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Conserved domains on  [gi|654547830|ref|WP_028015536|]
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MULTISPECIES: polyamine aminopropyltransferase [Enterobacter]

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
PubMed:  3316212|20051267|11731804
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;
3-284 5.41e-179

polyamine aminopropyltransferase;


:

Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 494.29  E-value: 5.41e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   3 DHTLWH-ETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHV 81
Cdd:PRK00811   1 SMELWFtETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  82 LIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTD 161
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 162 PIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAAIPTYYGGIMTFAWATDNDV 241
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 654547830 242 LRHLSTEIIQARFHQAGLTCRYYNPAIHTAAFALPQYLQDALS 284
Cdd:PRK00811 241 LKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
3-284 5.41e-179

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 494.29  E-value: 5.41e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   3 DHTLWH-ETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHV 81
Cdd:PRK00811   1 SMELWFtETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  82 LIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTD 161
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 162 PIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAAIPTYYGGIMTFAWATDNDV 241
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 654547830 242 LRHLSTEIIQARFHQAGLTCRYYNPAIHTAAFALPQYLQDALS 284
Cdd:PRK00811 241 LKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 7-278 1.10e-162

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: 452.65  E-value: 1.10e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830    7 WHETLHDQ-FGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIG 85
Cdd:TIGR00417   1 WFTEYHDKnFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   86 GGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNaGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGP 165
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  166 GASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAAIPTYYGGIMTFAWATDNDvLRHL 245
Cdd:TIGR00417 160 AETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNK-YRPL 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 654547830  246 STEIIQARFHQAGLTCRYYNPAIHTAAFALPQY 278
Cdd:TIGR00417 239 EVEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
44-236 5.05e-91

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 268.23  E-value: 5.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  44 GRVMALDGVVQTT-ERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLP 122
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 123 NHnAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEA 202
Cdd:COG0421   83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 654547830 203 LDSHRKLSTYFGDVSFYQAAIPTYYGGiMTFAWA 236
Cdd:COG0421  162 RRVLATLREVFPHVVLYAAPVPTYGGG-NVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 60-240 1.91e-86

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: 256.09  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   60 EFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHnAGSYDDPRFNLVID 139
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSL-AIGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  140 DGVNFVNQTTQTFDVIISDCTDPIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFY 219
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170       180
                  ....*....|....*....|.
gi 654547830  220 QAAIPTYYGGIMTFAWATDND 240
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKNP 180
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 81-191 6.62e-08

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: 49.74  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  81 VLIIGGGDGAMLREVSRHRSIEtITMVEIDAGVVSFCRQYLPNHNAgsyddPRFNLVIDDGVNFVNQTTQTFDVIISDCT 160
Cdd:cd02440    2 VLDLGCGTGALALALASGPGAR-VTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 654547830 161 DPIGPGaslFTSSFYEGCKRCLNPGGIFVAQ 191
Cdd:cd02440   76 LHHLVE---DLARFLEEARRLLKPGGVLVLT 103
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 45-233 1.26e-04

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: 43.29  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  45 RVMALDGVVQ-TTERDE----FI-YHEMMTHVPLLAHGHAK-HVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFC 117
Cdd:NF037959 236 RLMVLDHLAHgINARDDptvlFTpYAAMLDELARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 118 RQYLpnhnagSYDDPRFNLVIDDG-VNFVNQTTQTFDVIISDC-TDpIGPGASLFTSSFYEGCKRCLNPGGIFvAQNGVC 195
Cdd:NF037959 316 AEDF------WFDPASATVLHEDArRALRRRPEERFDVIVGDAfTD-IAVPAHLVTREFFELVRARLTPDGVY-LMNVID 387

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 654547830 196 FLQQDEALDS-HRKLSTYFGDVSFYQAAIPTYYGGIMTF 233
Cdd:NF037959 388 HADRLRALAAlVATLREVFPVVEVWTEARPPAPGERRTF 426
 
Name Accession Description Interval E-value
PRK00811 PRK00811
polyamine aminopropyltransferase;
3-284 5.41e-179

polyamine aminopropyltransferase;


Pssm-ID: 234843 [Multi-domain]  Cd Length: 283  Bit Score: 494.29  E-value: 5.41e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   3 DHTLWH-ETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHV 81
Cdd:PRK00811   1 SMELWFtETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  82 LIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTD 161
Cdd:PRK00811  81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 162 PIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAAIPTYYGGIMTFAWATDNDV 241
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 654547830 242 LRHLSTEIIQARFHQAGLTCRYYNPAIHTAAFALPQYLQDALS 284
Cdd:PRK00811 241 LKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
speE TIGR00417
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ...
 7-278 1.10e-162

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: 452.65  E-value: 1.10e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830    7 WHETLHDQ-FGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIG 85
Cdd:TIGR00417   1 WFTEYHDKnFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   86 GGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNaGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGP 165
Cdd:TIGR00417  81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLA-GSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  166 GASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAAIPTYYGGIMTFAWATDNDvLRHL 245
Cdd:TIGR00417 160 AETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNK-YRPL 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 654547830  246 STEIIQARFHQAGLTCRYYNPAIHTAAFALPQY 278
Cdd:TIGR00417 239 EVEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
44-236 5.05e-91

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


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 268.23  E-value: 5.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  44 GRVMALDGVVQTT-ERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLP 122
Cdd:COG0421    3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 123 NHnAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEA 202
Cdd:COG0421   83 LL-APAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 654547830 203 LDSHRKLSTYFGDVSFYQAAIPTYYGGiMTFAWA 236
Cdd:COG0421  162 RRVLATLREVFPHVVLYAAPVPTYGGG-NVFLLA 194
Spermine_synth pfam01564
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ...
 60-240 1.91e-86

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: 256.09  E-value: 1.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   60 EFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHnAGSYDDPRFNLVID 139
Cdd:pfam01564   1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSL-AIGFQDPRVKVVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  140 DGVNFVNQTTQTFDVIISDCTDPIGPGASLFTSSFYEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFY 219
Cdd:pfam01564  80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPY 159

                         170       180
                  ....*....|....*....|.
gi 654547830  220 QAAIPTYYGGIMTFAWATDND 240
Cdd:pfam01564 160 VATIPTYPSGGWGFTVCSKNP 180
PLN02366 PLN02366
spermidine synthase
 19-286 4.38e-86

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 259.96  E-value: 4.38e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  19 FAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRH 98
Cdd:PLN02366  33 LKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  99 RSIETITMVEIDAGVVSFCRQYLPNHNAGsYDDPRFNLVIDDGVNFV-NQTTQTFDVIISDCTDPIGPGASLFTSSFYEG 177
Cdd:PLN02366 113 SSVEQIDICEIDKMVIDVSKKFFPDLAVG-FDDPRVNLHIGDGVEFLkNAPEGTYDAIIVDSSDPVGPAQELFEKPFFES 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 178 CKRCLNPGGIfvaqngVCflQQDEALDSHRKL---------STYFGDVSFYQAAIPTYYGGIMTFAWAT----DNDVLRH 244
Cdd:PLN02366 192 VARALRPGGV------VC--TQAESMWLHMDLiedliaicrETFKGSVNYAWTTVPTYPSGVIGFVLCSkegpAVDFKHP 263

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 654547830 245 LSTEIIQARFHQAGLTCRYYNPAIHTAAFALPQYLQDALSTK 286
Cdd:PLN02366 264 VNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESL 305
PLN02823 PLN02823
spermine synthase
 3-284 8.30e-70

spermine synthase


Pssm-ID: 178418 [Multi-domain]  Cd Length: 336  Bit Score: 219.17  E-value: 8.30e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   3 DHTLW-HETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHV 81
Cdd:PLN02823  28 AKSLWyEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  82 LIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPnHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTD 161
Cdd:PLN02823 108 FIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLT-VNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLAD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 162 PI--GPGASLFTSSFYEG-CKRCLNPGGIFVAQNG-VCFLQQDEALDS-HRKLSTYFGDVSFYQAAIPTY---YGGIMtf 233
Cdd:PLN02823 187 PVegGPCYQLYTKSFYERiVKPKLNPGGIFVTQAGpAGILTHKEVFSSiYNTLRQVFKYVVPYTAHVPSFadtWGWVM-- 264

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 654547830 234 awATDNDvLRHLSTEIIQARFHQAGL-TCRYYNPAIHTAAFALPQYLQDALS 284
Cdd:PLN02823 265 --ASDHP-FADLSAEELDSRIKERIDgELKYLDGETFSSAFALNKTVRQALA 313
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 6-191 3.85e-52

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


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 176.21  E-value: 3.85e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   6 LWHETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFgRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIG 85
Cdd:COG4262  216 VFADPIESSAEQKLYGDPVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLG 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  86 GGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQ--YLPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPI 163
Cdd:COG4262  295 GGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPS 374

                        170       180
                 ....*....|....*....|....*....
gi 654547830 164 GPG-ASLFTSSFYEGCKRCLNPGGIFVAQ 191
Cdd:COG4262  375 NFSlGKLYSVEFYRLVRRHLAPGGVLVVQ 403
PRK03612 PRK03612
polyamine aminopropyltransferase;
22-193 6.08e-43

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 153.45  E-value: 6.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  22 DNVLYHEKTDHQDLIIFENA-AFGRVMAL--DGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRH 98
Cdd:PRK03612 239 DPVVYAEQTPYQRIVVTRRGnGRGPDLRLylNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKY 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  99 RSIETITMVEIDAGVVSFCRQY--LPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGPG-ASLFTSSFY 175
Cdd:PRK03612 319 PDVEQVTLVDLDPAMTELARTSpaLRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPAlGKLYSVEFY 398

                        170
                 ....*....|....*...
gi 654547830 176 EGCKRCLNPGGIFVAQNG 193
Cdd:PRK03612 399 RLLKRRLAPDGLLVVQST 416
speE PRK01581
polyamine aminopropyltransferase;
23-192 8.74e-26

polyamine aminopropyltransferase;


Pssm-ID: 234961 [Multi-domain]  Cd Length: 374  Bit Score: 104.66  E-value: 8.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  23 NVLYHEKTDHQDLIIFENAAFGrvMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIE 102
Cdd:PRK01581  98 TNLFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 103 TITMVEIDAGVVSFCRQY--LPNHNAGSYDDPRFNLVIDDGVNFVNQTTQTFDVIISDCTDPIGPGAS-LFTSSFYEGCK 179
Cdd:PRK01581 176 HVDLVDLDGSMINMARNVpeLVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARIA 255

                        170
                 ....*....|...
gi 654547830 180 RCLNPGGIFVAQN 192
Cdd:PRK01581 256 TFLTEDGAFVCQS 268
Spermine_synt_N pfam17284
Spermidine synthase tetramerization domain; This domain represents the N-terminal ...
 6-57 2.31e-19

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: 79.63  E-value: 2.31e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 654547830    6 LWHETLHD-QFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTE 57
Cdd:pfam17284   1 GWFTEIHDlGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
PRK04457 PRK04457
polyamine aminopropyltransferase;
66-189 4.48e-16

polyamine aminopropyltransferase;


Pssm-ID: 179854 [Multi-domain]  Cd Length: 262  Bit Score: 76.23  E-value: 4.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  66 MMthVPLLAHGHAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQ--YLPnhnagsYDDPRFNLVIDDGVN 143
Cdd:PRK04457  57 MM--GFLLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNhfELP------ENGERFEVIEADGAE 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654547830 144 FVNQTTQTFDVIISDCTDPIGPGASLFTSSFYEGCKRCLNPGGIFV 189
Cdd:PRK04457 129 YIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFV 174
speE PRK00536
spermidine synthase; Provisional
 15-283 1.13e-10

spermidine synthase; Provisional


Pssm-ID: 134311 [Multi-domain]  Cd Length: 262  Bit Score: 60.64  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  15 FGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVqTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLRE 94
Cdd:PRK00536  11 LRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQL-LFKNFLHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  95 VSRHRSieTITMVEIDAGVVSFCRQYLPnHNAGSYDDPRFNLViddgVNFVNQTTQTFDVIISDctdpigpgaSLFTSSF 174
Cdd:PRK00536  90 LFKYDT--HVDFVQADEKILDSFISFFP-HFHEVKNNKNFTHA----KQLLDLDIKKYDLIICL---------QEPDIHK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 175 YEGCKRCLNPGGIFVAQNGVCFLQQDEALDSHRKLSTYFGDVSFYQAaiPTYYGGIMTFAWATDN-DVLRHLSTEIIQAR 253
Cdd:PRK00536 154 IDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVA--PLRILSNKGYIYASFKtHPLKDLMLQKIEAL 231

                        250       260       270
                 ....*....|....*....|....*....|
gi 654547830 254 FHqagltCRYYNPAIHTAAFALPQYLQDAL 283
Cdd:PRK00536 232 KS-----VRYYNEDIHRAAFALPKNLQEVF 256
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 81-191 6.62e-08

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: 49.74  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  81 VLIIGGGDGAMLREVSRHRSIEtITMVEIDAGVVSFCRQYLPNHNAgsyddPRFNLVIDDGVNFVNQTTQTFDVIISDCT 160
Cdd:cd02440    2 VLDLGCGTGALALALASGPGAR-VTGVDISPVALELARKAAAALLA-----DNVEVLKGDAEELPPEADESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 654547830 161 DPIGPGaslFTSSFYEGCKRCLNPGGIFVAQ 191
Cdd:cd02440   76 LHHLVE---DLARFLEEARRLLKPGGVLVLT 103
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 66-216 8.94e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 45.18  E-value: 8.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  66 MMTHVPLLAHGHakhVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQylpnhNAGSYDDPRFNLVIDDGvnFV 145
Cdd:COG2813   41 LLEHLPEPLGGR---VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARA-----NAAANGLENVEVLWSDG--LS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 146 NQTTQTFDVIIS--------DCTDPIGpgaslftSSFYEGCKRCLNPGG--IFVAQNGvcflqqdeaLDSHRKLSTYFGD 215
Cdd:COG2813  111 GVPDGSFDLILSnppfhagrAVDKEVA-------HALIADAARHLRPGGelWLVANRH---------LPYERKLEELFGN 174


                 .
gi 654547830 216 V 216
Cdd:COG2813  175 V 175
MFS_SpdSyn NF037959
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ...
 45-233 1.26e-04

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: 43.29  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  45 RVMALDGVVQ-TTERDE----FI-YHEMMTHVPLLAHGHAK-HVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFC 117
Cdd:NF037959 236 RLMVLDHLAHgINARDDptvlFTpYAAMLDELARLRMGRADfSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVA 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830 118 RQYLpnhnagSYDDPRFNLVIDDG-VNFVNQTTQTFDVIISDC-TDpIGPGASLFTSSFYEGCKRCLNPGGIFvAQNGVC 195
Cdd:NF037959 316 AEDF------WFDPASATVLHEDArRALRRRPEERFDVIVGDAfTD-IAVPAHLVTREFFELVRARLTPDGVY-LMNVID 387

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 654547830 196 FLQQDEALDS-HRKLSTYFGDVSFYQAAIPTYYGGIMTF 233
Cdd:NF037959 388 HADRLRALAAlVATLREVFPVVEVWTEARPPAPGERRTF 426
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
77-191 3.25e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 39.04  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  77 HAKHVLIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNhnagsyddprFNLVIDDGVNFvnQTTQTFDVII 156
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN----------VRFVVADLRDL--DPPEPFDLVV 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 654547830 157 SdctdpigpGASLF----TSSFYEGCKRCLNPGGIFVAQ 191
Cdd:COG4106   69 S--------NAALHwlpdHAALLARLAAALAPGGVLAVQ 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 79-189 4.49e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 39.23  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  79 KHVLIIGGGDGAMLREVSRHRsiETITMVEIDAGVVSFCRQYLPNHNAgsyddprfNLVIDDGVNFvNQTTQTFDVIIS- 157
Cdd:COG2227   26 GRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAELNV--------DFVQGDLEDL-PLEDGSFDLVICs 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 654547830 158 ----DCTDPIgpgaslftsSFYEGCKRCLNPGGIFV 189
Cdd:COG2227   95 evleHLPDPA---------ALLRELARLLKPGGLLL 121
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 82-188 8.55e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.73  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   82 LIIGGGDGAMLREVSRHRSIETITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFNlVIDDGvnfvNQTTQTFDVIIS---- 157
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELF-QLDLG----ELDPGSFDVVVAsnvl 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 654547830  158 DCTDPIgpgaslftSSFYEGCKRCLNPGGIF 188
Cdd:pfam08242  76 HHLADP--------RAVLRNIRRLLKPGGVL 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 81-186 1.97e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.77  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830   81 VLIIGGGDGAMLREVSRHRSIEtITMVEIDAGVVSFCRQYLPNHNagsyddPRFNLVIDDGVNFvNQTTQTFDVIISDCT 160
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARERAAEAG------LNVEFVQGDAEDL-PFPDGSFDLVVSSGV 72

                          90       100
                  ....*....|....*....|....*.
gi 654547830  161 DPIGPGASLftSSFYEGCKRCLNPGG 186
Cdd:pfam13649  73 LHHLPDPDL--EAALREIARVLKPGG 96
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
96-187 5.07e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 37.97  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547830  96 SRHRSIETITMVEIDAGVVsfcrqYLPNHNAGSYD--DPRFNLVIDDGVNFVNQ-TTQTFDVIISDctdP--IGPGASLF 170
Cdd:COG2521  150 ALKRGAREVITVEKDPNVL-----ELAELNPWSRElaNERIKIILGDASEVIKTfPDESFDAIIHD---PprFSLAGELY 221

                         90
                 ....*....|....*..
gi 654547830 171 TSSFYEGCKRCLNPGGI 187
Cdd:COG2521  222 SLEFYRELYRVLKPGGR 238
 
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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