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Conserved domains on  [gi|2396517608|ref|XP_002314705|]
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thermospermine synthase ACAULIS5 [Populus trichocarpa]

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
 1-335 0e+00

spermine synthase


:

Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 667.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608   1 MGDISCSNGISSGNGVNGKSHSSLNGYRKSCWYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQ 80
Cdd:PLN02823    1 AVEIVHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  81 SAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLE 160
Cdd:PLN02823   81 SAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 161 VIINDARAELEIGKECYDVIIGDLADPIEGGPCYKLYTKSFYEHTVKPRLNQGGIFITQAGPAGIFSHTEVFSCIYNTLR 240
Cdd:PLN02823  161 LIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 241 QVFKYVVPYSAHIPSYADTWGWVMASDSPFM-LSADELDTRIKQRIEGENRYLDGKTFSSASTLSKAVRKSLDTETHVYT 319
Cdd:PLN02823  241 QVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYT 320

                         330
                  ....*....|....*.
gi 2396517608 320 EGAARFIYGHGSVHKQ 335
Cdd:PLN02823  321 EENARFIHGHGTAAKA 336
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 1-335 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 667.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608   1 MGDISCSNGISSGNGVNGKSHSSLNGYRKSCWYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQ 80
Cdd:PLN02823    1 AVEIVHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  81 SAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLE 160
Cdd:PLN02823   81 SAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 161 VIINDARAELEIGKECYDVIIGDLADPIEGGPCYKLYTKSFYEHTVKPRLNQGGIFITQAGPAGIFSHTEVFSCIYNTLR 240
Cdd:PLN02823  161 LIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 241 QVFKYVVPYSAHIPSYADTWGWVMASDSPFM-LSADELDTRIKQRIEGENRYLDGKTFSSASTLSKAVRKSLDTETHVYT 319
Cdd:PLN02823  241 QVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYT 320

                         330
                  ....*....|....*.
gi 2396517608 320 EGAARFIYGHGSVHKQ 335
Cdd:PLN02823  321 EENARFIHGHGTAAKA 336
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
70-265 2.23e-73

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 225.86  E-value: 2.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  70 GKALVIDGKLQSA-EVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLA 148
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 149 VNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIegGPCYKLYTKSFYEHtVKPRLNQGGIFITQAGpaGIFSH 228
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2396517608 229 TEVFSCIYNTLRQVFKYVVPYSAHIPSYADTWGWVMA 265
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 32-305 1.15e-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: 219.22  E-value: 1.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  32 WYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMG 111
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 112 GGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIegG 191
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 192 PCYKLYTKSFYEhTVKPRLNQGGIFITQAGpaGIFSHTEVFSCIYNTLRQVFKYVVPYSAHIPSY-ADTWGWVMASDSPF 270
Cdd:TIGR00417 159 PAETLFTKEFYE-LLKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2396517608 271 M-LSADelDTRIKQRIE-GENRYLDGKTFSSASTLSK 305
Cdd:TIGR00417 236 RpLEVE--IRRIKFEAEdGKTKYYNPDIHKAAFVLPK 270
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 86-269 6.69e-49

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: 162.49  E-value: 6.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  86 EFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLEVIIND 165
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 166 ARAELEIGKECYDVIIGDLADPIegGPCYKLYTKSFYEHtVKPRLNQGGIFITQAGpaGIFSHTEVFSCIYNTLRQVFKY 245
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....
gi 2396517608 246 VVPYSAHIPSYAdTWGWVMASDSP 269
Cdd:pfam01564 156 VMPYVATIPTYP-SGGWGFTVCSK 178
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 100-246 2.99e-06

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 48.69  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 100 HHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVvnfckayLAVNREAF-CDP-RLEVIINDARAEL-EIGKEC 176
Cdd:NF037959  272 MGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAV-------TRVAAEDFwFDPaSATVLHEDARRALrRRPEER 344

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2396517608 177 YDVIIGD----LADPieggpcYKLYTKSFYEhTVKPRLNQGGIFITQAgpagI--FSHTEVFSCIYNTLRQVFKYV 246
Cdd:NF037959  345 FDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVV 409
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-219 3.77e-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: 45.11  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 111 GGGEGSTAREILRHKtVEKVVMCDIDEEVVNFCKAylavNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLAdpieg 190
Cdd:cd02440     6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75

                          90       100
                  ....*....|....*....|....*....
gi 2396517608 191 GPCYKLYTKSFYEhTVKPRLNQGGIFITQ 219
Cdd:cd02440    76 LHHLVEDLARFLE-EARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PLN02823 PLN02823
spermine synthase
 1-335 0e+00

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 667.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608   1 MGDISCSNGISSGNGVNGKSHSSLNGYRKSCWYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQ 80
Cdd:PLN02823    1 AVEIVHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  81 SAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLE 160
Cdd:PLN02823   81 SAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 161 VIINDARAELEIGKECYDVIIGDLADPIEGGPCYKLYTKSFYEHTVKPRLNQGGIFITQAGPAGIFSHTEVFSCIYNTLR 240
Cdd:PLN02823  161 LIINDARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 241 QVFKYVVPYSAHIPSYADTWGWVMASDSPFM-LSADELDTRIKQRIEGENRYLDGKTFSSASTLSKAVRKSLDTETHVYT 319
Cdd:PLN02823  241 QVFKYVVPYTAHVPSFADTWGWVMASDHPFAdLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYT 320

                         330
                  ....*....|....*.
gi 2396517608 320 EGAARFIYGHGSVHKQ 335
Cdd:PLN02823  321 EENARFIHGHGTAAKA 336
PRK00811 PRK00811
polyamine aminopropyltransferase;
32-312 1.69e-85

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 260.09  E-value: 1.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  32 WYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMG 111
Cdd:PRK00811    5 WFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 112 GGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYL-AVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIeg 190
Cdd:PRK00811   85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLpEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV-- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 191 GPCYKLYTKSFYEHtVKPRLNQGGIFITQAG-PagiFSHTEVFSCIYNTLRQVFKYVVPYSAHIPSY-ADTWGWVMASDS 268
Cdd:PRK00811  163 GPAEGLFTKEFYEN-CKRALKEDGIFVAQSGsP---FYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKN 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2396517608 269 PF--MLSADELDTRIKQRiEGENRYLDGKTFSSASTLSKAVRKSLD 312
Cdd:PRK00811  239 DDlkFLPLDVIEARFAER-GIKTRYYNPELHKAAFALPQFVKDALK 283
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
70-265 2.23e-73

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 225.86  E-value: 2.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  70 GKALVIDGKLQSA-EVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLA 148
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 149 VNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIegGPCYKLYTKSFYEHtVKPRLNQGGIFITQAGpaGIFSH 228
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYED-CRRALKPGGVLVVNLG--SPFYG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2396517608 229 TEVFSCIYNTLRQVFKYVVPYSAHIPSYADTWGWVMA 265
Cdd:COG0421   158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 32-305 1.15e-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: 219.22  E-value: 1.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  32 WYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMG 111
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 112 GGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIegG 191
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 192 PCYKLYTKSFYEhTVKPRLNQGGIFITQAGpaGIFSHTEVFSCIYNTLRQVFKYVVPYSAHIPSY-ADTWGWVMASDSPF 270
Cdd:TIGR00417 159 PAETLFTKEFYE-LLKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2396517608 271 M-LSADelDTRIKQRIE-GENRYLDGKTFSSASTLSK 305
Cdd:TIGR00417 236 RpLEVE--IRRIKFEAEdGKTKYYNPDIHKAAFVLPK 270
PRK03612 PRK03612
polyamine aminopropyltransferase;
50-309 8.38e-61

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 203.53  E-value: 8.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  50 ILHTGASRYQDIAL---LDTKPFGKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKT 126
Cdd:PRK03612  241 VVYAEQTPYQRIVVtrrGNGRGPDLRLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPD 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 127 VEKVVMCDIDEEVVNFCKAY---LAVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADP--IEGGpcyKLYTKSF 201
Cdd:PRK03612  321 VEQVTLVDLDPAMTELARTSpalRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPsnPALG---KLYSVEF 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 202 YeHTVKPRLNQGGIFITQAGPAgiFSHTEVFSCIYNTLRQVFKYVVPYSAHIPSYADtWGWVMASDSPfmlsadELDTRI 281
Cdd:PRK03612  398 Y-RLLKRRLAPDGLLVVQSTSP--YFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLAGAGA------RPPLAV 467

                         250       260
                  ....*....|....*....|....*...
gi 2396517608 282 KQRIEGENRYLDGKTFSSASTLSKAVRK 309
Cdd:PRK03612  468 PTELPVPLRFLDPALLAAAFVFPKDMRR 495
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 50-243 9.22e-57

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 190.46  E-value: 9.22e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  50 ILHTGASRYQDIALLDTKPFgKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEK 129
Cdd:COG4262   234 VVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVES 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 130 VVMCDIDEEVVNFCKAY---LAVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIEGGPcYKLYTKSFYEHtV 206
Cdd:COG4262   313 VTLVDLDPEVTDLAKTNpflRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSL-GKLYSVEFYRL-V 390

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2396517608 207 KPRLNQGGIFITQAGPAGIFShtEVFSCIYNTLRQVF 243
Cdd:COG4262   391 RRHLAPGGVLVVQATSPYFAP--KAFWCIAKTLEAAG 425
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 86-269 6.69e-49

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: 162.49  E-value: 6.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  86 EFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLEVIIND 165
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 166 ARAELEIGKECYDVIIGDLADPIegGPCYKLYTKSFYEHtVKPRLNQGGIFITQAGpaGIFSHTEVFSCIYNTLRQVFKY 245
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155

                         170       180
                  ....*....|....*....|....
gi 2396517608 246 VVPYSAHIPSYAdTWGWVMASDSP 269
Cdd:pfam01564 156 VMPYVATIPTYP-SGGWGFTVCSK 178
PLN02366 PLN02366
spermidine synthase
 50-256 1.46e-44

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 155.19  E-value: 1.46e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  50 ILHTGASRYQDIALLDTKPFGKALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTVEK 129
Cdd:PLN02366   38 VLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQ 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 130 VVMCDIDEEVVNFCKAY---LAVnreAFCDPRLEVIINDARAELE-IGKECYDVIIGDLADPIegGPCYKLYTKSFYEhT 205
Cdd:PLN02366  118 IDICEIDKMVIDVSKKFfpdLAV---GFDDPRVNLHIGDGVEFLKnAPEGTYDAIIVDSSDPV--GPAQELFEKPFFE-S 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2396517608 206 VKPRLNQGGIFITQAgpAGIFSHTEVFSCIYNTLRQVFKYVVPY-SAHIPSY 256
Cdd:PLN02366  192 VARALRPGGVVCTQA--ESMWLHMDLIEDLIAICRETFKGSVNYaWTTVPTY 241
speE PRK01581
polyamine aminopropyltransferase;
48-276 8.94e-40

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 144.34  E-value: 8.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  48 NSILHTGASRYQDIALLDTKPFgkALVIDGKLQSAEVDEFIYHESLVHPAFLHHSSPKTVFIMGGGEGSTAREILRHKTV 127
Cdd:PRK01581   97 HTNLFAEKSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETV 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 128 EKVVMCDIDEEVVNFCK---AYLAVNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLADPIEgGPCYKLYTKSFYEH 204
Cdd:PRK01581  175 LHVDLVDLDGSMINMARnvpELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPAT-ELLSTLYTSELFAR 253

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2396517608 205 tVKPRLNQGGIFITQA-GPAgifSHTEVFSCIYNTLRQVFKYVVPYSAHIPSYADTWGWVMASDSPFMLSADE 276
Cdd:PRK01581  254 -IATFLTEDGAFVCQSnSPA---DAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQIE 322
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 32-83 1.14e-11

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: 59.21  E-value: 1.14e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2396517608  32 WYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQSAE 83
Cdd:pfam17284   2 WFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 100-246 2.99e-06

fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.


Pssm-ID: 468290 [Multi-domain]  Cd Length: 480  Bit Score: 48.69  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 100 HHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVvnfckayLAVNREAF-CDP-RLEVIINDARAEL-EIGKEC 176
Cdd:NF037959  272 MGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAV-------TRVAAEDFwFDPaSATVLHEDARRALrRRPEER 344

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2396517608 177 YDVIIGD----LADPieggpcYKLYTKSFYEhTVKPRLNQGGIFITQAgpagI--FSHTEVFSCIYNTLRQVFKYV 246
Cdd:NF037959  345 FDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVV 409
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-219 3.77e-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: 45.11  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 111 GGGEGSTAREILRHKtVEKVVMCDIDEEVVNFCKAylavNREAFCDPRLEVIINDARAELEIGKECYDVIIGDLAdpieg 190
Cdd:cd02440     6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75

                          90       100
                  ....*....|....*....|....*....
gi 2396517608 191 GPCYKLYTKSFYEhTVKPRLNQGGIFITQ 219
Cdd:cd02440    76 LHHLVEDLARFLE-EARRLLKPGGVLVLT 103
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 129-217 9.10e-05

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 42.48  E-value: 9.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 129 KVVMCDIDEEVVNFCKAYLAvnrEAFCDPRLEVIINDARAELE-IGKECYDVIIGDlADPIEggpcYKLYtksfYEHtVK 207
Cdd:COG4122    43 RLTTIEIDPERAAIARENFA---RAGLADRIRLILGDALEVLPrLADGPFDLVFID-ADKSN----YPDY----LEL-AL 109

                          90
                  ....*....|
gi 2396517608 208 PRLNQGGIFI 217
Cdd:COG4122   110 PLLRPGGLIV 119
PRK04457 PRK04457
polyamine aminopropyltransferase;
99-218 1.04e-04

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 43.49  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  99 LHHSSPKTVFIMGGGEGSTAREILRHKTVEKVVMCDIDEEVVnfckaylAVNREAFCDP----RLEVIINDARAELEIGK 174
Cdd:PRK04457   62 LFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVI-------AVARNHFELPengeRFEVIEADGAEYIAVHR 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2396517608 175 ECYDVIIGDLADpiEGGPCYKLYTKSFYeHTVKPRLNQGGIFIT 218
Cdd:PRK04457  135 HSTDVILVDGFD--GEGIIDALCTQPFF-DDCRNALSSDGIFVV 175
speE PRK00536
spermidine synthase; Provisional
 32-311 1.65e-04

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 42.54  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608  32 WYEEEIEENLRWCFALNSILHTGASRYQDIALLDTKPFGKALVIDGKLQsaeVDEFIYHES--LVHPAFLHHSSPKTVFI 109
Cdd:PRK00536    2 WITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLL---FKNFLHIESelLAHMGGCTKKELKEVLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 110 MGGGEGSTAREILRHKTveKVVMCDIDEEVVNFCKAYLAVNREAFCDPRLEVIinDARAELEIGKecYDVIIgdladpie 189
Cdd:PRK00536   79 VDGFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTHA--KQLLDLDIKK--YDLII-------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2396517608 190 ggpCYKLYTKsfyeHTVKP---RLNQGGIFITQAgpAGIFSHTEVFSCIYNTLRQVFKYVVPYSAHIPSYADTwGWVMAS 266
Cdd:PRK00536  145 ---CLQEPDI----HKIDGlkrMLKEDGVFISVA--KHPLLEHVSMQNALKNMGDFFSIAMPFVAPLRILSNK-GYIYAS 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2396517608 267 DSpFMLSADELdtriKQRIEGEN--RYLDGKTFSSASTLSKAVRKSL 311
Cdd:PRK00536  215 FK-THPLKDLM----LQKIEALKsvRYYNEDIHRAAFALPKNLQEVF 256
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 111-181 1.32e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 37.54  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2396517608 111 GGGEGSTAREILRHkTVEKVVMCDIDEEVVNFCKAYLAVNreafcDPRLEVIINDARaELEIGKECYDVII 181
Cdd:pfam13649   5 GCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEA-----GLNVEFVQGDAE-DLPFPDGSFDLVV 68
 
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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