|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
8-298 |
6.28e-157 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 440.24 E-value: 6.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366 6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366 86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678131 246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
20-293 |
1.75e-133 |
|
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: 379.46 E-value: 1.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417 1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
|
250 260 270
....*....|....*....|....*....|....
gi 6678131 260 REPVQQLTQAQvEQMQLKYYNSDMHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
76-255 |
7.63e-102 |
|
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: 295.77 E-value: 7.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170 180
....*....|....*....|
gi 6678131 236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
60-251 |
6.90e-78 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 235.49 E-value: 6.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIK 218
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 6678131 219 EMRHFCKSLFPVVDYAYCSIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
96-206 |
5.80e-10 |
|
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: 55.51 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440 1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72
|
90 100 110
....*....|....*....|....*....|.
gi 6678131 176 DPMGPAESLFKESYYQLMKTALKEDGILCCQ 206
Cdd:cd02440 73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
8-298 |
6.28e-157 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 440.24 E-value: 6.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 8 PAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLP 87
Cdd:PLN02366 6 SEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 88 LCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMK-QNQDA 166
Cdd:PLN02366 86 LCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 167 FDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFP-VVDYAYCSIPTYPSGQ 245
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGV 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678131 246 IGFMLCSK-NPSTNFREPVQQLTQ---AQVEQMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02366 246 IGFVLCSKeGPAVDFKHPVNPIDKlegAGKAKRPLKFYNSEVHRAAFCLPSFAKREL 302
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
20-293 |
1.75e-133 |
|
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: 379.46 E-value: 1.75e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 20 WFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLI 99
Cdd:TIGR00417 1 WFTEYHD--KNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 100 IGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMG 179
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 180 PAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNF 259
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
|
250 260 270
....*....|....*....|....*....|....
gi 6678131 260 REPVQQLTQAQvEQMQLKYYNSDMHRAAFVLPEF 293
Cdd:TIGR00417 239 EVEIRRIKFEA-EDGKTKYYNPDIHKAAFVLPKW 271
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
18-299 |
3.67e-126 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 361.01 E-value: 3.67e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 18 EGWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK00811 3 ELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSD 176
Cdd:PRK00811 81 LIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 177 PMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPS 256
Cdd:PRK00811 161 PVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKNDD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6678131 257 TNFRePVQQLTQAQVE-QMQLKYYNSDMHRAAFVLPEFTRKALN 299
Cdd:PRK00811 241 LKFL-PLDVIEARFAErGIKTRYYNPELHKAAFALPQFVKDALK 283
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
76-255 |
7.63e-102 |
|
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: 295.77 E-value: 7.63e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 76 EFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGD 155
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 156 GFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAY 235
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170 180
....*....|....*....|
gi 6678131 236 CSIPTYPSGQIGFMLCSKNP 255
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
60-251 |
6.90e-78 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 235.49 E-value: 6.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 60 GNVLVLDGVIQCT-ERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLP 138
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 139 GMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIK 218
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 6678131 219 EMRHFCKSLFPVVDYAYCSIPTYpSGQIGFMLC 251
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
4-298 |
1.21e-62 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 201.45 E-value: 1.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 4 GPDGPAAPGPAAIREG-WFRETcsLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEM 82
Cdd:PLN02823 15 AVATPTAALASNYAKSlWYEEE--IEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 83 IANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQ 162
Cdd:PLN02823 93 LVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 163 NQDAFDVIITDSSDPM--GPAESLFKESYYQLM-KTALKEDGILCCQGECQWL--HLDLIKEMRHFCKSLFP-VVDYAYC 236
Cdd:PLN02823 173 RDEKFDVIIGDLADPVegGPCYQLYTKSFYERIvKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKyVVPYTAH 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678131 237 sIPTYPSgQIGFMLCSKNPSTNF-REPVQQLTQAQVEqMQLKYYNSDMHRAAFVLPEFTRKAL 298
Cdd:PLN02823 253 -VPSFAD-TWGWVMASDHPFADLsAEELDSRIKERID-GELKYLDGETFSSAFALNKTVRQAL 312
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
27-203 |
2.51e-45 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 158.49 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSKTYGNvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLII 100
Cdd:COG4262 215 LVFADPIESSAEQKLygdpvvYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 101 GGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKK--FLPGMAVG-FSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDP 177
Cdd:COG4262 294 GGGDGLAAREVLKYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDP 373
|
170 180
....*....|....*....|....*....
gi 6678131 178 mgPAESLFK---ESYYQLMKTALKEDGIL 203
Cdd:COG4262 374 --SNFSLGKlysVEFYRLVRRHLAPGGVL 400
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
27-206 |
3.84e-34 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 129.96 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 27 LWPGQALSLQVEQLL------HHRRSRYQDILVFRSK-TYGNV--LVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKV 97
Cdd:PRK03612 222 FVLADRIETTAEQLLygdpvvYAEQTPYQRIVVTRRGnGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 98 LIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKF-----LPGMAvgFSSSKLTLHVGDGFEFMKQNQDAFDVIIT 172
Cdd:PRK03612 302 LVLGGGDGLALREVLKYPDVEQVTLVDLDPAMTELARTSpalraLNGGA--LDDPRVTVVNDDAFNWLRKLAEKFDVIIV 379
|
170 180 190
....*....|....*....|....*....|....*
gi 6678131 173 DSSDPMGPAES-LFKESYYQLMKTALKEDGILCCQ 206
Cdd:PRK03612 380 DLPDPSNPALGkLYSVEFYRLLKRRLAPDGLLVVQ 414
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
41-206 |
4.14e-24 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 100.42 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 41 LHHRRSRYQDILVFRSKTYGnvLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESV 120
Cdd:PRK01581 100 LFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 121 VQCEIDEDVIEVSKKfLPGMAV----GFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAES-LFKESYYQLMKT 195
Cdd:PRK01581 178 DLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARIAT 256
|
170
....*....|.
gi 6678131 196 ALKEDGILCCQ 206
Cdd:PRK01581 257 FLTEDGAFVCQ 267
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
19-73 |
1.06e-22 |
|
Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.
Pssm-ID: 407397 [Multi-domain] Cd Length: 53 Bit Score: 88.49 E-value: 1.06e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6678131 19 GWFRETCSlwPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTE 73
Cdd:pfam17284 1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
37-301 |
4.41e-18 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 81.83 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 37 VEQLLHHRRSRYQDILVFRSKTYGNVLVLDGviQCTERDEFSYQ-EMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHP 115
Cdd:PRK00536 17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 116 SVESVVQCeiDEDVIEVSKKFLPGMAVGFSSSKLTLHVgdgfEFMKQNQDAFDVIITDSSDPMGPAESLFKesyyqlmkt 195
Cdd:PRK00536 95 THVDFVQA--DEKILDSFISFFPHFHEVKNNKNFTHAK----QLLDLDIKKYDLIICLQEPDIHKIDGLKR--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 196 ALKEDGILCCQGECQWLH----LDLIKEMRHFCKSLFPVVdyAYCSIptypSGQIGFMLCSKNpstnfREPVQQLTQAQV 271
Cdd:PRK00536 160 MLKEDGVFISVAKHPLLEhvsmQNALKNMGDFFSIAMPFV--APLRI----LSNKGYIYASFK-----THPLKDLMLQKI 228
|
250 260 270
....*....|....*....|....*....|.
gi 6678131 272 EQMQ-LKYYNSDMHRAAFVLPEFTRKALNDI 301
Cdd:PRK00536 229 EALKsVRYYNEDIHRAAFALPKNLQEVFKDN 259
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
91-203 |
1.53e-13 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 68.91 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 91 HPNPRKVLIIGGGDGGVLREVVKH-PSVESVVqCEIDEDVIEVSKK--FLPgmavgFSSSKLTLHVGDGFEFMKQNQDAF 167
Cdd:PRK04457 64 NPRPQHILQIGLGGGSLAKFIYTYlPDTRQTA-VEINPQVIAVARNhfELP-----ENGERFEVIEADGAEYIAVHRHST 137
|
90 100 110
....*....|....*....|....*....|....*.
gi 6678131 168 DVIITDSSDPMGPAESLFKESYYQLMKTALKEDGIL 203
Cdd:PRK04457 138 DVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIF 173
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
96-206 |
5.80e-10 |
|
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: 55.51 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 96 KVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFlpgmAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIItdsS 175
Cdd:cd02440 1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARKA----AAALLADNVEVLKGDAEELPPEADESFDVII---S 72
|
90 100 110
....*....|....*....|....*....|.
gi 6678131 176 DPMGPAESLFKESYYQLMKTALKEDGILCCQ 206
Cdd:cd02440 73 DPPLHHLVEDLARFLEEARRLLKPGGVLVLT 103
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
74-207 |
5.64e-05 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 43.37 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 74 RDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPsVESVVQCEIDEDVIEVSKKFLPGMAVGfsssKLTLHV 153
Cdd:COG0500 7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLG----NVEFLV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6678131 154 GDGFEFMKQNQDAFDVII-TDSSDPMGPAESlfkESYYQLMKTALKEDGILCCQG 207
Cdd:COG0500 82 ADLAELDPLPAESFDLVVaFGVLHHLPPEER---EALLRELARALKPGGVLLLSA 133
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
92-203 |
7.63e-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: 38.85 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678131 92 PNPRKVLIIGGGDGGVLREVVKHpsVESVVQCEIDEDVIEVSKKFLPGMAVgfsssklTLHVGDgFEFMKQNQDAFDVII 171
Cdd:COG2227 23 PAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNV-------DFVQGD-LEDLPLEDGSFDLVI 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 6678131 172 TDSS-----DPmgpaESLFKEsyyqlMKTALKEDGIL 203
Cdd:COG2227 93 CSEVlehlpDP----AALLRE-----LARLLKPGGLL 120
|
|
|