|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
7-293 |
2.13e-156 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 438.70 E-value: 2.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 7 SHPLIKDGWFREINNMWPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSH 86
Cdd:PLN02366 10 CHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 87 PNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQD-YQNTFDVI 165
Cdd:PLN02366 90 PNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 166 ITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFP-NVRYAYTTIPTYPSGSIGFV 244
Cdd:PLN02366 170 IVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGVIGFV 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19112807 245 VASKD-ASIDLSKPLRKWSPEEENKLC----KYYNSEIHAASFVLPTFARDVVD 293
Cdd:PLN02366 250 LCSKEgPAVDFKHPVNPIDKLEGAGKAkrplKFYNSEVHRAAFCLPSFAKRELE 303
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
15-287 |
9.61e-147 |
|
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: 412.59 E-value: 9.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 15 WFREINNMwpGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLV 94
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 95 IGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDG 174
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 175 PAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAYTTIPTYPSGSIGFVVASKDASIDL 254
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
|
250 260 270
....*....|....*....|....*....|...
gi 19112807 255 SKPLRKWSPEEENKLCKYYNSEIHAASFVLPTF 287
Cdd:TIGR00417 239 EVEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
71-250 |
8.12e-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: 295.38 E-value: 8.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 71 EFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGD 150
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 151 GFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAY 230
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170 180
....*....|....*....|
gi 19112807 231 TTIPTYPSGSIGFVVASKDA 250
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
55-246 |
5.34e-82 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 245.51 E-value: 5.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 55 GHVLVLDGAIQAT-ERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLP 133
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 134 EMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVIS 213
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 19112807 214 NVLTAVKTVFPNVRYAYTTIPTYpSGSIGFVVA 246
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
91-198 |
1.09e-12 |
|
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: 63.22 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 91 KVLVIGGGDGGVLREVVKHECvEEAILCDIDEDVIKVSKQYLpemsAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSS 170
Cdd:cd02440 1 RVLDLGCGTGALALALASGPG-ARVTGVDISPVALELARKAA----AALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
|
90 100
....*....|....*....|....*...
gi 19112807 171 dpdGPAEALFQKPYFQLLSDALRGGGVI 198
Cdd:cd02440 76 ---LHHLVEDLARFLEEARRLLKPGGVL 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
7-293 |
2.13e-156 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 438.70 E-value: 2.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 7 SHPLIKDGWFREINNMWPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSH 86
Cdd:PLN02366 10 CHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 87 PNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQD-YQNTFDVI 165
Cdd:PLN02366 90 PNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNaPEGTYDAI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 166 ITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFP-NVRYAYTTIPTYPSGSIGFV 244
Cdd:PLN02366 170 IVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKgSVNYAWTTVPTYPSGVIGFV 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19112807 245 VASKD-ASIDLSKPLRKWSPEEENKLC----KYYNSEIHAASFVLPTFARDVVD 293
Cdd:PLN02366 250 LCSKEgPAVDFKHPVNPIDKLEGAGKAkrplKFYNSEVHRAAFCLPSFAKRELE 303
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
15-287 |
9.61e-147 |
|
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: 412.59 E-value: 9.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 15 WFREINNMwpGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLV 94
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 95 IGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDG 174
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 175 PAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAYTTIPTYPSGSIGFVVASKDASIDL 254
Cdd:TIGR00417 159 PAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNKYRPL 238
|
250 260 270
....*....|....*....|....*....|...
gi 19112807 255 SKPLRKWSPEEENKLCKYYNSEIHAASFVLPTF 287
Cdd:TIGR00417 239 EVEIRRIKFEAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
12-290 |
6.66e-123 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 352.92 E-value: 6.66e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 12 KDGWFREINNmwPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKK 91
Cdd:PRK00811 2 MELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 92 VLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAG-FNHPKVKVHIGDGFKFLQDYQNTFDVIITDSS 170
Cdd:PRK00811 80 VLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 171 DPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAYTTIPTYPSGSIGFVVASKDA 250
Cdd:PRK00811 160 DPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKND 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19112807 251 SID-LSKPLRKWSPEEENKLCKYYNSEIHAASFVLPTFARD 290
Cdd:PRK00811 240 DLKfLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKD 280
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
71-250 |
8.12e-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: 295.38 E-value: 8.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 71 EFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGD 150
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 151 GFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAY 230
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170 180
....*....|....*....|
gi 19112807 231 TTIPTYPSGSIGFVVASKDA 250
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
55-246 |
5.34e-82 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 245.51 E-value: 5.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 55 GHVLVLDGAIQAT-ERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLP 133
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 134 EMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVIS 213
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 19112807 214 NVLTAVKTVFPNVRYAYTTIPTYpSGSIGFVVA 246
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
12-296 |
1.51e-66 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 211.08 E-value: 1.51e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 12 KDGWFREinNMWPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKK 91
Cdd:PLN02823 29 KSLWYEE--EIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 92 VLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSD 171
Cdd:PLN02823 107 VFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 172 P--DGPAEALFQKPYFQ-LLSDALRGGGVITTQAECMWI--HLGVISNVLTAVKTVFPNVrYAYTT-IPTYPSgSIGFVV 245
Cdd:PLN02823 187 PveGGPCYQLYTKSFYErIVKPKLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKYV-VPYTAhVPSFAD-TWGWVM 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112807 246 ASKDASIDLskplrkwSPEEENKLCK--------YYNSEIHAASFVLPTFARDVVDKAT 296
Cdd:PLN02823 265 ASDHPFADL-------SAEELDSRIKeridgelkYLDGETFSSAFALNKTVRQALANET 316
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
34-202 |
7.25e-50 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 170.43 E-value: 7.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 34 KVLYAGKSKYQDVLVFESETYgHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVE 113
Cdd:COG4262 233 PVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 114 EAILCDIDEDVIKVSKQ--YLPEMSAG-FNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEA-LFQKPYFQLLS 189
Cdd:COG4262 312 SVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLVR 391
|
170
....*....|...
gi 19112807 190 DALRGGGVITTQA 202
Cdd:COG4262 392 RHLAPGGVLVVQA 404
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
34-285 |
1.07e-39 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 144.98 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 34 KVLYAGKSKYQDVLVFESETY---GHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHE 110
Cdd:PRK03612 240 PVVYAEQTPYQRIVVTRRGNGrgpDLRLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 111 CVEEAILCDIDEDVIKVSKQYlPEMSA----GFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEA-LFQKPYF 185
Cdd:PRK03612 320 DVEQVTLVDLDPAMTELARTS-PALRAlnggALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFY 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 186 QLLSDALRGGGVITTQA-------ECMWIhlgvISNVLTAVKtvFPNVRYaYTTIPTYpsGSIGFVVASKDASIDLSKPL 258
Cdd:PRK03612 399 RLLKRRLAPDGLLVVQStspyfapKAFWS----IEATLEAAG--LATTPY-HVNVPSF--GEWGFVLAGAGARPPLAVPT 469
|
250 260
....*....|....*....|....*..
gi 19112807 259 RkwSPEEEnklcKYYNSEIHAASFVLP 285
Cdd:PRK03612 470 E--LPVPL----RFLDPALLAAAFVFP 490
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
35-202 |
1.90e-23 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 98.50 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 35 VLYAGKSKYQDV-LVFESETYghvLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVE 113
Cdd:PRK01581 99 NLFAEKSNYQNInLLQVSDIR---LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 114 EAILCDIDEDVIKVSKQyLPEMSA----GFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPA-EALFQKPYFQLL 188
Cdd:PRK01581 176 HVDLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFARI 254
|
170
....*....|....
gi 19112807 189 SDALRGGGVITTQA 202
Cdd:PRK01581 255 ATFLTEDGAFVCQS 268
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
14-68 |
9.93e-23 |
|
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: 9.93e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 19112807 14 GWFREINNmwPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATE 68
Cdd:pfam17284 1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
91-198 |
1.09e-12 |
|
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: 63.22 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 91 KVLVIGGGDGGVLREVVKHECvEEAILCDIDEDVIKVSKQYLpemsAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSS 170
Cdd:cd02440 1 RVLDLGCGTGALALALASGPG-ARVTGVDISPVALELARKAA----AALLADNVEVLKGDAEELPPEADESFDVIISDPP 75
|
90 100
....*....|....*....|....*...
gi 19112807 171 dpdGPAEALFQKPYFQLLSDALRGGGVI 198
Cdd:cd02440 76 ---LHHLVEDLARFLEEARRLLKPGGVL 100
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
71-200 |
3.33e-10 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 59.28 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 71 EFSY-QEMIAHLALNshPNPKKVLVIGGGDGGVLREVVKH--ECVEEAIlcDIDEDVIKVSKQ--YLPEmsagfNHPKVK 145
Cdd:PRK04457 50 ELAYtRAMMGFLLFN--PRPQHILQIGLGGGSLAKFIYTYlpDTRQTAV--EINPQVIAVARNhfELPE-----NGERFE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19112807 146 VHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITT 200
Cdd:PRK04457 121 VIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVV 175
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
22-292 |
6.87e-10 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 58.33 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 22 MWPGQAMTLKVK-------KVLYAgKSKYQDVLVFESETYGHVLVLDGAIqATERDEFSYQEMIAHLALNSHPNPKKVLV 94
Cdd:PRK00536 1 MWITQEITPYLRkeytieaKLLDV-RSEHNILEIFKSKDFGEIAMLNKQL-LFKNFLHIESELLAHMGGCTKKELKEVLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 95 IGGGDGGVLREVVKHE----CVEEailcdiDEDVIKVSKQYLPEMSAGFNHPKVKVhigdgFKFLQDYQ-NTFDVIITDS 169
Cdd:PRK00536 79 VDGFDLELAHQLFKYDthvdFVQA------DEKILDSFISFFPHFHEVKNNKNFTH-----AKQLLDLDiKKYDLIICLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 170 sdpdgpaeaLFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVryayttIPTYPSGSI----GFVV 245
Cdd:PRK00536 148 ---------EPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIA------MPFVAPLRIlsnkGYIY 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19112807 246 ASKDasidlSKPLRKWSPEEENKL--CKYYNSEIHAASFVLPTFARDVV 292
Cdd:PRK00536 213 ASFK-----THPLKDLMLQKIEALksVRYYNEDIHRAAFALPKNLQEVF 256
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
88-231 |
5.33e-06 |
|
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: 45.95 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 88 NPKKVLVIGGG-------------DGGVLrevvkhecveeaILCDIDEDVIKVSKQYLPEmsAGFNHpKVKVHIGDGFKF 154
Cdd:COG4122 16 GAKRILEIGTGtgystlwlaralpDDGRL------------TTIEIDPERAAIARENFAR--AGLAD-RIRLILGDALEV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112807 155 LQDY-QNTFDVIITDSsDPDGpaealfQKPYFQLLSDALRGGGVIttqaecmwihlgVISNVLTAVKTVFPNVRYAYT 231
Cdd:COG4122 81 LPRLaDGPFDLVFIDA-DKSN------YPDYLELALPLLRPGGLI------------VADNVLWHGRVADPARRDPST 139
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
74-198 |
3.59e-05 |
|
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: 42.70 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 74 YQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECveEAILCDIDEDVIKVSKQYLPEMsagfnhpKVKVHIGDGFK 153
Cdd:COG2227 10 WDRRLAALLARLLPAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAEL-------NVDFVQGDLED 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 19112807 154 fLQDYQNTFDVIItdSSD-----PDgPAEALfqkpyfQLLSDALRGGGVI 198
Cdd:COG2227 81 -LPLEDGSFDLVI--CSEvlehlPD-PAALL------RELARLLKPGGLL 120
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
74-166 |
4.27e-05 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 42.67 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 74 YQEMIAHLALnshPNPKKVLVIGGGDGGVLREVVKHECveEAILCDIDEDVIKVSKQYLPEmsAGFNhpkVKVHIGDGFK 153
Cdd:COG2226 11 REALLAALGL---RPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAE--AGLN---VEFVVGDAED 80
|
90
....*....|....
gi 19112807 154 F-LQDyqNTFDVII 166
Cdd:COG2226 81 LpFPD--GSFDLVI 92
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
93-166 |
9.87e-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: 9.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112807 93 LVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPkVKVHIGDGFKFLqdyQNTFDVII 166
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVR-VELFQLDLGELD---PGSFDVVV 70
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
69-198 |
2.51e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.36 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112807 69 RDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECvEEAILCDIDEDVIKVSKqylpEMSAGFNHPKVKVHI 148
Cdd:COG0500 7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALAR----ARAAKAGLGNVEFLV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 19112807 149 GDGFKFLQDYQNTFDVIITDSS----DPDGpaealfQKPYFQLLSDALRGGGVI 198
Cdd:COG0500 82 ADLAELDPLPAESFDLVVAFGVlhhlPPEE------REALLRELARALKPGGVL 129
|
|
| |
