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Conserved domains on  [gi|63253298|ref|NP_003123|]
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spermidine synthase [Homo sapiens]

Protein Classification

spermidine/spermine synthase family protein( domain architecture ID 10010775)

spermidine/spermine synthase family protein similar to spermidine synthase, an aminopropyltransferase that transfers aminopropyl groups from decarboxylated S-adenosylmethionine to putrescine forming sperrmidine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 8-298 2.66e-159

spermidine synthase


:

Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 446.01  E-value: 2.66e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    8 PAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFP-VVAYAYCTIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63253298  246 IGFMLCSK-NPSTNFQEPVQPLTQ---QQVAQMQLKYYNSDVHRAAFVLPEFARKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 8-298 2.66e-159

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 446.01  E-value: 2.66e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    8 PAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFP-VVAYAYCTIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63253298  246 IGFMLCSK-NPSTNFQEPVQPLTQ---QQVAQMQLKYYNSDVHRAAFVLPEFARKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 20-293 1.48e-130

spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 188048 [Multi-domain]  Cd Length: 271  Bit Score: 372.14  E-value: 1.48e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   180 PAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 63253298   260 QEPVQPLTQQQvAQMQLKYYNSDVHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 76-255 2.55e-103

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: 299.62  E-value: 2.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170       180
                  ....*....|....*....|
gi 63253298   236 CTIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 9.41e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 232.41  E-value: 9.41e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298 139 GMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                       170       180       190
                ....*....|....*....|....*....|...
gi 63253298 219 EMRQFCQSLFPVVAYAYCTIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-206 4.06e-10

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: 56.28  E-value: 4.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIQVSKKFlpgmAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 63253298 176 DPMGPAESLFKESYYQLMKTALKEDGVLCCQ 206
Cdd:cd02440  73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 8-298 2.66e-159

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 446.01  E-value: 2.66e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    8 PAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFP-VVAYAYCTIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 63253298  246 IGFMLCSK-NPSTNFQEPVQPLTQ---QQVAQMQLKYYNSDVHRAAFVLPEFARKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 20-293 1.48e-130

spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine + S-adenosylmethioninamine = spermidine + 5'-methylthioadenosine) and is involved in polyamine biosynthesis and in the biosynthesis of spermidine from arganine. The region between residues 77 and 120 of the seed alignment is thought to be involved in binding to decarboxylated SAM. [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 188048 [Multi-domain]  Cd Length: 271  Bit Score: 372.14  E-value: 1.48e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   180 PAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 63253298   260 QEPVQPLTQQQvAQMQLKYYNSDVHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
PRK00811 PRK00811
polyamine aminopropyltransferase;
18-299 6.47e-124

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 355.62  E-value: 6.47e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   18 EGWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK00811   3 ELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIG-YSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSD 176
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  177 PMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPS 256
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 63253298  257 TNFQePVQPLTQQ-QVAQMQLKYYNSDVHRAAFVLPEFARKALN 299
Cdd:PRK00811 241 LKFL-PLDVIEARfAERGIKTRYYNPELHKAAFALPQFVKDALK 283
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 76-255 2.55e-103

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: 299.62  E-value: 2.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170       180
                  ....*....|....*....|
gi 63253298   236 CTIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 9.41e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 232.41  E-value: 9.41e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298 139 GMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                       170       180       190
                ....*....|....*....|....*....|...
gi 63253298 219 EMRQFCQSLFPVVAYAYCTIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02823 PLN02823
spermine synthase
 4-298 1.64e-60

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 195.67  E-value: 1.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298    4 GPDGPAASGPAAIREG-WFRETcsLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEM 82
Cdd:PLN02823  15 AVATPTAALASNYAKSlWYEEE--IEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHES 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   83 IANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQ 162
Cdd:PLN02823  93 LVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  163 NQDAFDVIITDSSDPM--GPAESLFKESYYQLM-KTALKEDGVLCCQGECQWL--HLDLIKEMRQFCQSLFP-VVAYAYC 236
Cdd:PLN02823 173 RDEKFDVIIGDLADPVegGPCYQLYTKSFYERIvKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKyVVPYTAH 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63253298  237 tIPTYPSgQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKAL 298
Cdd:PLN02823 253 -VPSFAD-TWGWVMASDHPFADLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQAL 312
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 27-203 5.18e-45

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 157.72  E-value: 5.18e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSKTYGNvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLII 100
Cdd:COG4262 215 LVFADPIESSAEQKLygdpvvYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298 101 GGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKF-----LPGMAigYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSS 175
Cdd:COG4262 294 GGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTNpflreLNGGA--LNDPRVTVVNADAFQFLRETDEKYDVIIVDLP 371

                       170       180       190
                ....*....|....*....|....*....|.
gi 63253298 176 DPmgPAESLFK---ESYYQLMKTALKEDGVL 203
Cdd:COG4262 372 DP--SNFSLGKlysVEFYRLVRRHLAPGGVL 400
PRK03612 PRK03612
polyamine aminopropyltransferase;
27-206 7.59e-34

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 129.19  E-value: 7.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSK-TYGNV--LVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK03612 222 FVLADRIETTAEQLLygdpvvYAEQTPYQRIVVTRRGnGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRV 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAI---GYSSSKLTLHVGDGFEFMKQNQDAFDVIITDS 174
Cdd:PRK03612 302 LVLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSPALRALnggALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDL 381

                        170       180       190
                 ....*....|....*....|....*....|...
gi 63253298  175 SDPMGPAES-LFKESYYQLMKTALKEDGVLCCQ 206
Cdd:PRK03612 382 PDPSNPALGkLYSVEFYRLLKRRLAPDGLLVVQ 414
speE PRK01581
polyamine aminopropyltransferase;
41-206 1.12e-23

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 99.27  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   41 LHHRRSRYQDILVFRSKTYGnvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV 120
Cdd:PRK01581 100 LFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  121 VQCEIDEDVIQVSKKFLPGMAIGYSS---SKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAES-LFKESYYQLMKTA 196
Cdd:PRK01581 178 DLVDLDGSMINMARNVPELVSLNKSAffdNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARIATF 257

                        170
                 ....*....|
gi 63253298  197 LKEDGVLCCQ 206
Cdd:PRK01581 258 LTEDGAFVCQ 267
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 19-73 8.71e-23

Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.


Pssm-ID: 407397 [Multi-domain]  Cd Length: 53  Bit Score: 88.87  E-value: 8.71e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 63253298    19 GWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTE 73
Cdd:pfam17284   1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
speE PRK00536
spermidine synthase; Provisional
 37-300 5.47e-17

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 78.75  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   37 VEQLLHHRRSRYQDILVFRSKTYGNVLVLDGviQCTERDEFSYQ-EMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHp 115
Cdd:PRK00536  17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKY- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  116 svesvvqcEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDgFEFMKQNQD----AFDVIITDSSDPMGPAESLFKesyyq 191
Cdd:PRK00536  94 --------DTHVDFVQADEKILDSFISFFPHFHEVKNNKN-FTHAKQLLDldikKYDLIICLQEPDIHKIDGLKR----- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  192 lmktALKEDGVLCCQGECQWLH----LDLIKEMRQFCQSLFPVVAyayctiPTYPSGQIGFMLCSKnpstNFQEPVQPLT 267
Cdd:PRK00536 160 ----MLKEDGVFISVAKHPLLEhvsmQNALKNMGDFFSIAMPFVA------PLRILSNKGYIYASF----KTHPLKDLML 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 63253298  268 QQQVAQMQLKYYNSDVHRAAFVLPEFARKALND 300
Cdd:PRK00536 226 QKIEALKSVRYYNEDIHRAAFALPKNLQEVFKD 258
PRK04457 PRK04457
polyamine aminopropyltransferase;
91-203 1.63e-13

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 68.91  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298   91 HPNPRKVLIIGGGDGGVLREVVKH-PSVESVVqCEIDEDVIQVSKK--FLPgmaigYSSSKLTLHVGDGFEFMKQNQDAF 167
Cdd:PRK04457  64 NPRPQHILQIGLGGGSLAKFIYTYlPDTRQTA-VEINPQVIAVARNhfELP-----ENGERFEVIEADGAEYIAVHRHST 137

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 63253298  168 DVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVL 203
Cdd:PRK04457 138 DVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIF 173
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-206 4.06e-10

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: 56.28  E-value: 4.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIQVSKKFlpgmAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 63253298 176 DPMGPAESLFKESYYQLMKTALKEDGVLCCQ 206
Cdd:cd02440  73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-207 6.67e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.98  E-value: 6.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  74 RDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIQVSKKFLPGMAIGysssKLTLHV 153
Cdd:COG0500   7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG----NVEFLV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 63253298 154 GDGFEFMKQNQDAFDVII-TDSSDPMGPAESlfkESYYQLMKTALKEDGVLCCQG 207
Cdd:COG0500  82 ADLAELDPLPAESFDLVVaFGVLHHLPPEER---EALLRELARALKPGGVLLLSA 133
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 92-203 1.28e-03

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: 38.07  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63253298  92 PNPRKVLIIGGGDGGVLREVVKHpsVESVVQCEIDEDVIQVSKKFLPGMAIgysssklTLHVGDgFEFMKQNQDAFDVII 171
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNV-------DFVQGD-LEDLPLEDGSFDLVI 92

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 63253298 172 TDSS-----DPmgpaESLFKEsyyqlMKTALKEDGVL 203
Cdd:COG2227  93 CSEVlehlpDP----AALLRE-----LARLLKPGGLL 120
 
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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