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Conserved domains on  [gi|24528555|ref|NP_733480|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform a [Mus musculus]

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 5.12e-134

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: 375.18  E-value: 5.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRV 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    87 VDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24528555   167 DNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR 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 5.12e-134

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: 375.18  E-value: 5.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRV 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    87 VDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24528555   167 DNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR 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 2.71e-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: 74.67  E-value: 2.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  46 RKFLQRFLREGPNKTGTscALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPE 125
Cdd:COG2227  11 DRRLAALLARLLPAGGR--VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24528555 126 PGSYDVIWIQWVIGHLTDqhLAEFLRRCKRGLRPNGIIVI 165
Cdd:COG2227  85 DGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 4.42e-12

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: 60.52  E-value: 4.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  66 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPGSYDVIWIQWVIGHLtDQ 144
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                        90       100
                ....*....|....*....|..
gi 24528555 145 HLAEFLRRCKRGLRPNGIIVIK 166
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 66-167 2.92e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.19  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555   66 LDCGAGIGRITKRLLLPLFRVVDMvDVTEDFLAKAKTYLGEEgKRVRnyFCCG---LQDFSPEPGSYDVIWIQWVIGHLT 142
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHY-KNVK--FMCAdvtSPDLNISDGSVDLIFSNWLLMYLS 117

                         90       100
                 ....*....|....*....|....*
gi 24528555  143 DQHLAEFLRRCKRGLRPNGIIVIKD 167
Cdd:PLN02336 118 DKEVENLAERMVKWLKVGGYIFFRE 142
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 8-223 5.12e-134

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: 375.18  E-value: 5.12e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555     8 DEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLRE-GPNKTGTSCALDCGAGIGRITKRLLLPLFRV 86
Cdd:pfam05891   1 DEEIFYEKAIDYWEGVSATVDGMLGGYGHVSDIDVNGSRNFLRRLLRErLPGKNRHLVALDCGAGIGRVTKNLLLPLFSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    87 VDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIK 166
Cdd:pfam05891  81 VDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFIVVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24528555   167 DNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR 223
Cdd:pfam05891 161 ENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQELYPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-161 7.51e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 80.69  E-value: 7.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    66 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRnYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQH 145
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 24528555   146 LAEFLRRCKRGLRPNG 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 2.71e-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: 74.67  E-value: 2.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  46 RKFLQRFLREGPNKTGTscALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPE 125
Cdd:COG2227  11 DRRLAALLARLLPAGGR--VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLE 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24528555 126 PGSYDVIWIQWVIGHLTDqhLAEFLRRCKRGLRPNGIIVI 165
Cdd:COG2227  85 DGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-200 1.22e-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: 68.10  E-value: 1.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  46 RKFLQRfLREGPNKTgtscALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRnyFCCG-LQDFSP 124
Cdd:COG2226  12 EALLAA-LGLRPGAR----VLDLGCGTGRLALALAERGARVT-GVDISPEMLELARERAAEAGLNVE--FVVGdAEDLPF 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24528555 125 EPGSYDVIWIQWVIGHLTDqhLAEFLRRCKRGLRPNGIIVIKDNMAqegvilddvdssvcRDLEVVRRIIRTAGLS 200
Cdd:COG2226  84 PDGSFDLVISSFVLHHLPD--PERALAEIARVLKPGGRLVVVDFSP--------------PDLAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 66-165 2.19e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.45  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    66 LDCGAGIGRITKRLLLPLFRVVDmVDVTEDFLAKAKTYLGEEGKrvrNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDqh 145
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTG-VDISPEMLELAREKAPREGL---TFVVGDAEDLPFPDNSFDLVLSSEVLHHVED-- 74

                          90       100
                  ....*....|....*....|
gi 24528555   146 LAEFLRRCKRGLRPNGIIVI 165
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-165 6.27e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.63  E-value: 6.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  46 RKFLQRFLREGPNKTGTScALDCGAGIGRITkRLLLPLFRVVDMVDVTEDFLAKAKTylgeegKRV-RNYFCCGLQDFSP 124
Cdd:COG4976  32 ALLAEELLARLPPGPFGR-VLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKARE------KGVyDRLLVADLADLAE 103

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24528555 125 EPGSYDVIWIQWVIGHLTDqhLAEFLRRCKRGLRPNGIIVI 165
Cdd:COG4976 104 PDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLFIF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
65-165 3.14e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 60.61  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  65 ALDCGAGIGRITKRLL--LPLFRVVdMVDVTEDFLAKAKTYLGeegkRVRnyFCCG-LQDFSPePGSYDVIWIQWVIGHL 141
Cdd:COG4106   5 VLDLGCGTGRLTALLAerFPGARVT-GVDLSPEMLARARARLP----NVR--FVVAdLRDLDP-PEPFDLVVSNAALHWL 76

                        90       100
                ....*....|....*....|....
gi 24528555 142 TDQhlAEFLRRCKRGLRPNGIIVI 165
Cdd:COG4106  77 PDH--AALLARLAAALAPGGVLAV 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 66-166 4.42e-12

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: 60.52  E-value: 4.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  66 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPGSYDVIWIQWVIGHLtDQ 144
Cdd:cd02440   3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                        90       100
                ....*....|....*....|..
gi 24528555 145 HLAEFLRRCKRGLRPNGIIVIK 166
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLT 103
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 66-163 2.77e-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: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    66 LDCGAGIGRITKRLLLPLFRV-VDMVDVTEDFLAKAKTYLGEEGKRVR---NYFCcgLQDFSPEPGSYDVIWIQWVIGHL 141
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 24528555   142 TDqhLAEFLRRCKRGLRPNGII 163
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-174 5.15e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.46  E-value: 5.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  49 LQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEG-KRVRnYFCCGLQDFSPEP- 126
Cdd:COG0500  14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPLPa 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24528555 127 GSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGV 174
Cdd:COG0500  93 ESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSASDAAAAL 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 45-165 1.23e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.54  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  45 SRKFLQRFLREGPNKTGTScALDCGAGIGRITKRLLlPLFRV-VDMVDVTEDFLAKAKTYLGEEG--KRVRnYFCCGLQD 121
Cdd:COG2230  36 QEAKLDLILRKLGLKPGMR-VLDIGCGWGGLALYLA-RRYGVrVTGVTLSPEQLEYARERAAEAGlaDRVE-VRLADYRD 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 24528555 122 FsPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVI 165
Cdd:COG2230 113 L-PADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
69-165 1.50e-04

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 41.35  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  69 GAGIGRITKRLL-LPLFRVVDMVDVTEDFLAKAKTYLGE-----EGKRVRNYFCCGLQDFSPEPGSYDVIwiqwvIGHLT 142
Cdd:COG0421  45 GGGDGGLARELLkHPPVERVDVVEIDPEVVELAREYFPLlapafDDPRLRVVIGDGRAFLREAEESYDVI-----IVDLT 119

                        90       100       110
                ....*....|....*....|....*....|
gi 24528555 143 D-----QHL--AEFLRRCKRGLRPNGIIVI 165
Cdd:COG0421 120 DpvgpaEGLftREFYEDCRRALKPGGVLVV 149
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 67-173 5.77e-04

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 39.70  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    67 DCGAGIGRITKRL--LLPLFR--VVDMVDVtedfLAKAKTYLgEEGKRVRNYFCCGlqDF--SPEPGSyDVIWIQWVIGH 140
Cdd:pfam00891  66 DVGGGTGALAQAIvsLYPGCKgiVFDLPHV----VEAAPTHF-SAGEEPRVTFHGG--DFfkDSLPEA-DAYILKRVLHD 137

                          90       100       110
                  ....*....|....*....|....*....|...
gi 24528555   141 LTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEG 173
Cdd:pfam00891 138 WSDEKCVKLLKRCYKACPAGGKVILVESLLGAD 170
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 66-200 7.65e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.55  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    66 LDCGAGIGRITKRLLLPLFRVVDMV--DVTEDFLAKAKTYLGEEG-KRVRnyFCcgLQDFSPEP-----GSYDVIWIQWV 137
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPNAEVVgiDISEEAIEKARENAQKLGfDNVE--FE--QGDIEELPelledDKFDVVISNCV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24528555   138 IGHLTDQhlAEFLRRCKRGLRPNGIIVIkdnmaQEGVILDDVDSSVCRDLEVVRRIIRTAGLS 200
Cdd:pfam13847  84 LNHIPDP--DKVLQEILRVLKPGGRLII-----SDPDSLAELPAHVKEDSTYYAGCVGGAILK 139
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
125-165 9.47e-04

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 38.69  E-value: 9.47e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24528555 125 EPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVI 165
Cdd:COG4627  43 PDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRI 83
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 66-167 2.92e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.19  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555   66 LDCGAGIGRITKRLLLPLFRVVDMvDVTEDFLAKAKTYLGEEgKRVRnyFCCG---LQDFSPEPGSYDVIWIQWVIGHLT 142
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHY-KNVK--FMCAdvtSPDLNISDGSVDLIFSNWLLMYLS 117

                         90       100
                 ....*....|....*....|....*
gi 24528555  143 DQHLAEFLRRCKRGLRPNGIIVIKD 167
Cdd:PLN02336 118 DKEVENLAERMVKWLKVGGYIFFRE 142
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
59-165 3.11e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 37.42  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555    59 KTGTScALDCGAGIGRITKRLLL---PLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQ 135
Cdd:pfam01209  41 KRGNK-FLDVAGGTGDWTFGLSDsagSSGKVV-GLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTIS 118

                          90       100       110
                  ....*....|....*....|....*....|
gi 24528555   136 WVIGHLTDQHLAefLRRCKRGLRPNGIIVI 165
Cdd:pfam01209 119 FGLRNFPDYLKV--LKEAFRVLKPGGRVVC 146
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-172 3.30e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 37.64  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555   33 GYGHISNIDLNSSRKFLQRFLREgPNktgtSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVR 112
Cdd:PTZ00098  29 GEDYISSGGIEATTKILSDIELN-EN----SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEF 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  113 NYFCCGLQDFsPEpGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQE 172
Cdd:PTZ00098 104 EANDILKKDF-PE-NTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADK 161
PRK00811 PRK00811
polyamine aminopropyltransferase;
87-164 3.91e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.44  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555   87 VDMVDVTEDFLAKAKTYLGE------EGKRVRNYFCCGLQDFSPEPGSYDVIwiqwvIGHLTD-----QHL--AEFLRRC 153
Cdd:PRK00811 103 ITLVEIDERVVEVCRKYLPEiaggayDDPRVELVIGDGIKFVAETENSFDVI-----IVDSTDpvgpaEGLftKEFYENC 177

                         90
                 ....*....|.
gi 24528555  154 KRGLRPNGIIV 164
Cdd:PRK00811 178 KRALKEDGIFV 188
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 90-177 5.67e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 36.32  E-value: 5.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24528555  90 VDVTEDFLAKAKTYLGEEG--KRVRnyFCCG-----LQDFSPEPgsYDVIWIqwvighltD---QHLAEFLRRCKRGLRP 159
Cdd:COG4122  47 IEIDPERAAIARENFARAGlaDRIR--LILGdalevLPRLADGP--FDLVFI--------DadkSNYPDYLELALPLLRP 114

                        90
                ....*....|....*...
gi 24528555 160 NGIIVIkDNMAQEGVILD 177
Cdd:COG4122 115 GGLIVA-DNVLWHGRVAD 131
 
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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