|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-275 |
2.25e-154 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 431.50 E-value: 2.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 1 MELWFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 81 vvgggdgGVI---------REVLKHPSVKKATLVEIDGKVIEYSKQYLPSIA-GALDDERVEVKVGDGFLHIAESENEYD 150
Cdd:PRK00811 80 -------VLIigggdggtlREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAgGAYDDPRVELVIGDGIKFVAETENSFD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 151 VIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYPSGLWTF 230
Cdd:PRK00811 153 VIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446346838 231 TIGSK----KHDPLEVSEERFHE--IETKYYTKELHNAAFALPKFVGDLIK 275
Cdd:PRK00811 233 TFASKnddlKFLPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDALK 283
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
2.53e-139 |
|
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: 392.95 E-value: 2.53e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 4 WFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 84 GGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 164 VNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYPSGLWTFTIGSK-KHDPLEV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKnKYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 446346838 243 SEER----FHEIETKYYTKELHNAAFALPKF 269
Cdd:TIGR00417 241 EIRRikfeAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
2.32e-78 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 235.49 E-value: 2.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 42 GNMLILDGMVMTT-EKDEFVYHEMVAHVPLFTHPNPENvlvvgggdggvI-----------REVLKHPSVKKATLVEIDG 109
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKR-----------VliigggdgglaRELLKHPPVERVDVVEIDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 110 KVIEYSKQYLPSIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQT 189
Cdd:COG0421 72 EVVELAREYFPLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446346838 190 DNPWFTPELITTVFKDVKEIFPITRLYTANIPTYpSGLWTFTIG 233
Cdd:COG0421 152 GSPFYGLDLLRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-236 |
6.25e-78 |
|
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: 234.14 E-value: 6.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 58 EFVYHEMVAHVPLFTHPNPENVLVVGGGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 138 GFLHIAESENEYDVIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*....
gi 446346838 218 ANIPTYPSGLWTFTIGSKK 236
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
100-188 |
1.25e-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: 43.19 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 100 KKATLVEIDGKVIEYSKQylpsIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDstePVGPAVNLFTKGFYAGISKAL 179
Cdd:cd02440 22 ARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFLEEARRLL 94
|
....*....
gi 446346838 180 KEDGIFVAQ 188
Cdd:cd02440 95 KPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-275 |
2.25e-154 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 431.50 E-value: 2.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 1 MELWFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 81 vvgggdgGVI---------REVLKHPSVKKATLVEIDGKVIEYSKQYLPSIA-GALDDERVEVKVGDGFLHIAESENEYD 150
Cdd:PRK00811 80 -------VLIigggdggtlREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAgGAYDDPRVELVIGDGIKFVAETENSFD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 151 VIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYPSGLWTF 230
Cdd:PRK00811 153 VIIVDSTDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSF 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446346838 231 TIGSK----KHDPLEVSEERFHE--IETKYYTKELHNAAFALPKFVGDLIK 275
Cdd:PRK00811 233 TFASKnddlKFLPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDALK 283
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
2.53e-139 |
|
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: 392.95 E-value: 2.53e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 4 WFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 84 GGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 164 VNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYPSGLWTFTIGSK-KHDPLEV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKnKYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 446346838 243 SEER----FHEIETKYYTKELHNAAFALPKF 269
Cdd:TIGR00417 241 EIRRikfeAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
2.32e-78 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 235.49 E-value: 2.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 42 GNMLILDGMVMTT-EKDEFVYHEMVAHVPLFTHPNPENvlvvgggdggvI-----------REVLKHPSVKKATLVEIDG 109
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKR-----------VliigggdgglaRELLKHPPVERVDVVEIDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 110 KVIEYSKQYLPSIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQT 189
Cdd:COG0421 72 EVVELAREYFPLLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446346838 190 DNPWFTPELITTVFKDVKEIFPITRLYTANIPTYpSGLWTFTIG 233
Cdd:COG0421 152 GSPFYGLDLLRRVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-236 |
6.25e-78 |
|
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: 234.14 E-value: 6.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 58 EFVYHEMVAHVPLFTHPNPENVLVVGGGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 138 GFLHIAESENEYDVIMVDSTEPVGPAVNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*....
gi 446346838 218 ANIPTYPSGLWTFTIGSKK 236
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
4-270 |
7.38e-67 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 210.27 E-value: 7.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 4 WFTEKQTKHFG--ITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLV 81
Cdd:PLN02366 18 WFSEISPMWPGeaHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 82 VGGGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGDG--FLHIAEsENEYDVIMVDSTEP 159
Cdd:PLN02366 98 VGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGveFLKNAP-EGTYDAIIVDSSDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 160 VGPAVNLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLY-TANIPTYPSGLWTFTIGSK--- 235
Cdd:PLN02366 177 VGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYaWTTVPTYPSGVIGFVLCSKegp 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446346838 236 ----KH--DPLEVSE-ERFHEIETKYYTKELHNAAFALPKFV 270
Cdd:PLN02366 257 avdfKHpvNPIDKLEgAGKAKRPLKFYNSEVHRAAFCLPSFA 298
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
3-270 |
3.52e-56 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 183.73 E-value: 3.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 3 LWFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLVV 82
Cdd:PLN02823 31 LWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 83 GGGDGGVIREVLKHPSVKKATLVEIDGKVIEYSKQYLPSIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPV-- 160
Cdd:PLN02823 111 GGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVeg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 161 GPAVNLFTKGFYAGISKA-LKEDGIFVAQTDNPWF--TPELITTVFKDVKEIFPITRLYTANIPTYPSgLWTFTIGS-KK 236
Cdd:PLN02823 191 GPCYQLYTKSFYERIVKPkLNPGGIFVTQAGPAGIltHKEVFSSIYNTLRQVFKYVVPYTAHVPSFAD-TWGWVMASdHP 269
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446346838 237 HDPLEVSE------ERFhEIETKYYTKELHNAAFALPKFV 270
Cdd:PLN02823 270 FADLSAEEldsrikERI-DGELKYLDGETFSSAFALNKTV 308
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
21-211 |
7.08e-39 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 140.39 E-value: 7.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 21 RTLHTEQTEFQKLDMVETEEFGNmLILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLVVGGGDGGVIREVLKHPSVK 100
Cdd:COG4262 233 PVVYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 101 KATLVEIDGKVIEYSKQ--YLPSI-AGALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVN-LFTKGFYAGIS 176
Cdd:COG4262 312 SVTLVDLDPEVTDLAKTnpFLRELnGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLVR 391
|
170 180 190
....*....|....*....|....*....|....*
gi 446346838 177 KALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFP 211
Cdd:COG4262 392 RHLAPGGVLVVQATSPYFAPKAFWCIAKTLEAAGF 426
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
21-268 |
1.78e-36 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 135.74 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 21 RTLHTEQTEFQKLdmVETEEFGNM-----LILDGMVMTTEKDEFVYHEMVAHVPLFTHPNPENVLVVGGGDGGVIREVLK 95
Cdd:PRK03612 240 PVVYAEQTPYQRI--VVTRRGNGRgpdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 96 HPSVKKATLVEIDGKVIEYSKQYLPSIA---GALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVN-LFTKGF 171
Cdd:PRK03612 318 YPDVEQVTLVDLDPAMTELARTSPALRAlngGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEF 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 172 YAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYpsGLWTFTI-GSKKHDPLEVSEERfhEI 250
Cdd:PRK03612 398 YRLLKRRLAPDGLLVVQSTSPYFAPKAFWSIEATLEAAGLATTPYHVNVPSF--GEWGFVLaGAGARPPLAVPTEL--PV 473
|
250
....*....|....*...
gi 446346838 251 ETKYYTKELHNAAFALPK 268
Cdd:PRK03612 474 PLRFLDPALLAAAFVFPK 491
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
22-245 |
3.18e-21 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 91.95 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 22 TLHTEQTEFQKLDMVETEEFgnMLILDGMVMTTEKDEFVYHEMVAHvPLFTHP-NPENVLVVGGGDGGVIREVLKHPSVK 100
Cdd:PRK01581 99 NLFAEKSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVH-PIMSKViDPKRVLILGGGDGLALREVLKYETVL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 101 KATLVEIDGKVIEYSKQyLPSIAG----ALDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVN-LFTKGFYAGI 175
Cdd:PRK01581 176 HVDLVDLDGSMINMARN-VPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELLStLYTSELFARI 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 176 SKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTANIPTYPSGlWTFTIGSKKHDPLEVSEE 245
Cdd:PRK01581 255 ATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTD-WGFHIAANSAYVLDQIEQ 323
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
3-55 |
1.22e-16 |
|
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: 71.93 E-value: 1.22e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446346838 3 LWFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTTE 55
Cdd:pfam17284 1 GWFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
3-275 |
1.22e-14 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 71.81 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 3 LWFTEKQTKHFGITARINRTLHTEQTEFQKLDMVETEEFGNMLILDGMVMTtEKDEFVYHEMVAHVPLFTHPNPENVLVV 82
Cdd:PRK00536 1 MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLF-KNFLHIESELLAHMGGCTKKELKEVLIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 83 GGGDGGVIREVLKHPSvkKATLVEIDGKVIEYSKQYLPSIAGALDDERvevkvgdgFLHIAESEN----EYDVIMVDSte 158
Cdd:PRK00536 80 DGFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKN--------FTHAKQLLDldikKYDLIICLQ-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 159 pvgpavnLFTKGFYAGISKALKEDGIFVAQTDNPWFTPELITTVFKDVKEIFPITRLYTAniPTYPSGLWTFTIGSKKHD 238
Cdd:PRK00536 148 -------EPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVA--PLRILSNKGYIYASFKTH 218
|
250 260 270
....*....|....*....|....*....|....*....
gi 446346838 239 PL-EVSEERFHEIET-KYYTKELHNAAFALPKFVGDLIK 275
Cdd:PRK00536 219 PLkDLMLQKIEALKSvRYYNEDIHRAAFALPKNLQEVFK 257
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
101-186 |
1.90e-10 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 59.67 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 101 KATLVEIDGKVIEYSKQ--YLPSiagalDDERVEVKVGDGFLHIAESENEYDVIMVDSTEPVGPAVNLFTKGFYAGISKA 178
Cdd:PRK04457 92 RQTAVEINPQVIAVARNhfELPE-----NGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPFFDDCRNA 166
|
....*...
gi 446346838 179 LKEDGIFV 186
Cdd:PRK04457 167 LSSDGIFV 174
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
100-188 |
1.25e-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: 43.19 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446346838 100 KKATLVEIDGKVIEYSKQylpsIAGALDDERVEVKVGDGFLHIAESENEYDVIMVDstePVGPAVNLFTKGFYAGISKAL 179
Cdd:cd02440 22 ARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFLEEARRLL 94
|
....*....
gi 446346838 180 KEDGIFVAQ 188
Cdd:cd02440 95 KPGGVLVLT 103
|
|
| |
