|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-273 |
3.30e-145 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 408.39 E-value: 3.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 1 MTLWFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRvl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 81 vvgggdggTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSE-YGNPRVELIIGDGFEHIIKSENRYDVILVDSTEP 159
Cdd:PRK00811 82 iigggdggTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 160 VGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYTCNIPTYPSGMWTFTMGSK---- 235
Cdd:PRK00811 162 VGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKnddl 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2023325848 236 KHDPLNVEDGHFFE--IDTKYYTKELHSASFVLPKFVQEL 273
Cdd:PRK00811 242 KFLPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDA 281
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
9.47e-127 |
|
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: 361.36 E-value: 9.47e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 4 WFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 84 GGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 164 AGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYTCNIPTYPSGMWTFTMGSK-KHDPLNV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKnKYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 2023325848 243 ED----GHFFEIDTKYYTKELHSASFVLPKF 269
Cdd:TIGR00417 241 EIrrikFEAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
5.43e-80 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 239.73 E-value: 5.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 42 GNMLLLDGMVMTS-EKDEFVYHEMIAHVPLFTHPSPKHvlvvgggdggTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLP 120
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRvliigggdggLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 121 HISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIK 200
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 2023325848 201 NAIHDTKEIFPIARLYTCNIPTYpSGMWTFTMG 233
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-236 |
1.67e-74 |
|
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: 225.28 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 58 EFVYHEMIAHVPLFTHPSPKHVLVVGGGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 138 GFEHIIKSENRYDVILVDSTEPVGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*....
gi 2023325848 218 CNIPTYPSGMWTFTMGSKK 236
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
93-188 |
3.51e-07 |
|
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: 47.81 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 93 VLKHTSVEKVTQVEIDGKVVEYSKKhlphISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDstePVGPAAGLFTKGFY 172
Cdd:cd02440 15 ALASGPGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFL 87
|
90
....*....|....*.
gi 2023325848 173 AGIAKALKEDGIFVAQ 188
Cdd:cd02440 88 EEARRLLKPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
1-273 |
3.30e-145 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 408.39 E-value: 3.30e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 1 MTLWFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHvl 80
Cdd:PRK00811 2 MELWFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRvl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 81 vvgggdggTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSE-YGNPRVELIIGDGFEHIIKSENRYDVILVDSTEP 159
Cdd:PRK00811 82 iigggdggTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 160 VGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYTCNIPTYPSGMWTFTMGSK---- 235
Cdd:PRK00811 162 VGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVRPYQAAIPTYPSGLWSFTFASKnddl 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2023325848 236 KHDPLNVEDGHFFE--IDTKYYTKELHSASFVLPKFVQEL 273
Cdd:PRK00811 242 KFLPLDVIEARFAErgIKTRYYNPELHKAAFALPQFVKDA 281
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
4-269 |
9.47e-127 |
|
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: 361.36 E-value: 9.47e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 4 WFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHVLVVG 83
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 84 GGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPA 163
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 164 AGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYTCNIPTYPSGMWTFTMGSK-KHDPLNV 242
Cdd:TIGR00417 161 ETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGLWTFTIASKnKYRPLEV 240
|
250 260 270
....*....|....*....|....*....|.
gi 2023325848 243 ED----GHFFEIDTKYYTKELHSASFVLPKF 269
Cdd:TIGR00417 241 EIrrikFEAEDGKTKYYNPDIHKAAFVLPKW 271
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
42-233 |
5.43e-80 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 239.73 E-value: 5.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 42 GNMLLLDGMVMTS-EKDEFVYHEMIAHVPLFTHPSPKHvlvvgggdggTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLP 120
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRvliigggdggLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 121 HISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIK 200
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
|
170 180 190
....*....|....*....|....*....|...
gi 2023325848 201 NAIHDTKEIFPIARLYTCNIPTYpSGMWTFTMG 233
Cdd:COG0421 163 RVLATLREVFPHVVLYAAPVPTY-GGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
58-236 |
1.67e-74 |
|
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: 225.28 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 58 EFVYHEMIAHVPLFTHPSPKHVLVVGGGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGD 137
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 138 GFEHIIKSENRYDVILVDSTEPVGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYT 217
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFPVVMPYV 160
|
170
....*....|....*....
gi 2023325848 218 CNIPTYPSGMWTFTMGSKK 236
Cdd:pfam01564 161 ATIPTYPSGGWGFTVCSKN 179
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
4-271 |
3.31e-73 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 226.45 E-value: 3.31e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 4 WFTEK------QTSSFgitgKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPK 77
Cdd:PLN02366 18 WFSEIspmwpgEAHSL----KVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 78 HVLVVGGGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGDGFEHIIKS-ENRYDVILVDS 156
Cdd:PLN02366 94 KVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNApEGTYDAIIVDS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 157 TEPVGPAAGLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLY-TCNIPTYPSGMWTFTMGSK 235
Cdd:PLN02366 174 SDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYaWTTVPTYPSGVIGFVLCSK 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2023325848 236 KHDPLN----------VEDGHFFEIDTKYYTKELHSASFVLPKFVQ 271
Cdd:PLN02366 254 EGPAVDfkhpvnpidkLEGAGKAKRPLKFYNSEVHRAAFCLPSFAK 299
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
3-278 |
2.41e-60 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 194.51 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 3 LWFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHVLVV 82
Cdd:PLN02823 31 LWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 83 GGGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPV-- 160
Cdd:PLN02823 111 GGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPVeg 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 161 GPAAGLFTKGFYAGIAKA-LKEDGIFVAQTdNP--WFKADLIKNAIHDT-KEIFPIARLYTCNIPTYPSgMWTFTMGS-K 235
Cdd:PLN02823 191 GPCYQLYTKSFYERIVKPkLNPGGIFVTQA-GPagILTHKEVFSSIYNTlRQVFKYVVPYTAHVPSFAD-TWGWVMASdH 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2023325848 236 KHDPLNVED-----GHFFEIDTKYYTKELHSASFVLPKFVQELCEDNK 278
Cdd:PLN02823 269 PFADLSAEEldsriKERIDGELKYLDGETFSSAFALNKTVRQALANET 316
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
21-194 |
3.24e-32 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 122.67 E-value: 3.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 21 RTLESEKTTFQQLDMLETQEFGNmLLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHVLVVGGGDGGTIREVLKHTSVE 100
Cdd:COG4262 233 PVVYSEQTPYQRIVVTRDKDDRR-LYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 101 KVTQVEIDGKVVEYSKKHlPHISS----EYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPAAG-LFTKGFYAGI 175
Cdd:COG4262 312 SVTLVDLDPEVTDLAKTN-PFLRElnggALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGkLYSVEFYRLV 390
|
170
....*....|....*....
gi 2023325848 176 AKALKEDGIFVAQTDNPWF 194
Cdd:COG4262 391 RRHLAPGGVLVVQATSPYF 409
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
25-268 |
4.98e-30 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 118.02 E-value: 4.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 25 SEKTTFQQLDMLET-QEFGNM--LLLDGMVMTSEKDEFVYHEMIAHVPLFTHPSPKHVLVVGGGDGGTIREVLKHTSVEK 101
Cdd:PRK03612 244 AEQTPYQRIVVTRRgNGRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVEQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 102 VTQVEIDGKVVEYSKKHlPHISS----EYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPAAG-LFTKGFYAGIA 176
Cdd:PRK03612 324 VTLVDLDPAMTELARTS-PALRAlnggALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGkLYSVEFYRLLK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 177 KALKEDGIFVAQTDNPWFKADL---IKNAIHDTKeiFPiARLYTCNIPTYpsGMWTFTM-GSKKHDPLNVEDghFFEIDT 252
Cdd:PRK03612 403 RRLAPDGLLVVQSTSPYFAPKAfwsIEATLEAAG--LA-TTPYHVNVPSF--GEWGFVLaGAGARPPLAVPT--ELPVPL 475
|
250
....*....|....*.
gi 2023325848 253 KYYTKELHSASFVLPK 268
Cdd:PRK03612 476 RFLDPALLAAAFVFPK 491
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
22-241 |
2.93e-18 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 83.48 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 22 TLESEKTTFQQLDMLETQEFgnMLLLDGMVMTSEKDEFVYHEMIAHvPLFTHP-SPKHVLVVGGGDGGTIREVLKHTSVE 100
Cdd:PRK01581 99 NLFAEKSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVH-PIMSKViDPKRVLILGGGDGLALREVLKYETVL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 101 KVTQVEIDGKVVEYSkKHLPHISS----EYGNPRVELIIGDGFEHIIKSENRYDVILVDSTEPVGPA-AGLFTKGFYAGI 175
Cdd:PRK01581 176 HVDLVDLDGSMINMA-RNVPELVSlnksAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATELlSTLYTSELFARI 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 176 AKALKEDGIFVAQTDNPwFKADLIKNAIHDTKEifpIARLYTCN----IPTYPSGmWTFTMGSKKHDPLN 241
Cdd:PRK01581 255 ATFLTEDGAFVCQSNSP-ADAPLVYWSIGNTIE---HAGLTVKSyhtiVPSFGTD-WGFHIAANSAYVLD 319
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
3-277 |
2.05e-17 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 3 LWFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTsEKDEFVYHEMIAHVPLFTHPSPKHVLVV 82
Cdd:PRK00536 1 MWITQEITPYLRKEYTIEAKLLDVRSEHNILEIFKSKDFGEIAMLNKQLLF-KNFLHIESELLAHMGGCTKKELKEVLIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 83 GGGDGGTIREVLKHTSveKVTQVEIDGKVVEYSKKHLPHISSEYGNPRVELiigdgFEHIIKSE-NRYDVILVDStepvg 161
Cdd:PRK00536 80 DGFDLELAHQLFKYDT--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTH-----AKQLLDLDiKKYDLIICLQ----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 162 paagLFTKGFYAGIAKALKEDGIFVAQTDNPWFKADLIKNAIHDTKEIFPIARLYTCniPTYPSGMWTFTMGSKKHDPLn 241
Cdd:PRK00536 148 ----EPDIHKIDGLKRMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFSIAMPFVA--PLRILSNKGYIYASFKTHPL- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2023325848 242 vEDGHFFEIDT----KYYTKELHSASFVLPKFVQELCEDN 277
Cdd:PRK00536 221 -KDLMLQKIEAlksvRYYNEDIHRAAFALPKNLQEVFKDN 259
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
3-55 |
8.30e-13 |
|
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: 61.52 E-value: 8.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2023325848 3 LWFTEKQTSSFGITGKVNRTLESEKTTFQQLDMLETQEFGNMLLLDGMVMTSE 55
Cdd:pfam17284 1 GWFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
70-186 |
2.81e-08 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 53.51 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 70 LFTHPSPKHVLVVGGGDGGTIREVLKHTSVEKVTQVEIDGKVVEYSKKH--LPHisseyGNPRVELIIGDGFEHIIKSEN 147
Cdd:PRK04457 61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHfeLPE-----NGERFEVIEADGAEYIAVHRH 135
|
90 100 110
....*....|....*....|....*....|....*....
gi 2023325848 148 RYDVILVDSTEPVGPAAGLFTKGFYAGIAKALKEDGIFV 186
Cdd:PRK04457 136 STDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFV 174
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
93-188 |
3.51e-07 |
|
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: 47.81 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 93 VLKHTSVEKVTQVEIDGKVVEYSKKhlphISSEYGNPRVELIIGDGFEHIIKSENRYDVILVDstePVGPAAGLFTKGFY 172
Cdd:cd02440 15 ALASGPGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISD---PPLHHLVEDLARFL 87
|
90
....*....|....*.
gi 2023325848 173 AGIAKALKEDGIFVAQ 188
Cdd:cd02440 88 EEARRLLKPGGVLVLT 103
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
101-191 |
3.24e-03 |
|
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: 37.47 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023325848 101 KVTQVEIDGKVVEYSKKHLphisSEYG-NPRVELIIGDGFEHIIK-SENRYDVILVDstepvgpAAGLFTKGFYAGIAKA 178
Cdd:COG4122 43 RLTTIEIDPERAAIARENF----ARAGlADRIRLILGDALEVLPRlADGPFDLVFID-------ADKSNYPDYLELALPL 111
|
90
....*....|...
gi 2023325848 179 LKEDGIFVAqtDN 191
Cdd:COG4122 112 LRPGGLIVA--DN 122
|
|
| |
