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Conserved domains on  [gi|242117904|ref|NP_957328|]
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spermidine synthase [Danio rerio]

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
 1-287 1.31e-158

spermidine synthase


:

Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 443.70  E-value: 1.31e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   1 MDNIKDGWFTETCTLWPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHP 80
Cdd:PLN02366  11 HSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  81 CPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKK-NQDAFDIII 159
Cdd:PLN02366  91 NPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAII 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 160 TDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFP-VVDYAYCTIPTYPSGQIGFML 238
Cdd:PLN02366 171 VDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGVIGFVL 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242117904 239 CSKNSKT-NFREPLRELTRDEIESMS---LKYYNPEIHRAAFILPEFARKVLS 287
Cdd:PLN02366 251 CSKEGPAvDFKHPVNPIDKLEGAGKAkrpLKFYNSEVHRAAFCLPSFAKRELE 303
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 1-287 1.31e-158

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 443.70  E-value: 1.31e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   1 MDNIKDGWFTETCTLWPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHP 80
Cdd:PLN02366  11 HSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  81 CPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKK-NQDAFDIII 159
Cdd:PLN02366  91 NPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAII 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 160 TDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFP-VVDYAYCTIPTYPSGQIGFML 238
Cdd:PLN02366 171 VDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGVIGFVL 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242117904 239 CSKNSKT-NFREPLRELTRDEIESMS---LKYYNPEIHRAAFILPEFARKVLS 287
Cdd:PLN02366 251 CSKEGPAvDFKHPVNPIDKLEGAGKAkrpLKFYNSEVHRAAFCLPSFAKRELE 303
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 8-281 3.20e-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: 370.60  E-value: 3.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904    8 WFTETCTlwPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHPCPKKVLI 87
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   88 IGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVG 167
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  168 PAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFPVVDYAYCTIPTYPSGQIGFMLCSKNSKTNF 247
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 242117904  248 REPLRELtRDEIESMSLKYYNPEIHRAAFILPEF 281
Cdd:TIGR00417 239 EVEIRRI-KFEAEDGKTKYYNPDIHKAAFVLPKW 271
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 64-242 3.31e-94

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: 275.74  E-value: 3.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   64 EFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGD 143
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  144 GFEFMKKNQDAFDIIITDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFPVVDYAY 223
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170
                  ....*....|....*....
gi 242117904  224 CTIPTYPSGQIGFMLCSKN 242
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
48-239 3.75e-75

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 227.79  E-value: 3.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  48 GNVLILDGVIQCT-ERDEFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLP 126
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 127 GMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIK 206
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 242117904 207 EM-RTFcKTLFPVVDYAYCTIPTYpSGQIGFMLC 239
Cdd:COG0421  163 RVlATL-REVFPHVVLYAAPVPTY-GGGNVFLLA 194
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-194 4.63e-11

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: 58.60  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  84 KVLIIGGGDGGVLREVVKHPlVESVVQCEIDEDVINVSKKylpgMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIItdsS 163
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 242117904 164 DPVGPAESLFKESYYQLMKTALCEGGILCCQ 194
Cdd:cd02440   73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PLN02366 PLN02366
spermidine synthase
 1-287 1.31e-158

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 443.70  E-value: 1.31e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   1 MDNIKDGWFTETCTLWPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHP 80
Cdd:PLN02366  11 HSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  81 CPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKK-NQDAFDIII 159
Cdd:PLN02366  91 NPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAII 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 160 TDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFP-VVDYAYCTIPTYPSGQIGFML 238
Cdd:PLN02366 171 VDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGVIGFVL 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 242117904 239 CSKNSKT-NFREPLRELTRDEIESMS---LKYYNPEIHRAAFILPEFARKVLS 287
Cdd:PLN02366 251 CSKEGPAvDFKHPVNPIDKLEGAGKAkrpLKFYNSEVHRAAFCLPSFAKRELE 303
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 8-281 3.20e-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: 370.60  E-value: 3.20e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904    8 WFTETCTlwPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHPCPKKVLI 87
Cdd:TIGR00417   1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   88 IGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVG 167
Cdd:TIGR00417  79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  168 PAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFPVVDYAYCTIPTYPSGQIGFMLCSKNSKTNF 247
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 242117904  248 REPLRELtRDEIESMSLKYYNPEIHRAAFILPEF 281
Cdd:TIGR00417 239 EVEIRRI-KFEAEDGKTKYYNPDIHKAAFVLPKW 271
PRK00811 PRK00811
polyamine aminopropyltransferase;
5-287 1.00e-123

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 354.46  E-value: 1.00e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   5 KDGWFTETCTlwPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCHPCPKK 84
Cdd:PRK00811   2 MELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  85 VLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFS-PKLTLHVGDGFEFMKKNQDAFDIIITDSS 163
Cdd:PRK00811  80 VLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDdPRVELVIGDGIKFVAETENSFDVIIVDST 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 164 DPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFPVVDYAYCTIPTYPSGQIGFMLCSKNS 243
Cdd:PRK00811 160 DPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKND 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 242117904 244 KTNFREPLRELTRDEIESMSLKYYNPEIHRAAFILPEFARKVLS 287
Cdd:PRK00811 240 DLKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 64-242 3.31e-94

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: 275.74  E-value: 3.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   64 EFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGD 143
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  144 GFEFMKKNQDAFDIIITDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIKEMRTFCKTLFPVVDYAY 223
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160

                         170
                  ....*....|....*....
gi 242117904  224 CTIPTYPSGQIGFMLCSKN 242
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
48-239 3.75e-75

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 227.79  E-value: 3.75e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  48 GNVLILDGVIQCT-ERDEFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLP 126
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 127 GMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVGPAESLFKESYYQLMKTALCEGGILCCQGECQWLHLELIK 206
Cdd:COG0421   83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 242117904 207 EM-RTFcKTLFPVVDYAYCTIPTYpSGQIGFMLC 239
Cdd:COG0421  163 RVlATL-REVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02823 PLN02823
spermine synthase
 1-288 1.22e-64

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 206.07  E-value: 1.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904   1 MDNIKDG-WFTETctLWPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTERDEFSYQEMIANLPLCCH 79
Cdd:PLN02823  24 ASNYAKSlWYEEE--IEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHH 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  80 PCPKKVLIIGGGDGGVLREVVKHPLVESVVQCEIDEDVINVSKKYLPGMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIII 159
Cdd:PLN02823 102 PNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVII 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 160 TDSSDPV--GPAESLFKESYYQLM-KTALCEGGILCCQGECQWL--HLELIKEMRTFCKTLFP-VVDYAYCtIPTYPSgQ 233
Cdd:PLN02823 182 GDLADPVegGPCYQLYTKSFYERIvKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKyVVPYTAH-VPSFAD-T 259

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242117904 234 IGFMLCSKnsktnfrEPLRELTRDEIESM-------SLKYYNPEIHRAAFILPEFARKVLSE 288
Cdd:PLN02823 260 WGWVMASD-------HPFADLSAEELDSRikeridgELKYLDGETFSSAFALNKTVRQALAN 314
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 26-191 8.43e-40

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 143.47  E-value: 8.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  26 EEVLYHKKSKFQDVMVFKSKTYGNvLILDGVIQCTERDEFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHPLV 105
Cdd:COG4262  232 DPVVYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDV 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 106 ESVVQCEIDEDVINVSKK--YLPGMAKGFF-SPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPvgPAESLFK---ESYYQ 179
Cdd:COG4262  311 ESVTLVDLDPEVTDLAKTnpFLRELNGGALnDPRVTVVNADAFQFLRETDEKYDVIIVDLPDP--SNFSLGKlysVEFYR 388

                        170
                 ....*....|..
gi 242117904 180 LMKTALCEGGIL 191
Cdd:COG4262  389 LVRRHLAPGGVL 400
PRK03612 PRK03612
polyamine aminopropyltransferase;
27-279 1.38e-30

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 119.94  E-value: 1.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  27 EVLYHKKSKFQDVMVFKSK-TYGNV--LILDGVIQCTERDEFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHP 103
Cdd:PRK03612 240 PVVYAEQTPYQRIVVTRRGnGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYP 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 104 LVESVVQCEIDEDVINVSKKYlPGMAK----GFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVGPAES-LFKESYY 178
Cdd:PRK03612 320 DVEQVTLVDLDPAMTELARTS-PALRAlnggALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFY 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 179 QLMKTALCEGGILCCQG-------ECQWlhlelikemrTFCKTL----FPVVDYaYCTIPTYpsGQIGFMLCSKNSktnf 247
Cdd:PRK03612 399 RLLKRRLAPDGLLVVQStspyfapKAFW----------SIEATLeaagLATTPY-HVNVPSF--GEWGFVLAGAGA---- 461

                        250       260       270
                 ....*....|....*....|....*....|..
gi 242117904 248 REPLRELTRDeieSMSLKYYNPEIHRAAFILP 279
Cdd:PRK03612 462 RPPLAVPTEL---PVPLRFLDPALLAAAFVFP 490
speE PRK01581
polyamine aminopropyltransferase;
28-194 4.60e-25

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 102.74  E-value: 4.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  28 VLYHKKSKFQDVMVFKSKTYGnvLILDGVIQCTERDEFSYQEMIAnlplccHPC------PKKVLIIGGGDGGVLREVVK 101
Cdd:PRK01581  99 NLFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALV------HPImskvidPKRVLILGGGDGLALREVLK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 102 HPLVESVVQCEIDEDVINVSKKyLPGMAK----GFFSPKLTLHVGDGFEFMKKNQDAFDIIITDSSDPVGPAES-LFKES 176
Cdd:PRK01581 171 YETVLHVDLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSE 249

                        170
                 ....*....|....*...
gi 242117904 177 YYQLMKTALCEGGILCCQ 194
Cdd:PRK01581 250 LFARIATFLTEDGAFVCQ 267
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 7-61 6.94e-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: 6.94e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 242117904    7 GWFTETCTlwPGQAMSLQVEEVLYHKKSKFQDVMVFKSKTYGNVLILDGVIQCTE 61
Cdd:pfam17284   1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
speE PRK00536
spermidine synthase; Provisional
 25-288 1.39e-15

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 74.90  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  25 VEEVLYHKKSKFQDVMVFKSKTYGNVLILDGviQCTERDEFSYQ-EMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHP 103
Cdd:PRK00536  17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 104 LVESVVQCeiDEDVINVSKKYLPGMAKGFFSPKLTLHVgdgfEFMKKNQDAFDIIITDSSDPVGPAESLFKesyyqlmkt 183
Cdd:PRK00536  95 THVDFVQA--DEKILDSFISFFPHFHEVKNNKNFTHAK----QLLDLDIKKYDLIICLQEPDIHKIDGLKR--------- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904 184 ALCEGGILCCQGECQWLHLEL----IKEMRTFCKTLFPVVdyAYCTIptypSGQIGFMLCSKNSktnfrEPLRELTRDEI 259
Cdd:PRK00536 160 MLKEDGVFISVAKHPLLEHVSmqnaLKNMGDFFSIAMPFV--APLRI----LSNKGYIYASFKT-----HPLKDLMLQKI 228

                        250       260       270
                 ....*....|....*....|....*....|
gi 242117904 260 ESM-SLKYYNPEIHRAAFILPEFARKVLSE 288
Cdd:PRK00536 229 EALkSVRYYNEDIHRAAFALPKNLQEVFKD 258
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-194 4.63e-11

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: 58.60  E-value: 4.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  84 KVLIIGGGDGGVLREVVKHPlVESVVQCEIDEDVINVSKKylpgMAKGFFSPKLTLHVGDGFEFMKKNQDAFDIIItdsS 163
Cdd:cd02440    1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVII---S 72

                         90       100       110
                 ....*....|....*....|....*....|.
gi 242117904 164 DPVGPAESLFKESYYQLMKTALCEGGILCCQ 194
Cdd:cd02440   73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK04457 PRK04457
polyamine aminopropyltransferase;
79-191 8.82e-10

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 58.13  E-value: 8.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  79 HPCPKKVLIIGGGDGGVLREVVKH-PLVESVVqCEIDEDVINVSKKYlpgmakgFFSP----KLTLHVGDGFEFMKKNQD 153
Cdd:PRK04457  64 NPRPQHILQIGLGGGSLAKFIYTYlPDTRQTA-VEINPQVIAVARNH-------FELPengeRFEVIEADGAEYIAVHRH 135

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 242117904 154 AFDIIITDSSDPVGPAESLFKESYYQLMKTALCEGGIL 191
Cdd:PRK04457 136 STDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIF 173
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 62-195 2.86e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242117904  62 RDEFSYQEMIANLPLCCHPCPKKVLIIGGGDGGVLREVVKHpLVESVVQCEIDEDVINVSKKylpgMAKGFFSPKLTLHV 141
Cdd:COG0500    7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARA----RAAKAGLGNVEFLV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 242117904 142 GDGFEFMKKNQDAFDIII-TDSSDPVGPAESlfkESYYQLMKTALCEGGILCCQG 195
Cdd:COG0500   82 ADLAELDPLPAESFDLVVaFGVLHHLPPEER---EALLRELARALKPGGVLLLSA 133
 
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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