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Conserved domains on  [gi|17510631|ref|NP_490660|]
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Alpha N-terminal protein methyltransferase 1 [Caenorhabditis elegans]

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 ...
 11-225 3.84e-129

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: 363.24  E-value: 3.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    11 NGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNL--FGYFDYALDCGAGIGRVTKHLLMPFFSK 88
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLpgKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    89 VDMEDVVEELITKSDQYIGK-HPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLK 167
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEgKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17510631   168 DNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALK 225
Cdd:pfam05891 161 ENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 11-225 3.84e-129

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: 363.24  E-value: 3.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    11 NGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNL--FGYFDYALDCGAGIGRVTKHLLMPFFSK 88
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLpgKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    89 VDMEDVVEELITKSDQYIGK-HPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLK 167
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEgKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17510631   168 DNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALK 225
Cdd:pfam05891 161 ENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
67-166 5.54e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.13  E-value: 5.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  67 ALDCGAGIGRVTKHLLmPFFSKVDME--DVVEELITKSDQyigKHPRIgdKFVEG-LQTFAPPERrYDLIW----IQWVs 139
Cdd:COG4106   5 VLDLGCGTGRLTALLA-ERFPGARVTgvDLSPEMLARARA---RLPNV--RFVVAdLRDLDPPEP-FDLVVsnaaLHWL- 76

                        90       100
                ....*....|....*....|....*..
gi 17510631 140 ghlvdEDLVDFFKRCAKGLKPGGCIVL 166
Cdd:COG4106  77 -----PDHAALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-167 1.26e-06

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: 45.88  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  68 LDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEG--LQTFAPPERRYDLIwIQWVSGHLVDE 145
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaEELPPEADESFDVI-ISDPPLHHLVE 81

                        90       100
                ....*....|....*....|..
gi 17510631 146 DLVDFFKRCAKGLKPGGCIVLK 167
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 66-168 5.05e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631   66 YALDCGAGIGRVTKHLLMPFFSKVDMeDVVEELITKSDQYIGKHPRIgdKFVEGLQTfAP----PERRYDLIWIQWVSGH 141
Cdd:PLN02336  40 SVLELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHYKNV--KFMCADVT-SPdlniSDGSVDLIFSNWLLMY 115

                         90       100
                 ....*....|....*....|....*..
gi 17510631  142 LVDEDLVDFFKRCAKGLKPGGCIVLKD 168
Cdd:PLN02336 116 LSDKEVENLAERMVKWLKVGGYIFFRE 142
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 11-225 3.84e-129

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: 363.24  E-value: 3.84e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    11 NGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNL--FGYFDYALDCGAGIGRVTKHLLMPFFSK 88
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRERLpgKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    89 VDMEDVVEELITKSDQYIGK-HPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLK 167
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEgKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17510631   168 DNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALK 225
Cdd:pfam05891 161 ENVTQNGFDVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-162 1.89e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 58.73  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    68 LDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKH-PRIgdKFVEG-LQTFAPPERRYDLIWIQWVSGHLVDE 145
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAgLNV--EFVQGdAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 17510631   146 DLVDFFKRCAKGLKPGG 162
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
67-166 5.54e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.13  E-value: 5.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  67 ALDCGAGIGRVTKHLLmPFFSKVDME--DVVEELITKSDQyigKHPRIgdKFVEG-LQTFAPPERrYDLIW----IQWVs 139
Cdd:COG4106   5 VLDLGCGTGRLTALLA-ERFPGARVTgvDLSPEMLARARA---RLPNV--RFVVAdLRDLDPPEP-FDLVVsnaaLHWL- 76

                        90       100
                ....*....|....*....|....*..
gi 17510631 140 ghlvdEDLVDFFKRCAKGLKPGGCIVL 166
Cdd:COG4106  77 -----PDHAALLARLAAALAPGGVLAV 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 67-166 1.79e-07

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: 48.48  E-value: 1.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  67 ALDCGAGIGRVTKHlLMPFFSKVDMEDVVEELITKSDQyigKHPRIGDKFVEG-LQTFAPPERRYDLIWIQWVSGHLvdE 145
Cdd:COG2227  28 VLDVGCGTGRLALA-LARRGADVTGVDISPEALEIARE---RAAELNVDFVQGdLEDLPLEDGSFDLVICSEVLEHL--P 101

                        90       100
                ....*....|....*....|.
gi 17510631 146 DLVDFFKRCAKGLKPGGCIVL 166
Cdd:COG2227 102 DPAALLRELARLLKPGGLLLL 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
64-166 3.94e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 3.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  64 FDYALDCGAGIGRVTKHLLmPFFSKVDMEDVVEELItksDQYIGKHprIGDKFVEG-LQTFAPPERRYDLIWIQWVSGHL 142
Cdd:COG4976  47 FGRVLDLGCGTGLLGEALR-PRGYRLTGVDLSEEML---AKAREKG--VYDRLLVAdLADLAEPDGRFDLIVAADVLTYL 120

                        90       100
                ....*....|....*....|....
gi 17510631 143 vdEDLVDFFKRCAKGLKPGGCIVL 166
Cdd:COG4976 121 --GDLAAVFAGVARALKPGGLFIF 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-167 1.26e-06

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: 45.88  E-value: 1.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  68 LDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEG--LQTFAPPERRYDLIwIQWVSGHLVDE 145
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGdaEELPPEADESFDVI-ISDPPLHHLVE 81

                        90       100
                ....*....|....*....|..
gi 17510631 146 DLVDFFKRCAKGLKPGGCIVLK 167
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-164 2.32e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 44.67  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    68 LDCGAGIGRVTKHLLMPF-FSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEGLQT--FAPPERRYDLIWIQWVSGHLvd 144
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLdlGELDPGSFDVVVASNVLHHL-- 78

                          90       100
                  ....*....|....*....|
gi 17510631   145 EDLVDFFKRCAKGLKPGGCI 164
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 68-166 5.62e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.73  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    68 LDCGAGIGRVTKHLLMPFFSKVDMeDVVEELITKSDQyigKHPRIGDKFVEG-LQTFAPPERRYDLIWIQWVSGHLvdED 146
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGV-DISPEMLELARE---KAPREGLTFVVGdAEDLPFPDNSFDLVLSSEVLHHV--ED 74

                          90       100
                  ....*....|....*....|
gi 17510631   147 LVDFFKRCAKGLKPGGCIVL 166
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-205 9.07e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631    68 LDCGAGIGRVTKHLlMPFFSKVdmedvveELITKSDQYIGKHPRIGDKFVEGLQTFAPPERRYDLIwIQW-VSGHLVD-E 145
Cdd:pfam13489  27 LDFGCGTGIFLRLL-RAQGFSV-------TGVDPSPIAIERALLNVRFDQFDEQEAAVPAGKFDVI-VAReVLEHVPDpP 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17510631   146 DLVDFFKRCakgLKPGGCIVLKD-NVTNHEKRLFDD-------DDHSWTRTEPELLKAFADSQLDMVS 205
Cdd:pfam13489  98 ALLRQIAAL---LKPGGLLLLSTpLASDEADRLLLEwpylrprNGHISLFSARSLKRLLEEAGFEVVS 162
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 68-179 2.04e-04

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: 40.36  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  68 LDCGAGIGRVTKHLLmPFFSKVDMEDVVEELITKSDQYIGKHPrIGDKFVEG-LQTFAPPERRYDLIWIQWVSGHLvdED 146
Cdd:COG2226  27 LDLGCGTGRLALALA-ERGARVTGVDISPEMLELARERAAEAG-LNVEFVVGdAEDLPFPDGSFDLVISSFVLHHL--PD 102

                        90       100       110
                ....*....|....*....|....*....|...
gi 17510631 147 LVDFFKRCAKGLKPGGCIVLKDNVTNHEKRLFD 179
Cdd:COG2226 103 PERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 125-166 3.00e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.91  E-value: 3.00e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 17510631 125 PPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVL 166
Cdd:COG2230 114 PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 66-168 5.05e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 40.50  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631   66 YALDCGAGIGRVTKHLLMPFFSKVDMeDVVEELITKSDQYIGKHPRIgdKFVEGLQTfAP----PERRYDLIWIQWVSGH 141
Cdd:PLN02336  40 SVLELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHYKNV--KFMCADVT-SPdlniSDGSVDLIFSNWLLMY 115

                         90       100
                 ....*....|....*....|....*..
gi 17510631  142 LVDEDLVDFFKRCAKGLKPGGCIVLKD 168
Cdd:PLN02336 116 LSDKEVENLAERMVKWLKVGGYIFFRE 142
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 67-177 5.35e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.90  E-value: 5.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  67 ALDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQyigKHPRIGDKFVEGLQ-----TFAPPERRYDLIWIQWVSGH 141
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARA---RAAKAGLGNVEFLVadlaeLDPLPAESFDLVVAFGVLHH 106

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17510631 142 LVDEDLVDFFKRCAKGLKPGGCIVLKDNVTNHEKRL 177
Cdd:COG0500 107 LPPEEREALLRELARALKPGGVLLLSASDAAAALSL 142
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
71-166 1.03e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 39.04  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631  71 GAGIGRVTKHLL-MPFFSKVDMEDVVEELITKSDQYIG------KHPR----IGD--KFVEGlqtfapPERRYDLIwiqw 137
Cdd:COG0421  45 GGGDGGLARELLkHPPVERVDVVEIDPEVVELAREYFPllapafDDPRlrvvIGDgrAFLRE------AEESYDVI---- 114

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17510631 138 vsghLVD--------EDL--VDFFKRCAKGLKPGGCIVL 166
Cdd:COG0421 115 ----IVDltdpvgpaEGLftREFYEDCRRALKPGGVLVV 149
PRK00811 PRK00811
polyamine aminopropyltransferase;
69-165 5.43e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.06  E-value: 5.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17510631   69 DCGAgIGRVTKHllmPFFSKVDMEDVVEELITKSDQYIGKH-------PR----IGD--KFVEGlqtfapPERRYDLIwi 135
Cdd:PRK00811  87 DGGT-LREVLKH---PSVEKITLVEIDERVVEVCRKYLPEIaggayddPRvelvIGDgiKFVAE------TENSFDVI-- 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 17510631  136 qwvsghLVD--------EDL--VDFFKRCAKGLKPGGCIV 165
Cdd:PRK00811 155 ------IVDstdpvgpaEGLftKEFYENCKRALKEDGIFV 188
 
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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