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Conserved domains on  [gi|1955857362|ref|XP_038886733|]
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thermospermine synthase ACAULIS5 isoform X1 [Benincasa hispida]

Protein Classification

spermidine/spermine synthase family protein( domain architecture ID 10010914)

spermidine/spermine synthase family protein similar to Arabidopsis thaliana thermospermine synthase ACAULIS5 that is required for correct xylem specification through regulation of the lifetime of the xylem elements

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 9-352 0e+00

spermine synthase


:

Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 589.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362   9 HTNGFSqsvdrnfeeksNYINGANSSHESVINNvngDDCHWYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGK 88
Cdd:PLN02823    6 HGNGTS-----------HITAVATPTAALASNY---AKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  89 TLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNR 168
Cdd:PLN02823   72 VLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 169 ETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVKDGPCYKLYTKSFYHDIVKPKLHHNGIFVTQAGPAGIFTHKEV 248
Cdd:PLN02823  152 EAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 249 FTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMASDHPFC-IKSEELDKRIEDRINGELLYLTGPSIVSSTILNKMVSLA 327
Cdd:PLN02823  232 FSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQA 311

                         330       340
                  ....*....|....*....|....*
gi 1955857362 328 LLNETHIYTEATAKFIHGQGVGFKQ 352
Cdd:PLN02823  312 LANETHVYTEENARFIHGHGTAAKA 336
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 9-352 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 589.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362   9 HTNGFSqsvdrnfeeksNYINGANSSHESVINNvngDDCHWYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGK 88
Cdd:PLN02823    6 HGNGTS-----------HITAVATPTAALASNY---AKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  89 TLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNR 168
Cdd:PLN02823   72 VLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 169 ETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVKDGPCYKLYTKSFYHDIVKPKLHHNGIFVTQAGPAGIFTHKEV 248
Cdd:PLN02823  152 EAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 249 FTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMASDHPFC-IKSEELDKRIEDRINGELLYLTGPSIVSSTILNKMVSLA 327
Cdd:PLN02823  232 FSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQA 311

                         330       340
                  ....*....|....*....|....*
gi 1955857362 328 LLNETHIYTEATAKFIHGQGVGFKQ 352
Cdd:PLN02823  312 LANETHVYTEENARFIHGHGTAAKA 336
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 49-308 8.54e-69

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: 216.91  E-value: 8.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  49 WYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGKTLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMG 128
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 129 GGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVkdG 208
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 209 PCYKLYTKSFYhDIVKPKLHHNGIFVTQAGpaGIFTHKEVFTSIYNTIKQTFNYVIAYTAYIPSF-ADTWGWVMASDHPF 287
Cdd:TIGR00417 159 PAETLFTKEFY-ELLKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260
                  ....*....|....*....|.
gi 1955857362 288 CIKSEELDKRIEDRINGELLY 308
Cdd:TIGR00417 236 RPLEVEIRRIKFEAEDGKTKY 256
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
87-282 5.28e-68

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 212.38  E-value: 5.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  87 GKTLMIDGKMQSA-EADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLT 165
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 166 VNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVkdGPCYKLYTKSFYHDiVKPKLHHNGIFVTQAGpaGIFTH 245
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1955857362 246 KEVFTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMA 282
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 103-287 5.39e-47

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: 157.87  E-value: 5.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 103 EFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETFCHSKLHLVIND 182
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 183 ARAELEKRREKYDIIIGDLADPVkdGPCYKLYTKSFYhDIVKPKLHHNGIFVTQAGpaGIFTHKEVFTSIYNTIKQTFNY 262
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFF-DLLKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....*.
gi 1955857362 263 VIAYTAYIPSFAD-TWGWVMASDHPF 287
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPL 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 128-202 5.74e-06

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: 44.73  E-value: 5.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955857362 128 GGGEGSAAREVLKHKSIEkVVMCDIDQDVVDFCRKhltvNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLA 202
Cdd:cd02440     6 GCGTGALALALASGPGAR-VTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 9-352 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 589.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362   9 HTNGFSqsvdrnfeeksNYINGANSSHESVINNvngDDCHWYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGK 88
Cdd:PLN02823    6 HGNGTS-----------HITAVATPTAALASNY---AKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  89 TLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNR 168
Cdd:PLN02823   72 VLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 169 ETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVKDGPCYKLYTKSFYHDIVKPKLHHNGIFVTQAGPAGIFTHKEV 248
Cdd:PLN02823  152 EAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 249 FTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMASDHPFC-IKSEELDKRIEDRINGELLYLTGPSIVSSTILNKMVSLA 327
Cdd:PLN02823  232 FSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQA 311

                         330       340
                  ....*....|....*....|....*
gi 1955857362 328 LLNETHIYTEATAKFIHGQGVGFKQ 352
Cdd:PLN02823  312 LANETHVYTEENARFIHGHGTAAKA 336
PRK00811 PRK00811
polyamine aminopropyltransferase;
49-301 1.06e-82

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 253.15  E-value: 1.06e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  49 WYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGKTLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMG 128
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 129 GGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHL-TVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVkd 207
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLpEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 208 GPCYKLYTKSFYHDIVKpKLHHNGIFVTQAG-PagiFTHKEVFTSIYNTIKQTFNYVIAYTAYIPSF-ADTWGWVMASDH 285
Cdd:PRK00811  163 GPAEGLFTKEFYENCKR-ALKEDGIFVAQSGsP---FYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKN 238

                         250
                  ....*....|....*...
gi 1955857362 286 PFC--IKSEELDKRIEDR 301
Cdd:PRK00811  239 DDLkfLPLDVIEARFAER 256
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 49-308 8.54e-69

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: 216.91  E-value: 8.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  49 WYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGKTLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMG 128
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 129 GGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVkdG 208
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 209 PCYKLYTKSFYhDIVKPKLHHNGIFVTQAGpaGIFTHKEVFTSIYNTIKQTFNYVIAYTAYIPSF-ADTWGWVMASDHPF 287
Cdd:TIGR00417 159 PAETLFTKEFY-ELLKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260
                  ....*....|....*....|.
gi 1955857362 288 CIKSEELDKRIEDRINGELLY 308
Cdd:TIGR00417 236 RPLEVEIRRIKFEAEDGKTKY 256
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
87-282 5.28e-68

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 212.38  E-value: 5.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  87 GKTLMIDGKMQSA-EADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLT 165
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 166 VNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVkdGPCYKLYTKSFYHDiVKPKLHHNGIFVTQAGpaGIFTH 245
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1955857362 246 KEVFTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMA 282
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
PRK03612 PRK03612
polyamine aminopropyltransferase;
72-286 8.31e-50

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 174.26  E-value: 8.31e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  72 TSEFQDIALLDTKRFGKT---LMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVV 148
Cdd:PRK03612  246 QTPYQRIVVTRRGNGRGPdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVEQVT 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 149 MCDIDQDVVDFCRKH---LTVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPvkDGPCY-KLYTKSFYHDiVK 224
Cdd:PRK03612  326 LVDLDPAMTELARTSpalRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDP--SNPALgKLYSVEFYRL-LK 402

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955857362 225 PKLHHNGIFVTQAGPAgiFTHKEVFTSIYNTIKQTFNYVIAYTAYIPSFADtWGWVMASDHP 286
Cdd:PRK03612  403 RRLAPDGLLVVQSTSP--YFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLAGAGA 461
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 103-287 5.39e-47

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: 157.87  E-value: 5.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 103 EFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETFCHSKLHLVIND 182
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 183 ARAELEKRREKYDIIIGDLADPVkdGPCYKLYTKSFYhDIVKPKLHHNGIFVTQAGpaGIFTHKEVFTSIYNTIKQTFNY 262
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFF-DLLKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....*.
gi 1955857362 263 VIAYTAYIPSFAD-TWGWVMASDHPF 287
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPL 181
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 66-260 6.12e-47

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 164.65  E-value: 6.12e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  66 RVLQKGTSEFQDIALLDTKRFgKTLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIE 145
Cdd:COG4262   233 PVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 146 KVVMCDIDQDVVDFCRKH---LTVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVKDGPcYKLYTKSFYHDi 222
Cdd:COG4262   312 SVTLVDLDPEVTDLAKTNpflRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSL-GKLYSVEFYRL- 389

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1955857362 223 VKPKLHHNGIFVTQAGPAgiFTHKEVFTSIYNTIKQTF 260
Cdd:COG4262   390 VRRHLAPGGVLVVQATSP--YFAPKAFWCIAKTLEAAG 425
PLN02366 PLN02366
spermidine synthase
 43-273 1.56e-41

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 147.48  E-value: 1.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  43 NGDDCH------WYEEIideNLKW-----SFALNRVLQKGTSEFQDIALLDTKRFGKTLMIDGKMQSAEADEFVYHECLI 111
Cdd:PLN02366    6 SEAKCHstvipgWFSEI---SPMWpgeahSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMIT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 112 HPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETFCHSKLHLVINDARAELEKRR 191
Cdd:PLN02366   83 HLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNAP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 192 E-KYDIIIGDLADPVkdGPCYKLYTKSFYHDIVKpKLHHNGIFVTQAgpAGIFTHKEVFTSIYNTIKQTF----NYviAY 266
Cdd:PLN02366  163 EgTYDAIIVDSSDPV--GPAQELFEKPFFESVAR-ALRPGGVVCTQA--ESMWLHMDLIEDLIAICRETFkgsvNY--AW 235


                  ....*..
gi 1955857362 267 TAyIPSF 273
Cdd:PLN02366  236 TT-VPTY 241
speE PRK01581
polyamine aminopropyltransferase;
73-293 4.02e-35

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 132.01  E-value: 4.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362  73 SEFQDIALLDTKRFgkTLMIDGKMQSAEADEFVYHECLIHPALLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDI 152
Cdd:PRK01581  105 SNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 153 DQDVVDFCR---KHLTVNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLADPVKDgPCYKLYTKSFYHDIVKpKLHH 229
Cdd:PRK01581  183 DGSMINMARnvpELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATE-LLSTLYTSELFARIAT-FLTE 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955857362 230 NGIFVTQA-GPAGIfthKEVFTSIYNTIKQTFNYVIAYTAYIPSFADTWGWVMASDHPFCIKSEE 293
Cdd:PRK01581  261 DGAFVCQSnSPADA---PLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIE 322
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 49-100 1.52e-09

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: 53.05  E-value: 1.52e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1955857362  49 WYEEIIDENLKWSFALNRVLQKGTSEFQDIALLDTKRFGKTLMIDGKMQSAE 100
Cdd:pfam17284   2 WFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 128-202 5.74e-06

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: 44.73  E-value: 5.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955857362 128 GGGEGSAAREVLKHKSIEkVVMCDIDQDVVDFCRKhltvNRETFCHSKLHLVINDARAELEKRREKYDIIIGDLA 202
Cdd:cd02440     6 GCGTGALALALASGPGAR-VTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
PRK04457 PRK04457
polyamine aminopropyltransferase;
115-235 1.06e-04

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 43.49  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955857362 115 LLCHSNPKTVFIMGGGEGSAAREVLKHKSIEKVVMCDIDQDVVDFCRKHLTVNRETfchSKLHLVINDARAELEKRREKY 194
Cdd:PRK04457   61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENG---ERFEVIEADGAEYIAVHRHST 137

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1955857362 195 DIIIGDLADpvKDGPCYKLYTKSFYHDiVKPKLHHNGIFVT 235
Cdd:PRK04457  138 DVILVDGFD--GEGIIDALCTQPFFDD-CRNALSSDGIFVV 175
 
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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