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Conserved domains on  [gi|56676399|ref|NP_054783|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform a [Homo sapiens]

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
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
8-223 4.70e-135

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 characteristic GxGxG motif.


:

Pssm-ID: 283530  Cd Length: 217  Bit Score: 377.87  E-value: 4.70e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEQFYSKAIAYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKRRHLVALDCGAGIGRVTKNLLLPLFSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFLAKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 56676399   167 DNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVAQNGFVFDKEDSSVTRSEAYFKKLFKKAGLKLVAEERQKGLPQELYPVKMYALK 217
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
8-223 4.70e-135

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 characteristic GxGxG motif.


Pssm-ID: 283530  Cd Length: 217  Bit Score: 377.87  E-value: 4.70e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEQFYSKAIAYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKRRHLVALDCGAGIGRVTKNLLLPLFSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFLAKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 56676399   167 DNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVAQNGFVFDKEDSSVTRSEAYFKKLFKKAGLKLVAEERQKGLPQELYPVKMYALK 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
66-166 3.55e-11

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: 58.21  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPD-SYDVIWIQWVIGHLtDQ 144
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHHL-VE 81
                        90       100
                ....*....|....*....|..
gi 56676399 145 HLAEFLRRCKGSLRPNGIIVIK 166
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
41-165 2.45e-08

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];


Pssm-ID: 225137 [Multi-domain]  Cd Length: 243  Bit Score: 52.72  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  41 DINSSR-KFLQRFLREGPNKTGTSCaLDCGAGIGRitkrLLLPLFRE---VDMVDITEDFLVQAKTYLGEEGKRVrNYFC 116
Cdd:COG2227  39 KINPLRlDYIREVARLRFDLPGLRV-LDVGCGGGI----LSEPLARLgasVTGIDASEKPIEVAKLHALESGVNI-DYRQ 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 56676399 117 CGLQDFTPEPDSYDVIWIQWVIGHLTDQhlAEFLRRCKGSLRPNGIIVI 165
Cdd:COG2227 113 ATVEDLASAGGQFDVVTCMEVLEHVPDP--ESFLRACAKLVKPGGILFL 159
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
33-172 6.05e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399   33 GYGHISSIDINSSRKFLQRFLREgPNktgtSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVR 112
Cdd:PTZ00098  29 GEDYISSGGIEATTKILSDIELN-EN----SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEF 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  113 NYFCCGLQDFtPEpDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQE 172
Cdd:PTZ00098 104 EANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADK 161
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
8-223 4.70e-135

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 characteristic GxGxG motif.


Pssm-ID: 283530  Cd Length: 217  Bit Score: 377.87  E-value: 4.70e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEQFYSKAIAYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKRRHLVALDCGAGIGRVTKNLLLPLFSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFLAKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 56676399   167 DNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVAQNGFVFDKEDSSVTRSEAYFKKLFKKAGLKLVAEERQKGLPQELYPVKMYALK 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
66-161 6.64e-18

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


Pssm-ID: 433377 [Multi-domain]  Cd Length: 97  Bit Score: 75.69  E-value: 6.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    66 LDCGAGIGRITKRLL-LPLFREVDMVDITEDFLVQAKTYLGEEGKRVRnYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQ 144
Cdd:pfam13649   2 LDLGCGTGRLTLALArRGPNARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 80
                          90
                  ....*....|....*..
gi 56676399   145 HLAEFLRRCKGSLRPNG 161
Cdd:pfam13649  81 DLEAALREIARVLKPGG 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
66-165 5.26e-12

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


Pssm-ID: 429883 [Multi-domain]  Cd Length: 94  Bit Score: 59.99  E-value: 5.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    66 LDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKrvrNYFCCGLQDfTPEPD-SYDVIWIQWVIGHLTDq 144
Cdd:pfam08241   1 LDVGCGTGLLT-ELLARLGARVTGVDISPEMLELAREKAPREGL---TFVVGDAED-LPFPDnSFDLVLSSEVLHHVED- 74
                          90       100
                  ....*....|....*....|.
gi 56676399   145 hLAEFLRRCKGSLRPNGIIVI 165
Cdd:pfam08241  75 -PERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
66-166 3.55e-11

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: 58.21  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPD-SYDVIWIQWVIGHLtDQ 144
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHHL-VE 81
                        90       100
                ....*....|....*....|..
gi 56676399 145 HLAEFLRRCKGSLRPNGIIVIK 166
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
66-163 2.28e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.45  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    66 LDCGAGIGRITKRLLLPLFR-EVDMVDITEDFLVQAKTYLGEEGKRVR---NYFCcgLQDFTPEPDSYDVIWIQWVIGHL 141
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHL 78
                          90       100
                  ....*....|....*....|..
gi 56676399   142 TDqhLAEFLRRCKGSLRPNGII 163
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
41-165 2.45e-08

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism];


Pssm-ID: 225137 [Multi-domain]  Cd Length: 243  Bit Score: 52.72  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  41 DINSSR-KFLQRFLREGPNKTGTSCaLDCGAGIGRitkrLLLPLFRE---VDMVDITEDFLVQAKTYLGEEGKRVrNYFC 116
Cdd:COG2227  39 KINPLRlDYIREVARLRFDLPGLRV-LDVGCGGGI----LSEPLARLgasVTGIDASEKPIEVAKLHALESGVNI-DYRQ 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 56676399 117 CGLQDFTPEPDSYDVIWIQWVIGHLTDQhlAEFLRRCKGSLRPNGIIVI 165
Cdd:COG2227 113 ATVEDLASAGGQFDVVTCMEVLEHVPDP--ESFLRACAKLVKPGGILFL 159
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
66-200 2.95e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 433524 [Multi-domain]  Cd Length: 150  Bit Score: 39.70  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    66 LDCGAGIGRITKRLLLPLFREVDMV--DITEDFLVQAKTYLGEEG-KRVRnyFCcgLQDFTPEP-----DSYDVIWIQWV 137
Cdd:pfam13847   8 LDLGCGTGHLSFELAEEVGPNAEVVgiDISEEAIEKARENAQKLGfDNVE--FE--QGDIEELPelledDKFDVVISNCV 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56676399   138 IGHLTDQhlAEFLRRCKGSLRPNGIIVIkdnmaQEGVILDDVDSSVCRDLDVVRRIICSAGLS 200
Cdd:pfam13847  84 LNLIPDP--DKVLQEILRVLKPGGRLII-----SDPDSLAELPAHVKEDSTYYAGCVGGAILK 139
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
33-172 6.05e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 6.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399   33 GYGHISSIDINSSRKFLQRFLREgPNktgtSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVR 112
Cdd:PTZ00098  29 GEDYISSGGIEATTKILSDIELN-EN----SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEF 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  113 NYFCCGLQDFtPEpDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQE 172
Cdd:PTZ00098 104 EANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADK 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];
46-165 6.14e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];


Pssm-ID: 225136 [Multi-domain]  Cd Length: 238  Bit Score: 39.55  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  46 RKFLQRFLREGPNKTgtscALDCGAGIGRITKRLL-LPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFccgLQDFT- 123
Cdd:COG2226  40 RRALISLLGIKPGDK----VLDVACGTGDMALLLAkSVGTGEVVGLDISESMLEVAREKLKKKGVQNVEFV---VGDAEn 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 56676399 124 -PEPD-SYDVIWIQWVIGHLTDQH--LAEFLRRCKgslrPNGIIVI 165
Cdd:COG2226 113 lPFPDnSFDAVTISFGLRNVTDIDkaLKEMYRVLK----PGGRLLV 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
61-216 6.19e-04

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


Pssm-ID: 223574 [Multi-domain]  Cd Length: 257  Bit Score: 39.88  E-value: 6.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  61 GTSCALDCGAGIGRIT--KRLLLPLFREVDmVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFT---PEPDSYDVIWIQ 135
Cdd:COG0500  48 GGLGVLDIGCGTGRLAllARLGGRGAYVVG-VDLSPEMLALARARAEGAGLGLVDFVVADALGGVlpfEDSASFDLVISL 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399 136 WVIGHLtdqHLAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIY 215
Cdd:COG0500 127 LVLHLL---PPAKALRELLRVLKPGGRLVLSDLLRDGLLEGRLAALLGFGDPVLERGDILLELEALLRLELLDLEELLGL 203

                .
gi 56676399 216 H 216
Cdd:COG0500 204 L 204
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
146-220 7.81e-04

Predicted methyltransferase [General function prediction only];


Pssm-ID: 227135  Cd Length: 238  Bit Score: 39.44  E-value: 7.81e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56676399 146 LAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSF 220
Cdd:COG4798 145 AAKVNAAVFKALKPGGVYLVEDHRADPGSGLSDTITLHRIDPAVVIAEVEAAGFKLEAESEILANPDDPRGIWVF 219
SpeE COG0421
Spermidine synthase [Amino acid transport and metabolism];
69-165 8.85e-04

Spermidine synthase [Amino acid transport and metabolism];


Pssm-ID: 223498 [Multi-domain]  Cd Length: 282  Bit Score: 39.28  E-value: 8.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  69 GAGIGRITKRLL-LPLFREVDMVDITEDFLVQAKTYLGE-----EGKRVRNYFCCGLQDFTPEPDSYDVIwiqwvIGHLT 142
Cdd:COG0421  84 GGGDGGTLREVLkHLPVERITMVEIDPAVIELARKYLPEpsggaDDPRVEIIIDDGVEFLRDCEEKFDVI-----IVDST 158
                        90       100       110
                ....*....|....*....|....*....|
gi 56676399 143 D-----QHL--AEFLRRCKGSLRPNGIIVI 165
Cdd:COG0421 159 DpvgpaEALftEEFYEGCRRALKEDGIFVA 188
PRK00811 PRK00811
polyamine aminopropyltransferase;
86-164 3.45e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.44  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399   86 EVDMVDITEDFLVQAKTYLGE------EGKRVRNYFCCGLqDFTPEPD-SYDVIwiqwvIGHLTD-----QHL--AEFLR 151
Cdd:PRK00811 102 KITLVEIDERVVEVCRKYLPEiaggayDDPRVELVIGDGI-KFVAETEnSFDVI-----IVDSTDpvgpaEGLftKEFYE 175
                         90
                 ....*....|...
gi 56676399  152 RCKGSLRPNGIIV 164
Cdd:PRK00811 176 NCKRALKEDGIFV 188
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
59-165 7.10e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 36.26  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399    59 KTGTScALDCGAGIGRITKRLLLPLFR--EVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQW 136
Cdd:pfam01209  41 KRGNK-FLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISF 119
                          90       100
                  ....*....|....*....|....*....
gi 56676399   137 VIGHLTDQHLAefLRRCKGSLRPNGIIVI 165
Cdd:pfam01209 120 GLRNFPDYLKV--LKEAFRVLKPGGRVVC 146
YrrM COG4122
Predicted O-methyltransferase YrrM [General function prediction only];
65-178 8.92e-03

Predicted O-methyltransferase YrrM [General function prediction only];


Pssm-ID: 226607 [Multi-domain]  Cd Length: 219  Bit Score: 36.15  E-value: 8.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56676399  65 ALDCGAGIGRITKRLL--LPLFREVDMVDITEDFLVQAKTYLGE---EGKRVRNYFCCGLQDFT-PEPDSYDVIWIQwvi 138
Cdd:COG4122  63 ILEIGTAIGYSALWMAlaLPDDGRLTTIERDEERAEIARENLAEagvDDRIELLLGGDALDVLSrLLDGSFDLVFID--- 139
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56676399 139 ghlTDQ-HLAEFLRRCKGSLRPNGIIVIkDNMAQEGVILDD 178
Cdd:COG4122 140 ---ADKaDYPEYLERALPLLRPGGLIVA-DNVLFGGRVADP 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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