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Conserved domains on  [gi|568914085|ref|XP_006498291|]
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N-terminal Xaa-Pro-Lys N-methyltransferase 1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_PK super family cl47937
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 26-193 1.85e-103

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.


The actual alignment was detected with superfamily member pfam05891:

Pssm-ID: 461771  Cd Length: 218  Bit Score: 296.60  E-value: 1.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  106 WVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 568914085  185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
 
Name Accession Description Interval E-value
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
 26-193 1.85e-103

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: 296.60  E-value: 1.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  106 WVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 568914085  185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-135 7.64e-16

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: 70.43  E-value: 7.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  35 ALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDq 114
Cdd:COG2227   28 VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD- 102

                         90       100
                 ....*....|....*....|.
gi 568914085 115 hLAEFLRRCKRGLRPNGIIVI 135
Cdd:COG2227  103 -PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-136 3.34e-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: 60.14  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPGSYDVIWIQWVIGHLtDQ 114
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                         90       100
                 ....*....|....*....|..
gi 568914085 115 HLAEFLRRCKRGLRPNGIIVIK 136
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 36-137 9.88e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.96  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLLPLFRVVDMvDVTEDFLAKAKTYLGEEgKRVRnyFCCG---LQDFSPEPGSYDVIWIQWVIGHLT 112
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHY-KNVK--FMCAdvtSPDLNISDGSVDLIFSNWLLMYLS 117

                         90       100
                 ....*....|....*....|....*
gi 568914085 113 DQHLAEFLRRCKRGLRPNGIIVIKD 137
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 ...
 26-193 1.85e-103

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: 296.60  E-value: 1.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   26 GPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQ 105
Cdd:pfam05891  50 LPGKNRHLVALDCGAGIGRVTKNLLLPLFSKVDLVEPVEDFIEKAKEYLAEGKKKVGNFFCVGLQDFTPEEGRYDLIWIQ 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  106 WVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGV-ILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEI 184
Cdd:pfam05891 130 WCIGHLTDEDLVAFLKRCKGGLKPNGFIVVKENVTQNGFdVFDKEDSSVTRSEAYFRQIFKKAGLKLVAEERQKGLPQEL 209


                  ....*....
gi 568914085  185 YHVYSFALR 193
Cdd:pfam05891 210 YPVKMYALK 218
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 36-131 9.03e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.53  E-value: 9.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRnYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQH 115
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 568914085  116 LAEFLRRCKRGLRPNG 131
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-135 7.64e-16

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: 70.43  E-value: 7.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  35 ALDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRvrnYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDq 114
Cdd:COG2227   28 VLDVGCGTGRLALALARRGADVT-GVDISPEALEIARERAAELNVD---FVQGDLEDLPLEDGSFDLVICSEVLEHLPD- 102

                         90       100
                 ....*....|....*....|.
gi 568914085 115 hLAEFLRRCKRGLRPNGIIVI 135
Cdd:COG2227  103 -PAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 36-170 6.08e-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: 65.79  E-value: 6.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLLPLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRnyFCCG-LQDFSPEPGSYDVIWIQWVIGHLTDq 114
Cdd:COG2226   27 LDLGCGTGRLALALAERGARVT-GVDISPEMLELARERAAEAGLNVE--FVVGdAEDLPFPDGSFDLVISSFVLHHLPD- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568914085 115 hLAEFLRRCKRGLRPNGIIVIKDNMAqegvilddvdssvcRDLEVVRRIIRTAGLS 170
Cdd:COG2226  103 -PERALAEIARVLKPGGRLVVVDFSP--------------PDLAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-135 1.91e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 63.07  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   36 LDCGAGIGRITKRLLLPLFRVVDmVDVTEDFLAKAKTYLGEEGKrvrNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDqh 115
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTG-VDISPEMLELAREKAPREGL---TFVVGDAEDLPFPDNSFDLVLSSEVLHHVED-- 74

                          90       100
                  ....*....|....*....|
gi 568914085  116 LAEFLRRCKRGLRPNGIIVI 135
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
35-135 9.77e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.48  E-value: 9.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  35 ALDCGAGIGRITkRLLLPLFRVVDMVDVTEDFLAKAKTylgeegKRV-RNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTD 113
Cdd:COG4976   50 VLDLGCGTGLLG-EALRPRGYRLTGVDLSEEMLAKARE------KGVyDRLLVADLADLAEPDGRFDLIVAADVLTYLGD 122

                         90       100
                 ....*....|....*....|..
gi 568914085 114 qhLAEFLRRCKRGLRPNGIIVI 135
Cdd:COG4976  123 --LAAVFAGVARALKPGGLFIF 142
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 36-136 3.34e-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: 60.14  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSP-EPGSYDVIWIQWVIGHLtDQ 114
Cdd:cd02440    3 LDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHL-VE 81

                         90       100
                 ....*....|....*....|..
gi 568914085 115 HLAEFLRRCKRGLRPNGIIVIK 136
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-135 1.42e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.30  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  35 ALDCGAGIGRITKRLL--LPLFRVVdMVDVTEDFLAKAKTYLGeegkRVRnyFCCG-LQDFSPePGSYDVIWIQWVIGHL 111
Cdd:COG4106    5 VLDLGCGTGRLTALLAerFPGARVT-GVDLSPEMLARARARLP----NVR--FVVAdLRDLDP-PEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....
gi 568914085 112 TDQhlAEFLRRCKRGLRPNGIIVI 135
Cdd:COG4106   77 PDH--AALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 36-133 2.69e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 55.07  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   36 LDCGAGIGRITKRLLLPLFRV-VDMVDVTEDFLAKAKTYLGEEGKRVR---NYFCcgLQDFSPEPGSYDVIWIQWVIGHL 111
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAvrvELFQ--LDLGELDPGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|..
gi 568914085  112 TDqhLAEFLRRCKRGLRPNGII 133
Cdd:pfam08242  79 AD--PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 31-144 9.30e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  31 GTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEG-KRVRnYFCCGLQDFSPEP-GSYDVIWIQWVI 108
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlGNVE-FLVADLAELDPLPaESFDLVVAFGVL 104

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568914085 109 GHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGV 144
Cdd:COG0500  105 HHLPPEEREALLRELARALKPGGVLLLSASDAAAAL 140
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 36-135 2.82e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.00  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLlPLFRV-VDMVDVTEDFLAKAKTYLGEEG--KRVRnYFCCGLQDFsPEPGSYDVIWIQWVIGHLT 112
Cdd:COG2230   56 LDIGCGWGGLALYLA-RRYGVrVTGVTLSPEQLEYARERAAEAGlaDRVE-VRLADYRDL-PADGQFDAIVSIGMFEHVG 132

                         90       100
                 ....*....|....*....|...
gi 568914085 113 DQHLAEFLRRCKRGLRPNGIIVI 135
Cdd:COG2230  133 PENYPAYFAKVARLLKPGGRLLL 155
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
39-135 1.44e-04

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 40.97  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  39 GAGIGRITKRLL-LPLFRVVDMVDVTEDFLAKAKTYLGE-----EGKRVRNYFCCGLQDFSPEPGSYDVIwiqwvIGHLT 112
Cdd:COG0421   45 GGGDGGLARELLkHPPVERVDVVEIDPEVVELAREYFPLlapafDDPRLRVVIGDGRAFLREAEESYDVI-----IVDLT 119

                         90       100       110
                 ....*....|....*....|....*....|
gi 568914085 113 D-----QHL--AEFLRRCKRGLRPNGIIVI 135
Cdd:COG0421  120 DpvgpaEGLftREFYEDCRRALKPGGVLVV 149
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 36-170 1.79e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.09  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   36 LDCGAGIGRITKRLLLPLFRVVDMV--DVTEDFLAKAKTYLGEEG-KRVRnyFCcgLQDFSPEP-----GSYDVIWIQWV 107
Cdd:pfam13847   8 LDLGCGTGHLSFELAEELGPNAEVVgiDISEEAIEKARENAQKLGfDNVE--FE--QGDIEELPelledDKFDVVISNCV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568914085  108 IGHLTDQhlAEFLRRCKRGLRPNGIIVIkdnmaQEGVILDDVDSSVCRDLEVVRRIIRTAGLS 170
Cdd:pfam13847  84 LNHIPDP--DKVLQEILRVLKPGGRLII-----SDPDSLAELPAHVKEDSTYYAGCVGGAILK 139
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
17-135 3.31e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 40.12  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   17 HPRWTA----CSGGpnKTGTScALDCGAGIGRITKRLLL---PLFRVVdMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGL 89
Cdd:pfam01209  27 HRLWKDftmkCMGV--KRGNK-FLDVAGGTGDWTFGLSDsagSSGKVV-GLDINENMLKEGEKKAKEEGKYNIEFLQGNA 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914085   90 QDFSPEPGSYDVIWIQWVIGHLTDQHLAefLRRCKRGLRPNGIIVI 135
Cdd:pfam01209 103 EELPFEDDSFDIVTISFGLRNFPDYLKV--LKEAFRVLKPGGRVVC 146
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 37-143 5.76e-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: 39.31  E-value: 5.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085   37 DCGAGIGRITKRL--LLPLFR--VVDMVDVtedfLAKAKTYLgEEGKRVRNYFCCGlqDF--SPEPGSyDVIWIQWVIGH 110
Cdd:pfam00891  66 DVGGGTGALAQAIvsLYPGCKgiVFDLPHV----VEAAPTHF-SAGEEPRVTFHGG--DFfkDSLPEA-DAYILKRVLHD 137

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568914085  111 LTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEG 143
Cdd:pfam00891 138 WSDEKCVKLLKRCYKACPAGGKVILVESLLGAD 170
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 36-137 9.88e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.96  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  36 LDCGAGIGRITKRLLLPLFRVVDMvDVTEDFLAKAKTYLGEEgKRVRnyFCCG---LQDFSPEPGSYDVIWIQWVIGHLT 112
Cdd:PLN02336  42 LELGAGIGRFTGELAKKAGQVIAL-DFIESVIKKNESINGHY-KNVK--FMCAdvtSPDLNISDGSVDLIFSNWLLMYLS 117

                         90       100
                 ....*....|....*....|....*
gi 568914085 113 DQHLAEFLRRCKRGLRPNGIIVIKD 137
Cdd:PLN02336 118 DKEVENLAERMVKWLKVGGYIFFRE 142
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
95-135 9.88e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 38.31  E-value: 9.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568914085  95 EPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVI 135
Cdd:COG4627   43 PDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRI 83
PRK00811 PRK00811
polyamine aminopropyltransferase;
57-134 1.90e-03

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 37.83  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  57 VDMVDVTEDFLAKAKTYLGE------EGKRVRNYFCCGLQDFSPEPGSYDVIwiqwvIGHLTD-----QHL--AEFLRRC 123
Cdd:PRK00811 103 ITLVEIDERVVEVCRKYLPEiaggayDDPRVELVIGDGIKFVAETENSFDVI-----IVDSTDpvgpaEGLftKEFYENC 177

                         90
                 ....*....|.
gi 568914085 124 KRGLRPNGIIV 134
Cdd:PRK00811 178 KRALKEDGIFV 188
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-142 4.64e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 36.87  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  33 SCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFsPEpGSYDVIWIQWVIGHLT 112
Cdd:PTZ00098  54 SKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDF-PE-NTFDMIYSRDAILHLS 131

                         90       100       110
                 ....*....|....*....|....*....|
gi 568914085 113 DQHLAEFLRRCKRGLRPNGIIVIKDNMAQE 142
Cdd:PTZ00098 132 YADKKKLFEKCYKWLKPNGILLITDYCADK 161
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 60-147 4.72e-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: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914085  60 VDVTEDFLAKAKTYLGEEG--KRVRnyFCCG-----LQDFSPEPgsYDVIWIqwvighltD---QHLAEFLRRCKRGLRP 129
Cdd:COG4122   47 IEIDPERAAIARENFARAGlaDRIR--LILGdalevLPRLADGP--FDLVFI--------DadkSNYPDYLELALPLLRP 114

                         90
                 ....*....|....*...
gi 568914085 130 NGIIVIkDNMAQEGVILD 147
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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