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Conserved domains on  [gi|2348119626|ref|XP_052141389|]
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uncharacterized protein LOC127761180 isoform X1 [Oryza glaberrima]

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; ...
 43-196 6.05e-19

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: 81.99  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  43 NHDLRvdIIENIEEDYGMFVWPCSVILAEYVWQ------QRSRFTASTVVELGAGTSLPGLVAAKV--GADVTLTDIAHN 114
Cdd:pfam10294   4 NPGLR--IEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626 115 TEVLN-NIrQVCGLNNvNCTVLGLTWGEWDEP-TFDLHP-DVILGADVLYDSAKFDDLFATVSFLLENSPGamFITTYHN 191
Cdd:pfam10294  82 LELLKkNI-ELNALSS-KVVVKVLDWGENLPPdLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKK 157


                  ....*
gi 2348119626 192 RRFQE 196
Cdd:pfam10294 158 RREAE 162
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 43-196 6.05e-19

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: 81.99  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  43 NHDLRvdIIENIEEDYGMFVWPCSVILAEYVWQ------QRSRFTASTVVELGAGTSLPGLVAAKV--GADVTLTDIAHN 114
Cdd:pfam10294   4 NPGLR--IEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626 115 TEVLN-NIrQVCGLNNvNCTVLGLTWGEWDEP-TFDLHP-DVILGADVLYDSAKFDDLFATVSFLLENSPGamFITTYHN 191
Cdd:pfam10294  82 LELLKkNI-ELNALSS-KVVVKVLDWGENLPPdLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKK 157


                  ....*
gi 2348119626 192 RRFQE 196
Cdd:pfam10294 158 RREAE 162
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 58-171 9.87e-17

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: 76.85  E-value: 9.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  58 YGMFVWPCSVILAEYVWQqRSRFTASTVVELGAGTSLPGLVAAKVGA-DVTLTDIahNTEVLNNIRQVCGLNNVNCTVLG 136
Cdd:COG3897    48 FWAFLWPSGQALARYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDY--DPEALAALRLNAALNGVAITTRL 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2348119626 137 LTWGEWDE-PTFDlhpdVILGADVLYDSAKFDDLFA 171
Cdd:COG3897   125 GDWRDPPAaGGFD----LILGGDVLYERDLAEPLLP 156
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-190 8.60e-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: 35.10  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  84 TVVELGAGTSLPGLVAAK-VGADVTLTDIahNTEVLNNIRQVC-GLNNVNCTVLGLTWGEWDEPTFDlHPDVILGADVLY 161
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDI--SPVALELARKAAaALLADNVEVLKGDAEELPPEADE-SFDVIISDPPLH 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2348119626 162 DSAK-FDDLFATVSFLLeNSPGAMFITTYH 190
Cdd:cd02440    78 HLVEdLARFLEEARRLL-KPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 43-196 6.05e-19

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: 81.99  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  43 NHDLRvdIIENIEEDYGMFVWPCSVILAEYVWQ------QRSRFTASTVVELGAGTSLPGLVAAKV--GADVTLTDIAHN 114
Cdd:pfam10294   4 NPGLR--IEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626 115 TEVLN-NIrQVCGLNNvNCTVLGLTWGEWDEP-TFDLHP-DVILGADVLYDSAKFDDLFATVSFLLENSPGamFITTYHN 191
Cdd:pfam10294  82 LELLKkNI-ELNALSS-KVVVKVLDWGENLPPdLFDGHPvDLILAADCVYNEDSFPLLEKTLKDLLGKESV--ILVAYKK 157


                  ....*
gi 2348119626 192 RRFQE 196
Cdd:pfam10294 158 RREAE 162
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 58-171 9.87e-17

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: 76.85  E-value: 9.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  58 YGMFVWPCSVILAEYVWQqRSRFTASTVVELGAGTSLPGLVAAKVGA-DVTLTDIahNTEVLNNIRQVCGLNNVNCTVLG 136
Cdd:COG3897    48 FWAFLWPSGQALARYLLD-HPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDY--DPEALAALRLNAALNGVAITTRL 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2348119626 137 LTWGEWDE-PTFDlhpdVILGADVLYDSAKFDDLFA 171
Cdd:COG3897   125 GDWRDPPAaGGFD----LILGGDVLYERDLAEPLLP 156
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-190 8.60e-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: 35.10  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2348119626  84 TVVELGAGTSLPGLVAAK-VGADVTLTDIahNTEVLNNIRQVC-GLNNVNCTVLGLTWGEWDEPTFDlHPDVILGADVLY 161
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDI--SPVALELARKAAaALLADNVEVLKGDAEELPPEADE-SFDVIISDPPLH 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2348119626 162 DSAK-FDDLFATVSFLLeNSPGAMFITTYH 190
Cdd:cd02440    78 HLVEdLARFLEEARRLL-KPGGVLVLTLVL 106
 
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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