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Conserved domains on  [gi|21536262|ref|NP_659126|]
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eEF1A lysine and N-terminal methyltransferase isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
500-638 6.97e-27

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


:

Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 108.38  E-value: 6.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQS----DRMKVHIADGLDYITslagEAPPHYDVIMfdV 575
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR----EAEESYDVII--V 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536262 576 DSKDPTlgmsCPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLK--DSVLAGLKAAFPLLYV 638
Cdd:COG0421 117 DLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 8.40e-16

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 73.37  E-value: 8.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 21536262   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
500-638 6.97e-27

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 108.38  E-value: 6.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQS----DRMKVHIADGLDYITslagEAPPHYDVIMfdV 575
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR----EAEESYDVII--V 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536262 576 DSKDPTlgmsCPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLK--DSVLAGLKAAFPLLYV 638
Cdd:COG0421 117 DLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
500-672 6.53e-19

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 87.02  E-value: 6.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVA-TQWFGFSQSDRMKVHIADGLDYItslaGEAPPHYDVIMFD-VDS 577
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYI----AVHRHSTDVILVDgFDG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  578 KDptlgmscPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLkDSVLAGLKAAFP-LLYVRRIEGEVNEILFCQLHPE 656
Cdd:PRK04457 148 EG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRDKRY-DRYLERLESSFEgRVLELPAESHGNVAVFAFKSAP 219

                        170
                 ....*....|....*.
gi 21536262  657 QKLATPELLEMAQVLE 672
Cdd:PRK04457 220 KELRWDKLRKRAKKLE 235
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 8.40e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 73.37  E-value: 8.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 21536262   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-159 3.57e-15

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: 73.10  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  30 EWYGTYLELCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLE 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21536262 110 FPDATFQVVLDKGTLDAVltdeeevtlRQVDRMLAEVGRVLQVGGRYLCI 159
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL---------PDPERALAEIARVLKPGGRLVVV 123
PRK08317 PRK08317
hypothetical protein; Provisional
 46-158 7.92e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 59.95  E-value: 7.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   46 IKPKEKVLVIGCGNSELSEQLYD-VGYQ-DIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFqvvldkgt 123
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARrVGPEgRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF-------- 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21536262  124 lDAVLTDEEEVTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:PRK08317  89 -DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 500-612 1.14e-08

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 55.40  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWF----GFSQSDRMKVHIADGLDYITSLAGEapphYDVIMfdV 575
Cdd:pfam01564  24 IIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVVIGDGFKFLKDYLNT----FDVII--V 97

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21536262   576 DSKDPTlgmsCPPPAFVDQVFLQKVKSILCHDGVFIL 612
Cdd:pfam01564  98 DSTDPV----GPAENLFSKPFFDLLKKALKEDGVFIT 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-159 1.25e-08

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: 53.20  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  51 KVLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERN-GSRRPHMSFLKMDMTQLEF-PDATFQVVLdkgtLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaALLADNVEVLKGDAEELPPeADESFDVII----SDPPL 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 21536262 129 TDEEEVtlrqVDRMLAEVGRVLQVGGRYLCI 159
Cdd:cd02440  77 HHLVED----LARFLEEARRLLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 503-634 1.73e-07

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 54.08  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  503 LGGG--SLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFsQSDRMKVHIADGLdyiTSLAGEAPPHYDVIMFDVdSKDP 580
Cdd:NF037959 282 IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHEDAR---RALRRRPEERFDVIVGDA-FTDI 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21536262  581 TLgmscpPPAFVDQVFLQKVKSILCHDGVFILNLV--CRDVRLKDSVLAGLKAAFP 634
Cdd:NF037959 357 AV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVATLREVFP 407
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 503-615 8.19e-04

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: 39.34  E-value: 8.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 503 LGGGS-LPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQSDRMKVHIADGLDyitsLAGEAPPHYDVIMFDvdskdpt 581
Cdd:cd02440   5 LGCGTgALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEE----LPPEADESFDVIISD------- 73

                        90       100       110
                ....*....|....*....|....*....|....
gi 21536262 582 lgMSCPPPAFVDQVFLQKVKSILCHDGVFILNLV 615
Cdd:cd02440  74 --PPLHHLVEDLARFLEEARRLLKPGGVLVLTLV 105
 
Name Accession Description Interval E-value
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
500-638 6.97e-27

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 108.38  E-value: 6.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQS----DRMKVHIADGLDYITslagEAPPHYDVIMfdV 575
Cdd:COG0421  43 IIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFPLLAPafddPRLRVVIGDGRAFLR----EAEESYDVII--V 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536262 576 DSKDPTlgmsCPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLK--DSVLAGLKAAFPLLYV 638
Cdd:COG0421 117 DLTDPV----GPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDllRRVLATLREVFPHVVL 177
PRK04457 PRK04457
polyamine aminopropyltransferase;
500-672 6.53e-19

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 87.02  E-value: 6.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVA-TQWFGFSQSDRMKVHIADGLDYItslaGEAPPHYDVIMFD-VDS 577
Cdd:PRK04457  72 QIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArNHFELPENGERFEVIEADGAEYI----AVHRHSTDVILVDgFDG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  578 KDptlgmscPPPAFVDQVFLQKVKSILCHDGVFILNLVCRDVRLkDSVLAGLKAAFP-LLYVRRIEGEVNEILFCQLHPE 656
Cdd:PRK04457 148 EG-------IIDALCTQPFFDDCRNALSSDGIFVVNLWSRDKRY-DRYLERLESSFEgRVLELPAESHGNVAVFAFKSAP 219

                        170
                 ....*....|....*.
gi 21536262  657 QKLATPELLEMAQVLE 672
Cdd:PRK04457 220 KELRWDKLRKRAKKLE 235
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 52-154 8.40e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 73.37  E-value: 8.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    52 VLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLdavltde 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVL------- 73

                          90       100
                  ....*....|....*....|...
gi 21536262   132 EEVTLRQVDRMLAEVGRVLQVGG 154
Cdd:pfam13649  74 HHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-159 3.57e-15

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: 73.10  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  30 EWYGTYLELCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLE 109
Cdd:COG2226   6 ARYDGREALLAALG--LRPGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21536262 110 FPDATFQVVLDKGTLDAVltdeeevtlRQVDRMLAEVGRVLQVGGRYLCI 159
Cdd:COG2226  83 FPDGSFDLVISSFVLHHL---------PDPERALAEIARVLKPGGRLVVV 123
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-157 1.60e-11

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: 61.96  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  37 ELCEVLHKYIKPKEKVLVIGCGNSELSEQLYDVGYqDIVNIDISEVVIKQMKERngSRRPHMSFLKMDMTQLEFPDATFQ 116
Cdd:COG2227  13 RLAALLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGSFD 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21536262 117 VVLDKGTLDAVltdeeevtlRQVDRMLAEVGRVLQVGGRYL 157
Cdd:COG2227  90 LVICSEVLEHL---------PDPAALLRELARLLKPGGLLL 121
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-158 1.36e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 58.45  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    53 LVIGCGNSELSEQLYDVGYQdIVNIDISEVVIKQMKERNgsRRPHMSFLKMDMTQLEFPDATFQVVLDKGTLDavltdee 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDISPEMLELAREKA--PREGLTFVVGDAEDLPFPDNSFDLVLSSEVLH------- 70

                          90       100
                  ....*....|....*....|....*.
gi 21536262   133 evTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:pfam08241  71 --HVEDPERALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 46-185 1.43e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.12  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    46 IKPKEKVLVIGCGNSELSEQLYDVGYQD--IVNIDISEVVIKQMKER---NGSRRphMSFLKMDMTQLE--FPDATFQVV 118
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNaeVVGIDISEEAIEKARENaqkLGFDN--VEFEQGDIEELPelLEDDKFDVV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536262   119 LDKGTLDAVlTDEEEVtlrqvdrmLAEVGRVLQVGGRYLCISLAQAHILKKAVGHFSREGWMVRAHQ 185
Cdd:pfam13847  79 ISNCVLNHI-PDPDKV--------LQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGA 136
PRK08317 PRK08317
hypothetical protein; Provisional
 46-158 7.92e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 59.95  E-value: 7.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   46 IKPKEKVLVIGCGNSELSEQLYD-VGYQ-DIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFqvvldkgt 123
Cdd:PRK08317  17 VQPGDRVLDVGCGPGNDARELARrVGPEgRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSF-------- 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 21536262  124 lDAVLTDEEEVTLRQVDRMLAEVGRVLQVGGRYLC 158
Cdd:PRK08317  89 -DAVRSDRVLQHLEDPARALAEIARVLRPGGRVVV 122
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 500-612 1.14e-08

Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family includes spermidine synthase that catalyzes the fifth (last) step in the biosynthesis of spermidine from arginine, and spermine synthase.


Pssm-ID: 396237 [Multi-domain]  Cd Length: 183  Bit Score: 55.40  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWF----GFSQSDRMKVHIADGLDYITSLAGEapphYDVIMfdV 575
Cdd:pfam01564  24 IIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLpslaIGFQDPRVKVVIGDGFKFLKDYLNT----FDVII--V 97

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21536262   576 DSKDPTlgmsCPPPAFVDQVFLQKVKSILCHDGVFIL 612
Cdd:pfam01564  98 DSTDPV----GPAENLFSKPFFDLLKKALKEDGVFIT 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 51-159 1.25e-08

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: 53.20  E-value: 1.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  51 KVLVIGCGNSELSEQLYDVGYQDIVNIDISEVVIKQMKERN-GSRRPHMSFLKMDMTQLEF-PDATFQVVLdkgtLDAVL 128
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAaALLADNVEVLKGDAEELPPeADESFDVII----SDPPL 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 21536262 129 TDEEEVtlrqVDRMLAEVGRVLQVGGRYLCI 159
Cdd:cd02440  77 HHLVED----LARFLEEARRLLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 503-634 1.73e-07

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 54.08  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  503 LGGG--SLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFsQSDRMKVHIADGLdyiTSLAGEAPPHYDVIMFDVdSKDP 580
Cdd:NF037959 282 IGGGayTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWF-DPASATVLHEDAR---RALRRRPEERFDVIVGDA-FTDI 356

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21536262  581 TLgmscpPPAFVDQVFLQKVKSILCHDGVFILNLV--CRDVRLKDSVLAGLKAAFP 634
Cdd:NF037959 357 AV-----PAHLVTREFFELVRARLTPDGVYLMNVIdhADRLRALAALVATLREVFP 407
PRK00811 PRK00811
polyamine aminopropyltransferase;
520-611 4.75e-07

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 52.08  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  520 RIDAVEIDPTMLEVATQWF-----GFSQSDRMKVHIADGLDYItslaGEAPPHYDVIMfdVDSKDPTlGmscppPA---F 591
Cdd:PRK00811 102 KITLVEIDERVVEVCRKYLpeiagGAYDDPRVELVIGDGIKFV----AETENSFDVII--VDSTDPV-G-----PAeglF 169

                         90       100
                 ....*....|....*....|
gi 21536262  592 VDQvFLQKVKSILCHDGVFI 611
Cdd:PRK00811 170 TKE-FYENCKRALKEDGIFV 188
PLN02366 PLN02366
spermidine synthase
 500-600 4.37e-06

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 49.26  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWF-----GFSQSdRMKVHIADGLDYItslaGEAPPH-YDVIMf 573
Cdd:PLN02366  97 VVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFpdlavGFDDP-RVNLHIGDGVEFL----KNAPEGtYDAII- 170

                         90       100
                 ....*....|....*....|....*..
gi 21536262  574 dVDSKDPtLGmscPPPAFVDQVFLQKV 600
Cdd:PLN02366 171 -VDSSDP-VG---PAQELFEKPFFESV 192
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 37-150 5.90e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 46.85  E-value: 5.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262  37 ELCEVLHkyIKPKEKVLVIGCGNSELSEQL---YDVgyqDIVNIDISEVVIKQMKERNGSR--RPHMSFLKMDMTQLEfP 111
Cdd:COG2230  42 LILRKLG--LKPGMRVLDIGCGWGGLALYLarrYGV---RVTGVTLSPEQLEYARERAAEAglADRVEVRLADYRDLP-A 115

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21536262 112 DATFQVVLDKGTLDAVLTDEEEVTLRQVDRMLAEVGRVL 150
Cdd:COG2230 116 DGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 501-572 7.21e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 44.75  E-value: 7.21e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536262 501 VGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQ-SDRMKVHIADgldyITSLAGEAPPH-YDVIM 572
Cdd:COG4123  44 LGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGlEDRITVIHGD----LKEFAAELPPGsFDLVV 113
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 500-581 1.27e-04

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 44.86  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 500 VVGLGGGSLPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQ-------SDRMKVHIADGLDYItslaGEAPPHYDVIM 572
Cdd:COG4262 292 VLGGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTNPFLRElnggalnDPRVTVVNADAFQFL----RETDEKYDVII 367


                ....*....
gi 21536262 573 fdVDSKDPT 581
Cdd:COG4262 368 --VDLPDPS 374
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 47-158 1.55e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.99  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   47 KPKEKVLVIGCGNSELSEQLY-DVGYQD-IVNIDISEVVIKQMKER--NGSRRPHMSFLKMDMTQLEFPDATFqvvldkg 122
Cdd:PRK00216  50 RPGDKVLDLACGTGDLAIALAkAVGKTGeVVGLDFSEGMLAVGREKlrDLGLSGNVEFVQGDAEALPFPDNSF------- 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 21536262  123 tlDAVltdeeevT----LRQV---DRMLAEVGRVLQVGGRYLC 158
Cdd:PRK00216 123 --DAV-------TiafgLRNVpdiDKALREMYRVLKPGGRLVI 156
PRK14968 PRK14968
putative methyltransferase; Provisional
 34-157 2.89e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.19  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   34 TYLeLCEVLHkyIKPKEKVLVIGCGNSELSEQLYDVGyQDIVNIDISEVVIKQMKE---RNGSRRPHMSFLKMDMtqlef 110
Cdd:PRK14968  12 SFL-LAENAV--DKKGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCnakLNNIRNNGVEVIRSDL----- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536262  111 pdatFQVVlDKGTLDAVL-------TDEEE-------------VTLRQV-DRMLAEVGRVLQVGGRYL 157
Cdd:PRK14968  83 ----FEPF-RGDKFDVILfnppylpTEEEEewddwlnyalsggKDGREViDRFLDEVGRYLKPGGRIL 145
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 503-615 8.19e-04

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: 39.34  E-value: 8.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262 503 LGGGS-LPLFVHDHFPKSRIDAVEIDPTMLEVATQWFGFSQSDRMKVHIADGLDyitsLAGEAPPHYDVIMFDvdskdpt 581
Cdd:cd02440   5 LGCGTgALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEE----LPPEADESFDVIISD------- 73

                        90       100       110
                ....*....|....*....|....*....|....
gi 21536262 582 lgMSCPPPAFVDQVFLQKVKSILCHDGVFILNLV 615
Cdd:cd02440  74 --PPLHHLVEDLARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-107 8.58e-04

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 40.25  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262    35 YLELCEVLHKYIKPKEKVLVI---GCGNSELSEQLYDVGYQ-DIVNIDISEVVIKQMKERNgsRR----PHMSFLKMDMT 106
Cdd:pfam13679   9 LAEFIAPLLKELLDENGPITIvdhGAGKGYLGFILYYLKYGvRVYGIDTRAELVEKANALA--QKlgfnKRMSFLEGTIA 86


                  .
gi 21536262   107 Q 107
Cdd:pfam13679  87 G 87
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 46-124 1.38e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 41.66  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536262   46 IKPKEKVLVIGCG----NSELSEQlYDVgyqDIVNIDISEVVIKQMKERNGSRRPHMSFLKMDMTQLEFPDATFQVVLDK 121
Cdd:PLN02336 264 LKPGQKVLDVGCGigggDFYMAEN-FDV---HVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSR 339


                 ...
gi 21536262  122 GTL 124
Cdd:PLN02336 340 DTI 342
 
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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