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Conserved domains on  [gi|1002258550|ref|XP_015633611|]
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uncharacterized protein [Oryza sativa Japonica Group]

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; ...
 47-160 6.69e-22

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 pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 88.93  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  47 LWDSSLVLASHL----ASCVHHHHLRGATVLELGAGTGLPGIAAVACLGAARCVLTDVRPLLPGLRANADANGLTaEQAD 122
Cdd:pfam10294  21 VWDAAVVLSKYLemkiFKELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITDLEEALELLKKNIELNALS-SKVV 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002258550 123 VRELRWGGHLEPEV----QVDVVLMSDVFYDPDDMPAMADTL 160
Cdd:pfam10294 100 VKVLDWGENLPPDLfdghPVDLILAADCVYNEDSFPLLEKTL 141
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 47-160 6.69e-22

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 88.93  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  47 LWDSSLVLASHL----ASCVHHHHLRGATVLELGAGTGLPGIAAVACLGAARCVLTDVRPLLPGLRANADANGLTaEQAD 122
Cdd:pfam10294  21 VWDAAVVLSKYLemkiFKELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITDLEEALELLKKNIELNALS-SKVV 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002258550 123 VRELRWGGHLEPEV----QVDVVLMSDVFYDPDDMPAMADTL 160
Cdd:pfam10294 100 VKVLDWGENLPPDLfdghPVDLILAADCVYNEDSFPLLEKTL 141
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 47-161 2.39e-21

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 88.40  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  47 LWDSSLVLASHLAscvHHHHLRGATVLELGAGTGLPGIAAvACLGAARCVLTDVRPL-LPGLRANADANGLTAEqadVRE 125
Cdd:COG3897    52 LWPSGQALARYLL---DHPEVAGKRVLELGCGLGLVGIAA-AKAGAADVTATDYDPEaLAALRLNAALNGVAIT---TRL 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002258550 126 LRWGGhLEPEVQVDVVLMSDVFYDPDDMPAMADTLH 161
Cdd:COG3897   125 GDWRD-PPAAGGFDLILGGDVLYERDLAEPLLPFLD 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-165 6.10e-04

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: 38.18  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  71 TVLELGAGTGLPGIaAVACLGAARCVLTDVRP----LLPGLRANADANGLTAEQADVRELrwggHLEPEVQVDVVLMSDV 146
Cdd:cd02440     1 RVLDLGCGTGALAL-ALASGPGARVTGVDISPvaleLARKAAAALLADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                          90       100
                  ....*....|....*....|
gi 1002258550 147 F-YDPDDMPAMADTLHGLWR 165
Cdd:cd02440    76 LhHLVEDLARFLEEARRLLK 95
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 47-160 6.69e-22

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 88.93  E-value: 6.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  47 LWDSSLVLASHL----ASCVHHHHLRGATVLELGAGTGLPGIAAVACLGAARCVLTDVRPLLPGLRANADANGLTaEQAD 122
Cdd:pfam10294  21 VWDAAVVLSKYLemkiFKELGANNLSGLNVLELGSGTGLVGIAVALLLPGASVTITDLEEALELLKKNIELNALS-SKVV 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002258550 123 VRELRWGGHLEPEV----QVDVVLMSDVFYDPDDMPAMADTL 160
Cdd:pfam10294 100 VKVLDWGENLPPDLfdghPVDLILAADCVYNEDSFPLLEKTL 141
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 47-161 2.39e-21

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 88.40  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  47 LWDSSLVLASHLAscvHHHHLRGATVLELGAGTGLPGIAAvACLGAARCVLTDVRPL-LPGLRANADANGLTAEqadVRE 125
Cdd:COG3897    52 LWPSGQALARYLL---DHPEVAGKRVLELGCGLGLVGIAA-AKAGAADVTATDYDPEaLAALRLNAALNGVAIT---TRL 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1002258550 126 LRWGGhLEPEVQVDVVLMSDVFYDPDDMPAMADTLH 161
Cdd:COG3897   125 GDWRD-PPAAGGFDLILGGDVLYERDLAEPLLPFLD 159
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
54-143 3.29e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 52.21  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  54 LASHLascVHHHHLRG----ATVLELGAGTGLPGIAAvACLGAARCVLTDV-RPLLPGLRANADANGLTAE--QADVREL 126
Cdd:COG2263    30 LAAEL---LHLAYLRGdiegKTVLDLGCGTGMLAIGA-ALLGAKKVVGVDIdPEALEIARENAERLGVRVDfiRADVTRI 105

                          90
                  ....*....|....*..
gi 1002258550 127 RWGGHlepevqVDVVLM 143
Cdd:COG2263   106 PLGGS------VDTVVM 116
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 57-163 2.77e-05

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: 42.70  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  57 HLASCVHHHHLRGATVLELGAGTGLpGIAAVACLGaARCVLTDVRP-LLPGLRANADANGLTAEQADVRELRWGGHlepe 135
Cdd:COG2227    13 RLAALLARLLPAGGRVLDVGCGTGR-LALALARRG-ADVTGVDISPeALEIARERAAELNVDFVQGDLEDLPLEDG---- 86

                          90       100
                  ....*....|....*....|....*...
gi 1002258550 136 vQVDVVLMSDVFYDPDDMPAMADTLHGL 163
Cdd:COG2227    87 -SFDLVICSEVLEHLPDPAALLRELARL 113
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
67-142 4.20e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.62  E-value: 4.20e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002258550  67 LRGATVLELGAGTGLPGIAAvACLGAARCVLTDVRPL-LPGLRANADANGLtAEQADVRElrwgGHLEPEVQVDVVL 142
Cdd:COG2264   147 KPGKTVLDVGCGSGILAIAA-AKLGAKRVLAVDIDPVaVEAARENAELNGV-EDRIEVVL----GDLLEDGPYDLVV 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 72-161 7.20e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  72 VLELGAGTGLPGIAAVACLGaARCVLTDVRP-LLPGLRANADANGLTAE--QADVRELRwgghlEPEVQVDVVLMSDVFY 148
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG-ARVTGVDLSPeMLERARERAAEAGLNVEfvQGDAEDLP-----FPDGSFDLVVSSGVLH 74

                          90
                  ....*....|....*
gi 1002258550 149 --DPDDMPAMADTLH 161
Cdd:pfam13649  75 hlPDPDLEAALREIA 89
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
68-163 1.05e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.19  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  68 RGATVLELGAGTGLPGIAAVACLGAARCVLTDvrpLLPGL--RANADANGLTAEQADVRelrwggHLEPEVQVDVVLMSD 145
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVD---LSPEMlaRARARLPNVRFVVADLR------DLDPPEPFDLVVSNA 71

                          90
                  ....*....|....*...
gi 1002258550 146 VFYDPDDMPAMADTLHGL 163
Cdd:COG4106    72 ALHWLPDHAALLARLAAA 89
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 73-163 2.60e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.27  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  73 LELGAGTGLPGIAAVACLGAARCVLTDV--RPLLPGLRANADANGLTAEQADVRELRwgGHLEPEVQVDVVLMSDVFYDP 150
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIspAALEAARERLAALGLLNAVRVELFQLD--LGELDPGSFDVVVASNVLHHL 78

                          90
                  ....*....|...
gi 1002258550 151 DDMPAMADTLHGL 163
Cdd:pfam08242  79 ADPRAVLRNIRRL 91
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-165 6.10e-04

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: 38.18  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  71 TVLELGAGTGLPGIaAVACLGAARCVLTDVRP----LLPGLRANADANGLTAEQADVRELrwggHLEPEVQVDVVLMSDV 146
Cdd:cd02440     1 RVLDLGCGTGALAL-ALASGPGARVTGVDISPvaleLARKAAAALLADNVEVLKGDAEEL----PPEADESFDVIISDPP 75

                          90       100
                  ....*....|....*....|
gi 1002258550 147 F-YDPDDMPAMADTLHGLWR 165
Cdd:cd02440    76 LhHLVEDLARFLEEARRLLK 95
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 69-163 7.40e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.06  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002258550  69 GATVLELGAGTGLPGIAAVACLGaARCVLTDV-RPLLPGLRANADANGL----TAEQADVRELRWGGhlepevQVDVVLM 143
Cdd:COG2230    52 GMRVLDIGCGWGGLALYLARRYG-VRVTGVTLsPEQLEYARERAAEAGLadrvEVRLADYRDLPADG------QFDAIVS 124

                          90       100
                  ....*....|....*....|..
gi 1002258550 144 SDVFY--DPDDMPAMADTLHGL 163
Cdd:COG2230   125 IGMFEhvGPENYPAYFAKVARL 146
 
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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