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Conserved domains on  [gi|26390475|dbj|BAC25903|]
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unnamed protein product [Mus musculus]

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 1.42e-155

spermidine synthase


:

Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 436.77  E-value: 1.42e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26390475  246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 8-298 1.42e-155

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 436.77  E-value: 1.42e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26390475  246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 20-293 6.78e-133

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: 377.92  E-value: 6.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 26390475   260 REPVQQLTQAQvEQMQLKYYNSDMHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 76-255 7.17e-101

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: 293.46  E-value: 7.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170       180
                  ....*....|....*....|
gi 26390475   236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 1.82e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 234.34  E-value: 1.82e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475 139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                       170       180       190
                ....*....|....*....|....*....|...
gi 26390475 219 EMRHFCKSLFPVVDYAYCSIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-206 5.80e-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: 55.51  E-value: 5.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 26390475 176 DPMGPAESLFKESYYQLMKTALKEDGILCCQ 206
Cdd:cd02440  73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 8-298 1.42e-155

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 436.77  E-value: 1.42e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 26390475  246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 20-293 6.78e-133

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: 377.92  E-value: 6.78e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 26390475   260 REPVQQLTQAQvEQMQLKYYNSDMHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
PRK00811 PRK00811
polyamine aminopropyltransferase;
18-299 6.44e-125

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 357.93  E-value: 6.44e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   18 EGWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK00811   3 ELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSD 176
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  177 PMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPS 256
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 26390475  257 TNFRePVQQLTQAQVE-QMQLKYYNSDMHRAAFVLPEFTRKALN 299
Cdd:PRK00811 241 LKFL-PLDVIEARFAErGIKTRYYNPELHKAAFALPQFVKDALK 283
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 76-255 7.17e-101

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: 293.46  E-value: 7.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170       180
                  ....*....|....*....|
gi 26390475   236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 1.82e-77

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 234.34  E-value: 1.82e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475 139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDHIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                       170       180       190
                ....*....|....*....|....*....|...
gi 26390475 219 EMRHFCKSLFPVVDYAYCSIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02823 PLN02823
spermine synthase
 4-298 7.51e-62

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 199.14  E-value: 7.51e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475    4 GPDGPAAPGPAAIREG-WFRETcsLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEM 82
Cdd:PLN02823  15 AVATPTAALASNYAKSlWYEEE--IEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHES 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   83 IANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQ 162
Cdd:PLN02823  93 LVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  163 NQDAFDVIITDSSDPM--GPAESLFKESYYQLM-KTALKEDGILCCQGECQWL--HLDHIKEMRHFCKSLFP-VVDYAYC 236
Cdd:PLN02823 173 RDEKFDVIIGDLADPVegGPCYQLYTKSFYERIvKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKyVVPYTAH 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26390475  237 sIPTYPSgQIGFMLCSKNPSTNF-REPVQQLTQAQVEqMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02823 253 -VPSFAD-TWGWVMASDHPFADLsAEELDSRIKERID-GELKYLDGETFSSAFALNKTVRQAL 312
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 27-203 2.51e-45

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 158.49  E-value: 2.51e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSKTYGNvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLII 100
Cdd:COG4262 215 LVFADPIESSAEQKLygdpvvYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVL 293

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475 101 GGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKK--FLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDP 177
Cdd:COG4262 294 GGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDP 373

                       170       180
                ....*....|....*....|....*....
gi 26390475 178 mgPAESLFK---ESYYQLMKTALKEDGIL 203
Cdd:COG4262 374 --SNFSLGKlysVEFYRLVRRHLAPGGVL 400
PRK03612 PRK03612
polyamine aminopropyltransferase;
27-206 3.84e-34

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 129.96  E-value: 3.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSK-TYGNV--LVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK03612 222 FVLADRIETTAEQLLygdpvvYAEQTPYQRIVVTRRGnGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRV 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKF-----LPGMAvgFSSSKLTLHVGDGFEFMKQNQDAFDVIIT 172
Cdd:PRK03612 302 LVLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSpalraLNGGA--LDDPRVTVVNDDAFNWLRKLAEKFDVIIV 379

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 26390475  173 DSSDPMGPAES-LFKESYYQLMKTALKEDGILCCQ 206
Cdd:PRK03612 380 DLPDPSNPALGkLYSVEFYRLLKRRLAPDGLLVVQ 414
speE PRK01581
polyamine aminopropyltransferase;
41-206 4.80e-24

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 100.42  E-value: 4.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   41 LHHRRSRYQDILVFRSKTYGnvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV 120
Cdd:PRK01581 100 LFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  121 VQCEIDEDVIEVSKKfLPGMAV----GFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAES-LFKESYYQLMKT 195
Cdd:PRK01581 178 DLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARIAT 256

                        170
                 ....*....|.
gi 26390475  196 ALKEDGILCCQ 206
Cdd:PRK01581 257 FLTEDGAFVCQ 267
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 19-73 1.06e-22

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: 88.49  E-value: 1.06e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26390475    19 GWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTE 73
Cdd:pfam17284   1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
speE PRK00536
spermidine synthase; Provisional
 37-301 3.14e-18

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 82.21  E-value: 3.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   37 VEQLLHHRRSRYQDILVFRSKTYGNVLVLDGviQCTERDEFSYQ-EMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHP 115
Cdd:PRK00536  17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  116 SVESVVQCeiDEDVIEVSKKFLPGMAVGFSSSKLTLHVgdgfEFMKQNQDAFDVIITDSSDPMGPAESLFKesyyqlmkt 195
Cdd:PRK00536  95 THVDFVQA--DEKILDSFISFFPHFHEVKNNKNFTHAK----QLLDLDIKKYDLIICLQEPDIHKIDGLKR--------- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  196 ALKEDGILCCQGECQWLH----LDHIKEMRHFCKSLFPVVdyAYCSIptypSGQIGFMLCSKNpstnfREPVQQLTQAQV 271
Cdd:PRK00536 160 MLKEDGVFISVAKHPLLEhvsmQNALKNMGDFFSIAMPFV--APLRI----LSNKGYIYASFK-----THPLKDLMLQKI 228

                        250       260       270
                 ....*....|....*....|....*....|.
gi 26390475  272 EQMQ-LKYYNSDMHRAAFVLPEFTRKALNDI 301
Cdd:PRK00536 229 EALKsVRYYNEDIHRAAFALPKNLQEVFKDN 259
PRK04457 PRK04457
polyamine aminopropyltransferase;
91-203 1.53e-13

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 68.91  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475   91 HPNPRKVLIIGGGDGGVLREVVKH-PSVESVVqCEIDEDVIEVSKK--FLPgmavgFSSSKLTLHVGDGFEFMKQNQDAF 167
Cdd:PRK04457  64 NPRPQHILQIGLGGGSLAKFIYTYlPDTRQTA-VEINPQVIAVARNhfELP-----ENGERFEVIEADGAEYIAVHRHST 137

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 26390475  168 DVIITDSSDPMGPAESLFKESYYQLMKTALKEDGIL 203
Cdd:PRK04457 138 DVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIF 173
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 96-206 5.80e-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: 55.51  E-value: 5.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 26390475 176 DPMGPAESLFKESYYQLMKTALKEDGILCCQ 206
Cdd:cd02440  73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-207 5.64e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.37  E-value: 5.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  74 RDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFLPGMAVGfsssKLTLHV 153
Cdd:COG0500   7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG----NVEFLV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26390475 154 GDGFEFMKQNQDAFDVII-TDSSDPMGPAESlfkESYYQLMKTALKEDGILCCQG 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 7.63e-04

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: 38.85  E-value: 7.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26390475  92 PNPRKVLIIGGGDGGVLREVVKHpsVESVVQCEIDEDVIEVSKKFLPGMAVgfsssklTLHVGDgFEFMKQNQDAFDVII 171
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNV-------DFVQGD-LEDLPLEDGSFDLVI 92

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26390475 172 TDSS-----DPmgpaESLFKEsyyqlMKTALKEDGIL 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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