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Conserved domains on  [gi|6678131|ref|NP_033298|]
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spermidine synthase [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 6.28e-157

spermidine synthase


:

Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 440.24  E-value: 6.28e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678131   246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
8-298 6.28e-157

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 440.24  E-value: 6.28e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678131   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 1.75e-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: 379.46  E-value: 1.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 6678131    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 7.63e-102

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: 295.77  E-value: 7.63e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
                         170       180
                  ....*....|....*....|
gi 6678131    236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 6.90e-78

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 235.49  E-value: 6.90e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131  139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
                       170       180       190
                ....*....|....*....|....*....|...
gi 6678131  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 6678131   96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 6678131  176 DPMGPAESLFKESYYQLMKTALKEDGILCCQ 206
Cdd:cd02440  73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
8-298 6.28e-157

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 440.24  E-value: 6.28e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366   6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366  86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6678131   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 1.75e-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: 379.46  E-value: 1.75e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 6678131    260 REPVQQLTQAQvEQMQLKYYNSDMHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
PRK00811 PRK00811
polyamine aminopropyltransferase;
18-299 3.67e-126

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 361.01  E-value: 3.67e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    18 EGWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK00811   3 ELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSD 176
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   177 PMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPS 256
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 6678131   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 7.63e-102

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: 295.77  E-value: 7.63e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
                         170       180
                  ....*....|....*....|
gi 6678131    236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-251 6.90e-78

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 235.49  E-value: 6.90e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421   3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131  139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIK 218
Cdd:COG0421  83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
                       170       180       190
                ....*....|....*....|....*....|...
gi 6678131  219 EMRHFCKSLFPVVDYAYCSIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02823 PLN02823
spermine synthase
4-298 1.21e-62

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 201.45  E-value: 1.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131     4 GPDGPAAPGPAAIREG-WFRETcsLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEM 82
Cdd:PLN02823  15 AVATPTAALASNYAKSlWYEEE--IEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHES 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    83 IANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQ 162
Cdd:PLN02823  93 LVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   163 NQDAFDVIITDSSDPM--GPAESLFKESYYQLM-KTALKEDGILCCQGECQWL--HLDLIKEMRHFCKSLFP-VVDYAYC 236
Cdd:PLN02823 173 RDEKFDVIIGDLADPVegGPCYQLYTKSFYERIvKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKyVVPYTAH 252
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678131   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 6678131   27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSKTYGNvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLII 100
Cdd:COG4262 215 LVFADPIESSAEQKLygdpvvYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVL 293
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131  101 GGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKK--FLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDP 177
Cdd:COG4262 294 GGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDP 373
                       170       180
                ....*....|....*....|....*....
gi 6678131  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 6678131    27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSK-TYGNV--LVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK03612 222 FVLADRIETTAEQLLygdpvvYAEQTPYQRIVVTRRGnGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRV 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKF-----LPGMAvgFSSSKLTLHVGDGFEFMKQNQDAFDVIIT 172
Cdd:PRK03612 302 LVLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSpalraLNGGA--LDDPRVTVVNDDAFNWLRKLAEKFDVIIV 379
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 6678131   173 DSSDPMGPAES-LFKESYYQLMKTALKEDGILCCQ 206
Cdd:PRK03612 380 DLPDPSNPALGkLYSVEFYRLLKRRLAPDGLLVVQ 414
speE PRK01581
polyamine aminopropyltransferase;
41-206 4.14e-24

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 100.42  E-value: 4.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    41 LHHRRSRYQDILVFRSKTYGnvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV 120
Cdd:PRK01581 100 LFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   121 VQCEIDEDVIEVSKKfLPGMAV----GFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAES-LFKESYYQLMKT 195
Cdd:PRK01581 178 DLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARIAT 256
                        170
                 ....*....|.
gi 6678131   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 6678131     19 GWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTE 73
Cdd:pfam17284   1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
speE PRK00536
spermidine synthase; Provisional
37-301 4.41e-18

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 81.83  E-value: 4.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131    37 VEQLLHHRRSRYQDILVFRSKTYGNVLVLDGviQCTERDEFSYQ-EMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHP 115
Cdd:PRK00536  17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   116 SVESVVQCeiDEDVIEVSKKFLPGMAVGFSSSKLTLHVgdgfEFMKQNQDAFDVIITDSSDPMGPAESLFKesyyqlmkt 195
Cdd:PRK00536  95 THVDFVQA--DEKILDSFISFFPHFHEVKNNKNFTHAK----QLLDLDIKKYDLIICLQEPDIHKIDGLKR--------- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131   196 ALKEDGILCCQGECQWLH----LDLIKEMRHFCKSLFPVVdyAYCSIptypSGQIGFMLCSKNpstnfREPVQQLTQAQV 271
Cdd:PRK00536 160 MLKEDGVFISVAKHPLLEhvsmQNALKNMGDFFSIAMPFV--APLRI----LSNKGYIYASFK-----THPLKDLMLQKI 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 6678131   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 6678131    91 HPNPRKVLIIGGGDGGVLREVVKH-PSVESVVqCEIDEDVIEVSKK--FLPgmavgFSSSKLTLHVGDGFEFMKQNQDAF 167
Cdd:PRK04457  64 NPRPQHILQIGLGGGSLAKFIYTYlPDTRQTA-VEINPQVIAVARNhfELP-----ENGERFEVIEADGAEYIAVHRHST 137
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 6678131   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 6678131   96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440   1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72
                        90       100       110
                ....*....|....*....|....*....|.
gi 6678131  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 6678131   74 RDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFLPGMAVGfsssKLTLHV 153
Cdd:COG0500   7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG----NVEFLV 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6678131  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 6678131   92 PNPRKVLIIGGGDGGVLREVVKHpsVESVVQCEIDEDVIEVSKKFLPGMAVgfsssklTLHVGDgFEFMKQNQDAFDVII 171
Cdd:COG2227  23 PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNV-------DFVQGD-LEDLPLEDGSFDLVI 92
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6678131  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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