|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-273 |
6.86e-140 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 394.91 E-value: 6.86e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 1 MSIWFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 81 vvgggdgGVI---------REVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSL-DDERVEVKVDDGFMFIANSEKAFD 150
Cdd:PRK00811 80 -------VLIigggdggtlREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAyDDPRVELVIGDGIKFVAETENSFD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 151 VILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYPSGLWTF 230
Cdd:PRK00811 153 VIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 983529465 231 TIGSKIHD----PLKVKQERFHE--VDTKYYTPEIHFASFALPRFVKEL 273
Cdd:PRK00811 233 TFASKNDDlkflPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDA 281
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
1.12e-128 |
|
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: 365.98 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 4 WFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 84 GGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 164 VNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYPSGLWTFTIGSKI-HDPLKV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNkYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 983529465 243 KQER----FHEVDTKYYTPEIHFASFALPRF 269
Cdd:TIGR00417 241 EIRRikfeAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
2.33e-74 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 225.48 E-value: 2.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 42 GNMLLLDDMVMTT-EKDEFVYHEMVAHVPLFTHPSPKHvlvvgggdggvI-----------REVLRHPSVQKATLVDIDG 109
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKR-----------VliigggdgglaRELLKHPPVERVDVVEIDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 110 EVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQT 189
Cdd:COG0421 72 EVVELAREYFPLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 983529465 190 DNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYpSGLWTFTIG 233
Cdd:COG0421 152 GSPFYGLDLLRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-235 |
7.68e-72 |
|
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: 218.73 E-value: 7.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 58 EFVYHEMVAHVPLFTHPSPKHVLVVGGGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 138 GFMFIANSEKAFDVILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*...
gi 983529465 218 ANIPTYPSGLWTFTIGSK 235
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSK 178
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
101-188 |
4.39e-05 |
|
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: 41.65 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 101 KATLVDIDGEVIHYSKKylptIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDstePVGPAVNLFTQGFYAGIHKALK 180
Cdd:cd02440 23 RVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFLEEARRLLK 95
|
....*...
gi 983529465 181 DDGIFVAQ 188
Cdd:cd02440 96 PGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-273 |
6.86e-140 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 394.91 E-value: 6.86e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 1 MSIWFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 81 vvgggdgGVI---------REVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSL-DDERVEVKVDDGFMFIANSEKAFD 150
Cdd:PRK00811 80 -------VLIigggdggtlREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGAyDDPRVELVIGDGIKFVAETENSFD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 151 VILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYPSGLWTF 230
Cdd:PRK00811 153 VIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 983529465 231 TIGSKIHD----PLKVKQERFHE--VDTKYYTPEIHFASFALPRFVKEL 273
Cdd:PRK00811 233 TFASKNDDlkflPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDA 281
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
1.12e-128 |
|
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: 365.98 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 4 WFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 84 GGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 164 VNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYPSGLWTFTIGSKI-HDPLKV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKNkYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 983529465 243 KQER----FHEVDTKYYTPEIHFASFALPRF 269
Cdd:TIGR00417 241 EIRRikfeAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
2.33e-74 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 225.48 E-value: 2.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 42 GNMLLLDDMVMTT-EKDEFVYHEMVAHVPLFTHPSPKHvlvvgggdggvI-----------REVLRHPSVQKATLVDIDG 109
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKR-----------VliigggdgglaRELLKHPPVERVDVVEIDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 110 EVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQT 189
Cdd:COG0421 72 EVVELAREYFPLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 983529465 190 DNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYpSGLWTFTIG 233
Cdd:COG0421 152 GSPFYGLDLLRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-235 |
7.68e-72 |
|
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: 218.73 E-value: 7.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 58 EFVYHEMVAHVPLFTHPSPKHVLVVGGGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 138 GFMFIANSEKAFDVILVDSTEPVGPAVNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*...
gi 983529465 218 ANIPTYPSGLWTFTIGSK 235
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSK 178
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
1-271 |
5.80e-68 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 212.97 E-value: 5.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 1 MSIWFTEKQTANFG--ITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKH 78
Cdd:PLN02366 15 IPGWFSEISPMWPGeaHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 79 VLVVGGGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANS-EKAFDVILVDST 157
Cdd:PLN02366 95 VLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNApEGTYDAIIVDSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 158 EPVGPAVNLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLY-TANIPTYPSGLWTFTIGSK- 235
Cdd:PLN02366 175 DPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYaWTTVPTYPSGVIGFVLCSKe 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 983529465 236 ---------IHDPLKVKQERFHEVDTKYYTPEIHFASFALPRFVK 271
Cdd:PLN02366 255 gpavdfkhpVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAK 299
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
1-272 |
6.28e-51 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 169.86 E-value: 6.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 1 MSIWFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHVL 80
Cdd:PLN02823 29 KSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 81 VVGGGDGGVIREVLRHPSVQKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPV 160
Cdd:PLN02823 109 IMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 161 --GPAVNLFTQGFYAGIHKA-LKDDGIFVAQTDNPWFKADliHQVF----HDVKEIFPVTRLYTANIPTYPSgLWTFTIG 233
Cdd:PLN02823 189 egGPCYQLYTKSFYERIVKPkLNPGGIFVTQAGPAGILTH--KEVFssiyNTLRQVFKYVVPYTAHVPSFAD-TWGWVMA 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 983529465 234 S-KIHDPLKVKQ------ERFhEVDTKYYTPEIHFASFALPRFVKE 272
Cdd:PLN02823 266 SdHPFADLSAEEldsrikERI-DGELKYLDGETFSSAFALNKTVRQ 310
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
21-211 |
1.08e-32 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 123.82 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 21 KTLAALQTDYQDLKMVEtveWGN--MLLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHVLVVGGGDGGVIREVLRHPS 98
Cdd:COG4262 233 PVVYSEQTPYQRIVVTR---DKDdrRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 99 VQKATLVDIDGEVIHYSKK--YLPTI-AGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVN-LFTQGFYAG 174
Cdd:COG4262 310 VESVTLVDLDPEVTDLAKTnpFLRELnGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRL 389
|
170 180 190
....*....|....*....|....*....|....*..
gi 983529465 175 IHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFP 211
Cdd:COG4262 390 VRRHLAPGGVLVVQATSPYFAPKAFWCIAKTLEAAGF 426
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
21-268 |
4.10e-29 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 115.32 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 21 KTLAALQTDYQDLkmVETvEWGNM------LLLDDMVMTTEKDEFVYHEMVAHVPLFTHPSPKHVLVVGGGDGGVIREVL 94
Cdd:PRK03612 240 PVVYAEQTPYQRI--VVT-RRGNGrgpdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 95 RHPSVQKATLVDIDGEVIHYSKKYlPTI----AGSLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVN-LFTQ 169
Cdd:PRK03612 317 KYPDVEQVTLVDLDPAMTELARTS-PALralnGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSV 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 170 GFYAGIHKALKDDGIFVAQTDNPWFKADL---IHQVFHDVKeiFPVTRlYTANIPTYpsGLWTFTI-GSKIHDPLKVKQE 245
Cdd:PRK03612 396 EFYRLLKRRLAPDGLLVVQSTSPYFAPKAfwsIEATLEAAG--LATTP-YHVNVPSF--GEWGFVLaGAGARPPLAVPTE 470
|
250 260
....*....|....*....|...
gi 983529465 246 RfhEVDTKYYTPEIHFASFALPR 268
Cdd:PRK03612 471 L--PVPLRFLDPALLAAAFVFPK 491
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
15-240 |
8.87e-19 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 85.02 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 15 ITAKVNKTLAALQTDYQDLKMVETVEWgnMLLLDDMVMTTEKDEFVYHEMVAHvPLFTHP-SPKHVLVVGGGDGGVIREV 93
Cdd:PRK01581 92 IQAGEHTNLFAEKSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVH-PIMSKViDPKRVLILGGGDGLALREV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 94 LRHPSVQKATLVDIDGEVIHYSKKyLPTIAG----SLDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVN-LFT 168
Cdd:PRK01581 169 LKYETVLHVDLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYT 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983529465 169 QGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTANIPTYPSGlWTFTIGSKIHDPL 240
Cdd:PRK01581 248 SELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTD-WGFHIAANSAYVL 318
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
3-55 |
7.61e-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: 64.61 E-value: 7.61e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 983529465 3 IWFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTTE 55
Cdd:pfam17284 1 GWFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
3-272 |
4.31e-10 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 58.72 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 3 IWFTEKQTANFGITAKVNKTLAALQTDYQDLKMVETVEWGNMLLLDDMVMTtEKDEFVYHEMVAHVPLFTHPSPKHVLVV 82
Cdd:PRK00536 1 MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLF-KNFLHIESELLAHMGGCTKKELKEVLIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 83 GGGDGGVIREVLRHPSvqKATLVDIDGEVIHYSKKYLPTIAGSLDDERVEVKVDdgfmFIANSEKAFDVILVDStepvgp 162
Cdd:PRK00536 80 DGFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTHAKQ----LLDLDIKKYDLIICLQ------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 163 avnLFTQGFYAGIHKALKDDGIFVAQTDNPWFKADLIHQVFHDVKEIFPVTRLYTAniPTYPSGLWTFTIGSKIHDPLK- 241
Cdd:PRK00536 148 ---EPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVA--PLRILSNKGYIYASFKTHPLKd 222
|
250 260 270
....*....|....*....|....*....|..
gi 983529465 242 -VKQERFHEVDTKYYTPEIHFASFALPRFVKE 272
Cdd:PRK00536 223 lMLQKIEALKSVRYYNEDIHRAAFALPKNLQE 254
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
101-186 |
6.75e-09 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 55.43 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 101 KATLVDIDGEVIHYSKK--YLPTiagslDDERVEVKVDDGFMFIANSEKAFDVILVDSTEPVGPAVNLFTQGFYAGIHKA 178
Cdd:PRK04457 92 RQTAVEINPQVIAVARNhfELPE-----NGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNA 166
|
....*...
gi 983529465 179 LKDDGIFV 186
Cdd:PRK04457 167 LSSDGIFV 174
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
101-188 |
4.39e-05 |
|
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: 41.65 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983529465 101 KATLVDIDGEVIHYSKKylptIAGSLDDERVEVKVDDGFMFIANSEKAFDVILVDstePVGPAVNLFTQGFYAGIHKALK 180
Cdd:cd02440 23 RVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFLEEARRLLK 95
|
....*...
gi 983529465 181 DDGIFVAQ 188
Cdd:cd02440 96 PGGVLVLT 103
|
|
| |
