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Conserved domains on  [gi|56121880|gb|AAV74221|]
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At5g44450 [Arabidopsis thaliana]

Protein Classification

N-terminal Xaa-Pro-Lys N-methyltransferase 1( domain architecture ID 10531238)

N-terminal Xaa-Pro-Lys N-methyltransferase 1, also called alpha N-terminal protein methyltransferase 1, is a class I SAM-dependent methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 31-253 1.75e-136

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


:

Pssm-ID: 461771  Cd Length: 218  Bit Score: 383.65  E-value: 1.75e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    31 KKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVnnvGANQHLVALDCGSGIGRITKNLLIRY 110
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLP---GKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   111 FNEVDLLEPVAQFLDAARENLasaGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPG 190
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYL---AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPN 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56121880   191 GFFVVKENLAKNGF-VLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALT 253
Cdd:pfam05891 155 GFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 31-253 1.75e-136

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


Pssm-ID: 461771  Cd Length: 218  Bit Score: 383.65  E-value: 1.75e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    31 KKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVnnvGANQHLVALDCGSGIGRITKNLLIRY 110
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLP---GKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   111 FNEVDLLEPVAQFLDAARENLasaGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPG 190
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYL---AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPN 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56121880   191 GFFVVKENLAKNGF-VLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALT 253
Cdd:pfam05891 155 GFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 92-195 6.56e-12

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: 61.19  E-value: 6.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  92 ALDCGSGIGRITKnLLIRYFNEVDLLEPVAQFLDAARENLASAGsethkaTNFFCVPLQEFTPAAGRYDVIWVQWCIGHL 171
Cdd:COG2227  28 VLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELN------VDFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                        90       100
                ....*....|....*....|....
gi 56121880 172 TdnDFVSFFNRAKGYLKPGGFFVV 195
Cdd:COG2227 101 P--DPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 93-196 6.83e-07

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: 47.04  E-value: 6.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  93 LDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSEThkaTNFFCVPLQEFTPAA-GRYDVIWVQWCIGHL 171
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN---VEVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*
gi 56121880 172 TDnDFVSFFNRAKGYLKPGGFFVVK 196
Cdd:cd02440  80 VE-DLARFLEEARRLLKPGGVLVLT 103
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 93-244 9.00e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 9.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   93 LDCGSGIGRITKNLLIRYFN--EVDLLEPVAqfldaaRENLASAGSetHKATNFFC--VPLQEFTPAAGRYDVIWVQWCI 168
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQviALDFIESVI------KKNESINGH--YKNVKFMCadVTSPDLNISDGSVDLIFSNWLL 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56121880  169 GHLTDNDFVSFFNRAKGYLKPGGFFVVKEN-LAKNGFVLDKEDHSITRSDPYFKQLFRQCglhlyRTKDQKGLPQEL 244
Cdd:PLN02336 114 MYLSDKEVENLAERMVKWLKVGGYIFFREScFHQSGDSKRKNNPTHYREPRFYTKVFKEC-----HTRDEDGNSFEL 185
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 31-253 1.75e-136

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


Pssm-ID: 461771  Cd Length: 218  Bit Score: 383.65  E-value: 1.75e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    31 KKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVnnvGANQHLVALDCGSGIGRITKNLLIRY 110
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLP---GKNRHLVALDCGAGIGRVTKNLLLPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   111 FNEVDLLEPVAQFLDAARENLasaGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPG 190
Cdd:pfam05891  78 FSKVDLVEPVEDFIEKAKEYL---AEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPN 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56121880   191 GFFVVKENLAKNGF-VLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALT 253
Cdd:pfam05891 155 GFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 93-191 2.40e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.90  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    93 LDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHkatnFFCVPLQEFTPAAGRYDVIWVQWCIGHLT 172
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE----FVQGDAEDLPFPDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 56121880   173 DNDFVSFFNRAKGYLKPGG 191
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 92-195 6.56e-12

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: 61.19  E-value: 6.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  92 ALDCGSGIGRITKnLLIRYFNEVDLLEPVAQFLDAARENLASAGsethkaTNFFCVPLQEFTPAAGRYDVIWVQWCIGHL 171
Cdd:COG2227  28 VLDVGCGTGRLAL-ALARRGADVTGVDISPEALEIARERAAELN------VDFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                        90       100
                ....*....|....*....|....
gi 56121880 172 TdnDFVSFFNRAKGYLKPGGFFVV 195
Cdd:COG2227 101 P--DPAALLRELARLLKPGGLLLL 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
75-232 2.04e-10

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.47  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  75 LLQERLVNNVGANQHLVALDCGSGIGRITKnLLIRYFNEVDLLEPVAQFLDAARENLASAgsethkatNFFCVPLQEFTP 154
Cdd:COG4976  33 LLAEELLARLPPGPFGRVLDLGCGTGLLGE-ALRPRGYRLTGVDLSEEMLAKAREKGVYD--------RLLVADLADLAE 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880 155 AAGRYDVIWVQWCIGHLtdNDFVSFFNRAKGYLKPGGFFVvkenlakngFVLDKED--HSITRSDPYFKQLFRQCGLHLY 232
Cdd:COG4976 104 PDGRFDLIVAADVLTYL--GDLAAVFAGVARALKPGGLFI---------FSVEDADgsGRYAHSLDYVRDLLAAAGFEVP 172
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
92-195 1.06e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.44  E-value: 1.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  92 ALDCGSGIGRITKNLLIRYFN-EVDLLEPVAQFLDAARENLASAgsethkatNFFCVPLQEFTPaAGRYDVIWVQWCIGH 170
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFPGaRVTGVDLSPEMLARARARLPNV--------RFVVADLRDLDP-PEPFDLVVSNAALHW 75

                        90       100
                ....*....|....*....|....*
gi 56121880 171 LtdNDFVSFFNRAKGYLKPGGFFVV 195
Cdd:COG4106  76 L--PDHAALLARLAAALAPGGVLAV 98
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-195 1.68e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.82  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    93 LDCGSGIGRITKnLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHKAtNFFCVPLQEftpaaGRYDVIWVQWCIGHLt 172
Cdd:pfam08241   1 LDVGCGTGLLTE-LLARLGARVTGVDISPEMLELAREKAPREGLTFVVG-DAEDLPFPD-----NSFDLVLSSEVLHHV- 72

                          90       100
                  ....*....|....*....|...
gi 56121880   173 dNDFVSFFNRAKGYLKPGGFFVV 195
Cdd:pfam08241  73 -EDPERALREIARVLKPGGILII 94
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 76-204 2.63e-09

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: 54.61  E-value: 2.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  76 LQERLVNNVGANQHLVALDCGSGIGRITKnLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHkatnFFCVPLQEFTPA 155
Cdd:COG2226  10 GREALLAALGLRPGARVLDLGCGTGRLAL-ALAERGARVTGVDISPEMLELARERAAEAGLNVE----FVVGDAEDLPFP 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880 156 AGRYDVIWVQWCIGHLTdnDFVSFFNRAKGYLKPGGFFVV-----------KENLAKNGF 204
Cdd:COG2226  85 DGSFDLVISSFVLHHLP--DPERALAEIARVLKPGGRLVVvdfsppdlaelEELLAEAGF 142
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-193 2.11e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.13  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    93 LDCGSGIGRITKNLL-IRYFNEVDLLEPVAQFLDAARENLASAGSETHKATNFFcvPLQEFTPAAGRYDVIWVQWCIGHL 171
Cdd:pfam08242   1 LEIGCGTGTLLRALLeALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELF--QLDLGELDPGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 56121880   172 tdNDFVSFFNRAKGYLKPGGFF 193
Cdd:pfam08242  79 --ADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 93-196 6.83e-07

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: 47.04  E-value: 6.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  93 LDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSEThkaTNFFCVPLQEFTPAA-GRYDVIWVQWCIGHL 171
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADN---VEVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*
gi 56121880 172 TDnDFVSFFNRAKGYLKPGGFFVVK 196
Cdd:cd02440  80 VE-DLARFLEEARRLLKPGGVLVLT 103
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 93-195 4.75e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  93 LDCGSGIGRitknlLIRYFNE--------VDLlepVAQFLDAARENLASAGSEtHKATnFFCVPLQEFtPAAGRYDVIWV 164
Cdd:COG2230  56 LDIGCGWGG-----LALYLARrygvrvtgVTL---SPEQLEYARERAAEAGLA-DRVE-VRLADYRDL-PADGQFDAIVS 124

                        90       100       110
                ....*....|....*....|....*....|.
gi 56121880 165 QWCIGHLTDNDFVSFFNRAKGYLKPGGFFVV 195
Cdd:COG2230 125 IGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 92-195 1.27e-05

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 44.91  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880  92 ALDCGSGIGRITkNLLIRYFNE----VDLlEPVAqfLDAARENLASAGsetHKATNFFCVPLQEFTP-AAGRYDVIWVQW 166
Cdd:COG0500  30 VLDLGCGTGRNL-LALAARFGGrvigIDL-SPEA--IALARARAAKAG---LGNVEFLVADLAELDPlPAESFDLVVAFG 102

                        90       100
                ....*....|....*....|....*....
gi 56121880 167 CIGHLTDNDFVSFFNRAKGYLKPGGFFVV 195
Cdd:COG0500 103 VLHHLPPEEREALLRELARALKPGGVLLL 131
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 93-232 7.53e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 39.33  E-value: 7.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    93 LDCGSGIGRITKNLLIRYFnEVDLLEPVAQFLDAARENLasagsethkatNFFCVPLQEFTPAAGRYDVIwVQW-CIGHL 171
Cdd:pfam13489  27 LDFGCGTGIFLRLLRAQGF-SVTGVDPSPIAIERALLNV-----------RFDQFDEQEAAVPAGKFDVI-VAReVLEHV 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   172 tdNDFVSFFNRAKGYLKPGGFFVVKENLA---------KNGFVLDKEDHSITRSDPYFKQLFRQCGLHLY 232
Cdd:pfam13489  94 --PDPPALLRQIAALLKPGGLLLLSTPLAsdeadrlllEWPYLRPRNGHISLFSARSLKRLLEEAGFEVV 161
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 66-195 8.47e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 39.11  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880    66 IGSEVFLKTLlQERLVNNVganqhlvaLDCGSGIGRITKNLLIRY-FNEVDLLEPVAQFLDAARENLASAGsetHKATNF 144
Cdd:pfam05175  18 IGSRLLLEHL-PKDLSGKV--------LDLGCGAGVLGAALAKESpDAELTMVDINARALESARENLAANG---LENGEV 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   145 FCVPLQEfTPAAGRYDVIwvqwcI-------GHLTDNDFV-SFFNRAKGYLKPGG-FFVV 195
Cdd:pfam05175  86 VASDVYS-GVEDGKFDLI-----IsnppfhaGLATTYNVAqRFIADAKRHLRPGGeLWIV 139
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 93-244 9.00e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 9.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56121880   93 LDCGSGIGRITKNLLIRYFN--EVDLLEPVAqfldaaRENLASAGSetHKATNFFC--VPLQEFTPAAGRYDVIWVQWCI 168
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQviALDFIESVI------KKNESINGH--YKNVKFMCadVTSPDLNISDGSVDLIFSNWLL 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56121880  169 GHLTDNDFVSFFNRAKGYLKPGGFFVVKEN-LAKNGFVLDKEDHSITRSDPYFKQLFRQCglhlyRTKDQKGLPQEL 244
Cdd:PLN02336 114 MYLSDKEVENLAERMVKWLKVGGYIFFREScFHQSGDSKRKNNPTHYREPRFYTKVFKEC-----HTRDEDGNSFEL 185
 
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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