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Conserved domains on  [gi|557948039|ref|NP_001273727|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform a [Homo sapiens]

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 ...
 8-223 1.47e-128

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: 361.31  E-value: 1.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 557948039  167 DNMAQEGV-ILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
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 ...
 8-223 1.47e-128

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: 361.31  E-value: 1.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 557948039  167 DNMAQEGV-ILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-165 8.53e-17

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: 73.51  E-value: 8.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  46 RKFLQRFLREGPNKTGTscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRvrnYFCCGLQDFTPE 125
Cdd:COG2227   11 DRRLAALLARLLPAGGR--VLDVGCGTGRLA-LALARRGADVTGVDISPEALEIARERAAELNVD---FVQGDLEDLPLE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557948039 126 PDSYDVIWIQWVIGHLTDqhLAEFLRRCKGSLRPNGIIVI 165
Cdd:COG2227   85 DGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 3.71e-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: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPD-SYDVIWIQWVIGHLtDQ 144
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHHL-VE 81

                         90       100
                 ....*....|....*....|..
gi 557948039 145 HLAEFLRRCKGSLRPNGIIVIK 166
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-172 6.31e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  33 GYGHISSIDINSSRKFLQRFLREgPNktgtSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVR 112
Cdd:PTZ00098  29 GEDYISSGGIEATTKILSDIELN-EN----SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEF 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039 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 1.47e-128

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: 361.31  E-value: 1.47e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039    8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRE 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   87 VDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 557948039  167 DNMAQEGV-ILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-161 1.20e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 77.60  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRnYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQH 145
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 557948039  146 LAEFLRRCKGSLRPNG 161
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-165 8.53e-17

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: 73.51  E-value: 8.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  46 RKFLQRFLREGPNKTGTscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRvrnYFCCGLQDFTPE 125
Cdd:COG2227   11 DRRLAALLARLLPAGGR--VLDVGCGTGRLA-LALARRGADVTGVDISPEALEIARERAAELNVD---FVQGDLEDLPLE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557948039 126 PDSYDVIWIQWVIGHLTDqhLAEFLRRCKGSLRPNGIIVI 165
Cdd:COG2227   85 DGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-167 6.50e-14

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: 66.17  E-value: 6.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  46 RKFLQRfLREGPNKTgtscALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRnyFCCG-LQDFTP 124
Cdd:COG2226   12 EALLAA-LGLRPGAR----VLDLGCGTGRLA-LALAERGARVTGVDISPEMLELARERAAEAGLNVE--FVVGdAEDLPF 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 557948039 125 EPDSYDVIWIQWVIGHLTDQH--LAEFLRRckgsLRPNGIIVIKD 167
Cdd:COG2226   84 PDGSFDLVISSFVLHHLPDPEraLAEIARV----LKPGGRLVVVD 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-165 1.11e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.86  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  46 RKFLQRFLREGPNKTGTScALDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTylgeegKRV-RNYFCCGLQDFTP 124
Cdd:COG4976   32 ALLAEELLARLPPGPFGR-VLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKARE------KGVyDRLLVADLADLAE 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 557948039 125 EPDSYDVIWIQWVIGHLTDqhLAEFLRRCKGSLRPNGIIVI 165
Cdd:COG4976  104 PDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLFIF 142
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 66-165 6.68e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.60  E-value: 6.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   66 LDCGAGIGRITkRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKrvrNYFCCGLQDfTPEPD-SYDVIWIQWVIGHLTDq 144
Cdd:pfam08241   1 LDVGCGTGLLT-ELLARLGARVTGVDISPEMLELAREKAPREGL---TFVVGDAED-LPFPDnSFDLVLSSEVLHHVED- 74

                          90       100
                  ....*....|....*....|.
gi 557948039  145 hLAEFLRRCKGSLRPNGIIVI 165
Cdd:pfam08241  75 -PERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 3.71e-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: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  66 LDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPD-SYDVIWIQWVIGHLtDQ 144
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADeSFDVIISDPPLHHL-VE 81

                         90       100
                 ....*....|....*....|..
gi 557948039 145 HLAEFLRRCKGSLRPNGIIVIK 166
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
65-165 2.07e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.60  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  65 ALDCGAGIGRITkRLLLPLFREVDM--VDITEDFLVQAKTYLGeegkRVRnyFCCG-LQDFTPEPdSYDVIWIQWVIGHL 141
Cdd:COG4106    5 VLDLGCGTGRLT-ALLAERFPGARVtgVDLSPEMLARARARLP----NVR--FVVAdLRDLDPPE-PFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....
gi 557948039 142 TDQhlAEFLRRCKGSLRPNGIIVI 165
Cdd:COG4106   77 PDH--AALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 66-163 2.37e-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: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   66 LDCGAGIGRITKRLLLPLFR-EVDMVDITEDFLVQAKTYLGEEGKRVR---NYFCcgLQDFTPEPDSYDVIWIQWVIGHL 141
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 557948039  142 TDqhLAEFLRRCKGSLRPNGII 163
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-174 9.51e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 50.69  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  49 LQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEG-KRVRnYFCCGLQDFTPEPD 127
Cdd:COG0500   14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPLPA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557948039 128 -SYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQEGV 174
Cdd:COG0500   93 eSFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAAL 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 45-165 1.58e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.46  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  45 SRKFLQRFLREGPNKTGTScALDCGAGIGRitkrLLLPLFRE----VDMVDITEDFLVQAKTYLGEEG--KRVRnYFCCG 118
Cdd:COG2230   36 QEAKLDLILRKLGLKPGMR-VLDIGCGWGG----LALYLARRygvrVTGVTLSPEQLEYARERAAEAGlaDRVE-VRLAD 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557948039 119 LQDFtPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVI 165
Cdd:COG2230  110 YRDL-PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
69-165 8.23e-05

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 42.12  E-value: 8.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  69 GAGIGRITKRLL-LPLFREVDMVDITEDFLVQAKTYLGE-----EGKRVRNYFCCGLQdFTPE-PDSYDVIwiqwvIGHL 141
Cdd:COG0421   45 GGGDGGLARELLkHPPVERVDVVEIDPEVVELAREYFPLlapafDDPRLRVVIGDGRA-FLREaEESYDVI-----IVDL 118

                         90       100       110
                 ....*....|....*....|....*....|.
gi 557948039 142 TD-----QHL--AEFLRRCKGSLRPNGIIVI 165
Cdd:COG0421  119 TDpvgpaEGLftREFYEDCRRALKPGGVLVV 149
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 66-200 3.10e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   66 LDCGAGIGRITKRLLLPLFREVDMV--DITEDFLVQAKTYLGEEG-KRVRnyFCcgLQDFTPEP-----DSYDVIWIQWV 137
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPNAEVVgiDISEEAIEKARENAQKLGfDNVE--FE--QGDIEELPelledDKFDVVISNCV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557948039  138 IGHLTDQhlAEFLRRCKGSLRPNGIIVIkdnmaQEGVILDDVDSSVCRDLDVVRRIICSAGLS 200
Cdd:pfam13847  84 LNHIPDP--DKVLQEILRVLKPGGRLII-----SDPDSLAELPAHVKEDSTYYAGCVGGAILK 139
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-172 6.31e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  33 GYGHISSIDINSSRKFLQRFLREgPNktgtSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVR 112
Cdd:PTZ00098  29 GEDYISSGGIEATTKILSDIELN-EN----SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEF 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039 113 NYFCCGLQDFtPEpDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQE 172
Cdd:PTZ00098 104 EANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADK 161
PRK00811 PRK00811
polyamine aminopropyltransferase;
86-164 3.60e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.44  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039  86 EVDMVDITEDFLVQAKTYLGE------EGKRVRNYFCCGLqDFTPEPD-SYDVIwiqwvIGHLTD-----QHL--AEFLR 151
Cdd:PRK00811 102 KITLVEIDERVVEVCRKYLPEiaggayDDPRVELVIGDGI-KFVAETEnSFDVI-----IVDSTDpvgpaEGLftKEFYE 175

                         90
                 ....*....|...
gi 557948039 152 RCKGSLRPNGIIV 164
Cdd:PRK00811 176 NCKRALKEDGIFV 188
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
59-165 7.40e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 36.26  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557948039   59 KTGTScALDCGAGIGRITKRLLLPLFR--EVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQW 136
Cdd:pfam01209  41 KRGNK-FLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISF 119

                          90       100
                  ....*....|....*....|....*....
gi 557948039  137 VIGHLTDQHLAefLRRCKGSLRPNGIIVI 165
Cdd:pfam01209 120 GLRNFPDYLKV--LKEAFRVLKPGGRVVC 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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