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Conserved domains on  [gi|1028925456|gb|ANF14956|]
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spermidine synthase [Clostridium butyricum]

Protein Classification

spermidine synthase( domain architecture ID 10011535)

spermidine synthase catalyzes the irreversible transfer of a propylamine group from S-adenosylmethioninamine to putrescine to form spermidine

CATH:  2.30.140.10
EC:  2.5.1.16
Gene Symbol:  speE
Gene Ontology:  GO:0004766|GO:0008295
SCOP:  4003319

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
1-274 1.28e-173

polyamine aminopropyltransferase;


:

Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 480.42  E-value: 1.28e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   1 MELWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVL 80
Cdd:PRK00811    2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  81 VIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRL-NDERVNLFFEDGLRFVRNKENEYDLIIVDSTDP 159
Cdd:PRK00811   82 IIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAyDDPRVELVIGDGIKFVAETENSFDVIIVDSTDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 160 FGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFGFASKNY 239
Cdd:PRK00811  162 VGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFY--QADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKND 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1028925456 240 DP---VKDLNAERWNNLNIDTKYYNTELHSGCFALPNY 274
Cdd:PRK00811  240 DLkflPLDVIEARFAERGIKTRYYNPELHKAAFALPQF 277
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
1-274 1.28e-173

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 480.42  E-value: 1.28e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   1 MELWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVL 80
Cdd:PRK00811    2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  81 VIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRL-NDERVNLFFEDGLRFVRNKENEYDLIIVDSTDP 159
Cdd:PRK00811   82 IIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAyDDPRVELVIGDGIKFVAETENSFDVIIVDSTDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 160 FGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFGFASKNY 239
Cdd:PRK00811  162 VGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFY--QADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKND 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1028925456 240 DP---VKDLNAERWNNLNIDTKYYNTELHSGCFALPNY 274
Cdd:PRK00811  240 DLkflPLDVIEARFAERGIKTRYYNPELHKAAFALPQF 277
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
4-274 1.54e-108

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: 315.52  E-value: 1.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   4 WYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVIG 83
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  84 AGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPG 163
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 164 EGLFTKEFYGNCYKALKEDGILVNQHESPYYEKyaKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFGFASKN-YDPV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQL--ELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNkYRPL 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1028925456 243 K-DLNAERWNNLNIDTKYYNTELHSGCFALPNY 274
Cdd:TIGR00417 239 EvEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
42-235 1.26e-91

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 269.39  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  42 GRFFTLDGMMMVT-EKDEFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLP 120
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 121 QTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKA 200
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFY--GLDL 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1028925456 201 MQDAHEKIYGLFKVHRVYQAHIPTYpSGHWLFGFA 235
Cdd:COG0421   161 LRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
58-238 2.46e-68

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: 209.87  E-value: 2.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  58 EFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFED 137
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 138 GLRFVRNKENEYDLIIVDSTDPFGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYEKYakAMQDAHEKIYGLFKVHRV 217
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLE--LIINILKNGKQVFPVVMP 158
                         170       180
                  ....*....|....*....|.
gi 1028925456 218 YQAHIPTYPSGHWLFGFASKN 238
Cdd:pfam01564 159 YVATIPTYPSGGWGFTVCSKN 179
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
78-186 6.12e-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: 58.21  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  78 NVLVIGAGDGGTVRELVKYKSIEnIDMVEIDKRVVEvcmeYLPQTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDst 157
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGAR-VTGVDISPVALE----LARKAAAALLADNVEVLKGDAEELPPEADESFDVIISD-- 73
                          90       100
                  ....*....|....*....|....*....
gi 1028925456 158 DPFGPGEGLFtKEFYGNCYKALKEDGILV 186
Cdd:cd02440    74 PPLHHLVEDL-ARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
1-274 1.28e-173

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 480.42  E-value: 1.28e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   1 MELWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVL 80
Cdd:PRK00811    2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  81 VIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRL-NDERVNLFFEDGLRFVRNKENEYDLIIVDSTDP 159
Cdd:PRK00811   82 IIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAyDDPRVELVIGDGIKFVAETENSFDVIIVDSTDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 160 FGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFGFASKNY 239
Cdd:PRK00811  162 VGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFY--QADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKND 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1028925456 240 DP---VKDLNAERWNNLNIDTKYYNTELHSGCFALPNY 274
Cdd:PRK00811  240 DLkflPLDVIEARFAERGIKTRYYNPELHKAAFALPQF 277
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
4-274 1.54e-108

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: 315.52  E-value: 1.54e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   4 WYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVIG 83
Cdd:TIGR00417   1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  84 AGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPG 163
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 164 EGLFTKEFYGNCYKALKEDGILVNQHESPYYEKyaKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFGFASKN-YDPV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQL--ELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNkYRPL 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1028925456 243 K-DLNAERWNNLNIDTKYYNTELHSGCFALPNY 274
Cdd:TIGR00417 239 EvEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
42-235 1.26e-91

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 269.39  E-value: 1.26e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  42 GRFFTLDGMMMVT-EKDEFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLP 120
Cdd:COG0421     3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 121 QTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKA 200
Cdd:COG0421    83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFY--GLDL 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1028925456 201 MQDAHEKIYGLFKVHRVYQAHIPTYpSGHWLFGFA 235
Cdd:COG0421   161 LRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
PLN02366 PLN02366
spermidine synthase
2-272 2.36e-76

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 234.92  E-value: 2.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   2 ELWYTEQHtenvrfSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLV 81
Cdd:PLN02366   24 PMWPGEAH------SLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  82 IGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFEDGLRFVRN-KENEYDLIIVDSTDPF 160
Cdd:PLN02366   98 VGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAIIVDSSDPV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 161 GPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYekYAKAMQDAHEKIYGLFKVHRVYQ-AHIPTYPSGHWLFGFASKNY 239
Cdd:PLN02366  178 GPAQELFEKPFFESVARALRPGGVVCTQAESMWL--HMDLIEDLIAICRETFKGSVNYAwTTVPTYPSGVIGFVLCSKEG 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1028925456 240 DPVKDLNAERwnnlNIDT-----------KYYNTELHSGCFALP 272
Cdd:PLN02366  256 PAVDFKHPVN----PIDKlegagkakrplKFYNSEVHRAAFCLP 295
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
58-238 2.46e-68

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: 209.87  E-value: 2.46e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  58 EFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFED 137
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 138 GLRFVRNKENEYDLIIVDSTDPFGPGEGLFTKEFYGNCYKALKEDGILVNQHESPYYEKYakAMQDAHEKIYGLFKVHRV 217
Cdd:pfam01564  81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLE--LIINILKNGKQVFPVVMP 158
                         170       180
                  ....*....|....*....|.
gi 1028925456 218 YQAHIPTYPSGHWLFGFASKN 238
Cdd:pfam01564 159 YVATIPTYPSGGWGFTVCSKN 179
PLN02823 PLN02823
spermine synthase
3-272 7.51e-57

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 185.65  E-value: 7.51e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   3 LWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVI 82
Cdd:PLN02823   31 LWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  83 GAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPF-- 160
Cdd:PLN02823  111 GGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVeg 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 161 GPGEGLFTKEFYGN-CYKALKEDGILVNQHESPYYEKYAKAMQDAHEKIYGLFKVHRVYQAHIPTYPSgHWLFGFASKny 239
Cdd:PLN02823  191 GPCYQLYTKSFYERiVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFAD-TWGWVMASD-- 267
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1028925456 240 DPVKDLNAERWNN-----LNIDTKYYNTELHSGCFALP 272
Cdd:PLN02823  268 HPFADLSAEELDSrikerIDGELKYLDGETFSSAFALN 305
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
23-204 1.02e-53

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 180.06  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  23 LHSEQTEFQRIDILESKEFGRFFtLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENI 102
Cdd:COG4262   235 VYSEQTPYQRIVVTRDKDDRRLY-LNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVESV 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 103 DMVEIDKRVVEVCMEYLPQTAC---RLNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPGEG-LFTKEFYGNCYKA 178
Cdd:COG4262   314 TLVDLDPEVTDLAKTNPFLRELnggALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLVRRH 393
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1028925456 179 LKEDGILVNQHESPYYEK-----YAKAMQDA 204
Cdd:COG4262   394 LAPGGVLVVQATSPYFAPkafwcIAKTLEAA 424
PRK03612 PRK03612
polyamine aminopropyltransferase;
24-272 1.94e-41

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 149.22  E-value: 1.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  24 HSEQTEFQRIDILESK-EFG---RFFtLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSI 99
Cdd:PRK03612  243 YAEQTPYQRIVVTRRGnGRGpdlRLY-LNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDV 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 100 ENIDMVEIDKRVVEVCMEYLPQTACR---LNDERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPGEG-LFTKEFYGNC 175
Cdd:PRK03612  322 EQVTLVDLDPAMTELARTSPALRALNggaLDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFYRLL 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 176 YKALKEDGILVNQHESPYYEKYA-----KAMQDAhekiyGlFKVhRVYQAHIPTYpsGHWLFGFASKNYDPVKDLNAErw 250
Cdd:PRK03612  402 KRRLAPDGLLVVQSTSPYFAPKAfwsieATLEAA-----G-LAT-TPYHVNVPSF--GEWGFVLAGAGARPPLAVPTE-- 470
                         250       260
                  ....*....|....*....|..
gi 1028925456 251 nnLNIDTKYYNTELHSGCFALP 272
Cdd:PRK03612  471 --LPVPLRFLDPALLAAAFVFP 490
speE PRK01581
polyamine aminopropyltransferase;
23-192 2.49e-26

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 106.20  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  23 LHSEQTEFQRIDILESKEFgRFFtLDGMMMVTEKDEFIYHDMIVHVPMAVNPDIKNVLVIGAGDGGTVRELVKYKSIENI 102
Cdd:PRK01581  100 LFAEKSNYQNINLLQVSDI-RLY-LDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 103 DMVEIDKRVVEVCMEyLPQTAcRLN-----DERVNLFFEDGLRFVRNKENEYDLIIVDSTDPFGPG-EGLFTKEFYGNCY 176
Cdd:PRK01581  178 DLVDLDGSMINMARN-VPELV-SLNksaffDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFARIA 255
                         170
                  ....*....|....*.
gi 1028925456 177 KALKEDGILVNQHESP 192
Cdd:PRK01581  256 TFLTEDGAFVCQSNSP 271
speE PRK00536
spermidine synthase; Provisional
3-274 5.24e-22

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 92.23  E-value: 5.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456   3 LWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVtEKDEFIYHDMIVHVPMAVNPDIKNVLVI 82
Cdd:PRK00536    1 MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLF-KNFLHIESELLAHMGGCTKKELKEVLIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  83 GAGDGGTVRELVKYKSieNIDMVEIDKRVVEVCMEYLPQTACRLNDERVNLFFEdglrFVRNKENEYDLIIVDStdpfgp 162
Cdd:PRK00536   80 DGFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQ----LLDLDIKKYDLIICLQ------ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456 163 gegLFTKEFYGNCYKALKEDGILVNQHESPYYEKyaKAMQDAHEKIYGLFKVHRVYQAHIPTYPSGHWLFgfASKNYDPV 242
Cdd:PRK00536  148 ---EPDIHKIDGLKRMLKEDGVFISVAKHPLLEH--VSMQNALKNMGDFFSIAMPFVAPLRILSNKGYIY--ASFKTHPL 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1028925456 243 KDLNAERWNNLNiDTKYYNTELHSGCFALPNY 274
Cdd:PRK00536  221 KDLMLQKIEALK-SVRYYNEDIHRAAFALPKN 251
PRK04457 PRK04457
polyamine aminopropyltransferase;
73-186 8.46e-15

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 72.38  E-value: 8.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  73 NPDIKNVLVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVC--MEYLPQtacrlNDERVNLFFEDGLRFVRNKENEYD 150
Cdd:PRK04457   64 NPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVArnHFELPE-----NGERFEVIEADGAEYIAVHRHSTD 138
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1028925456 151 LIIVDSTDPFGPGEGLFTKEFYGNCYKALKEDGILV 186
Cdd:PRK04457  139 VILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFV 174
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
3-55 3.45e-14

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: 65.38  E-value: 3.45e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1028925456   3 LWYTEQHTENVRFSIKVEKQLHSEQTEFQRIDILESKEFGRFFTLDGMMMVTE 55
Cdd:pfam17284   1 GWFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
78-186 6.12e-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: 58.21  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  78 NVLVIGAGDGGTVRELVKYKSIEnIDMVEIDKRVVEvcmeYLPQTACRLNDERVNLFFEDGLRFVRNKENEYDLIIVDst 157
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGAR-VTGVDISPVALE----LARKAAAALLADNVEVLKGDAEELPPEADESFDVIISD-- 73
                          90       100
                  ....*....|....*....|....*....
gi 1028925456 158 DPFGPGEGLFtKEFYGNCYKALKEDGILV 186
Cdd:cd02440    74 PPLHHLVEDL-ARFLEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
80-185 4.23e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028925456  80 LVIGAGDGGTVRELVKYKSIENIDMVEIDKRVVEVCMEYLPQtACRLNDERVNLFFEDGLRFVRNKeneYDLIIVDST-- 157
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAA-LGLLNAVRVELFQLDLGELDPGS---FDVVVASNVlh 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1028925456 158 ---DPfgpgeglftKEFYGNCYKALKEDGIL 185
Cdd:pfam08242  77 hlaDP---------RAVLRNIRRLLKPGGVL 98
 
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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