffknynkkakkyLKRR-HKVHSFD-----LKKANER-------ITVADIRNVPLPDESCTIVV 269
Cdd:COG2227   28 VLDVGCGTGRLALA---------------LARRgADVTGVDispeaLEIARERaaelnvdFVQGDLEDLPLEDGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 398365487 270 FCLALMG-TNFLDFIKEAYRILAPRGELWIA 299
Cdd:COG2227   93 CSEVLEHlPDPAALLRELARLLKPGGLLLLS 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
243-298 7.20e-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: 35.87  E-value: 7.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398365487 243 LKKANERITVADIRNVPL-PDESCTIVVFCLALMG--TNFLDFIKEAYRILAPRGELWI 298
Cdd:cd02440   44 LLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlvEDLARFLEEARRLLKPGGVLVL 102
 
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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