|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
74-316 |
0e+00 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 544.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 74 NGDQKKEPACFSTVIPGWFSEMSPMWPGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEM 153
Cdd:PLN02366 1 AAAPESEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 154 ITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGDGVAFLKN 233
Cdd:PLN02366 81 ITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 234 AAEGSYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKGSVNYAWTSVPT 313
Cdd:PLN02366 161 APEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYAWTTVPT 240
|
...
gi 145362282 314 YPR 316
Cdd:PLN02366 241 YPS 243
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
91-325 |
9.55e-99 |
|
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: 292.41 E-value: 9.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 91 WFSEMSPMwpGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLV 170
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 171 IGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGDGVAFLkNAAEGSYDAVIVDSSDPI 250
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFL-ADTENTFDVIIVDSTDPV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362282 251 GPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKgSVNYAWTSVPTYPRhwGHWIYAL 325
Cdd:TIGR00417 158 GPAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFP-ITEYYTAAIPTYPS--GLWTFTI 229
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
147-326 |
4.70e-89 |
|
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: 264.18 E-value: 4.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 147 ECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGD 226
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 227 GVAFLKNAAEGsYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKgSVNY 306
Cdd:pfam01564 81 GFKFLKDYLNT-FDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP-VVMP 158
|
170 180
....*....|....*....|
gi 145362282 307 AWTSVPTYPRHWghWIYALF 326
Cdd:pfam01564 159 YVATIPTYPSGG--WGFTVC 176
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
131-325 |
2.08e-81 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 245.12 E-value: 2.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 131 GKVLVLDGVIQLT-ERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFP 209
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 210 DVAIGYEDPRVNLVIGDGVAFLKNAAEgSYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDII 289
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 145362282 290 EDIVSNCREIFKGSVNYaWTSVPTYPRHWGhWIYAL 325
Cdd:COG0421 162 RRVLATLREVFPHVVLY-AAPVPTYGGGNV-FLLAL 195
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
167-278 |
2.18e-13 |
|
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: 65.53 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 167 KVLVIGGGDGGVLREVARHaSIEQIDMCEIDKMVVDVSKQffpdVAIGYEDPRVNLVIGDGVAFLKNaAEGSYDAVIVDs 246
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPE-ADESFDVIISD- 73
|
90 100 110
....*....|....*....|....*....|..
gi 145362282 247 sDPIGPAKELFEKpFFQSVARALRPGGVVCTQ 278
Cdd:cd02440 74 -PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
74-316 |
0e+00 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 544.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 74 NGDQKKEPACFSTVIPGWFSEMSPMWPGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEM 153
Cdd:PLN02366 1 AAAPESEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 154 ITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGDGVAFLKN 233
Cdd:PLN02366 81 ITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 234 AAEGSYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKGSVNYAWTSVPT 313
Cdd:PLN02366 161 APEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYAWTTVPT 240
|
...
gi 145362282 314 YPR 316
Cdd:PLN02366 241 YPS 243
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
88-325 |
3.27e-112 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 326.73 E-value: 3.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 88 IPGWFSEMSPmwPGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKK 167
Cdd:PRK00811 2 MELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 168 VLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIG-YEDPRVNLVIGDGVAFLKNaAEGSYDAVIVDS 246
Cdd:PRK00811 80 VLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAE-TENSFDVIIVDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 247 SDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKGS-VNYAWtsVPTYPRhwGHWIYAL 325
Cdd:PRK00811 159 TDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVrPYQAA--IPTYPS--GLWSFTF 234
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
91-325 |
9.55e-99 |
|
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: 292.41 E-value: 9.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 91 WFSEMSPMwpGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLV 170
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 171 IGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGDGVAFLkNAAEGSYDAVIVDSSDPI 250
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFL-ADTENTFDVIIVDSTDPV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362282 251 GPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKgSVNYAWTSVPTYPRhwGHWIYAL 325
Cdd:TIGR00417 158 GPAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFP-ITEYYTAAIPTYPS--GLWTFTI 229
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
147-326 |
4.70e-89 |
|
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: 264.18 E-value: 4.70e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 147 ECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGD 226
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 227 GVAFLKNAAEGsYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFKgSVNY 306
Cdd:pfam01564 81 GFKFLKDYLNT-FDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP-VVMP 158
|
170 180
....*....|....*....|
gi 145362282 307 AWTSVPTYPRHWghWIYALF 326
Cdd:pfam01564 159 YVATIPTYPSGG--WGFTVC 176
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
131-325 |
2.08e-81 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 245.12 E-value: 2.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 131 GKVLVLDGVIQLT-ERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFP 209
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 210 DVAIGYEDPRVNLVIGDGVAFLKNAAEgSYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTQAESLWLHMDII 289
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 145362282 290 EDIVSNCREIFKGSVNYaWTSVPTYPRHWGhWIYAL 325
Cdd:COG0421 162 RRVLATLREVFPHVVLY-AAPVPTYGGGNV-FLLAL 195
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
105-324 |
1.01e-56 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 186.81 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 105 SLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVAR 184
Cdd:PLN02823 44 SYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 185 HASIEQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLVIGDGVAFLkNAAEGSYDAVIVDSSDPI--GPAKELFEKPFF 262
Cdd:PLN02823 124 HKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAEL-EKRDEKFDVIIGDLADPVegGPCYQLYTKSFY 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362282 263 QSVARA-LRPGGVVCTQA--ESLWLHMDIIEDIVSNCREIFKGSVNYAwTSVPTYPRHWGhWIYA 324
Cdd:PLN02823 203 ERIVKPkLNPGGIFVTQAgpAGILTHKEVFSSIYNTLRQVFKYVVPYT-AHVPSFADTWG-WVMA 265
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
104-281 |
1.76e-47 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 165.04 E-value: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 104 HSLKVEKVLFQGKSDYQDVIVFQSATYgKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVA 183
Cdd:COG4262 227 QKLYGDPVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 184 RHASIEQIDMCEIDKMVVDVSKQ--FFPDVAIG-YEDPRVNLVIGDGVAFLKNAAEgSYDAVIVDSSDP--IGPAKeLFE 258
Cdd:COG4262 306 KYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDE-KYDVIIVDLPDPsnFSLGK-LYS 383
|
170 180
....*....|....*....|...
gi 145362282 259 KPFFQSVARALRPGGVVCTQAES 281
Cdd:COG4262 384 VEFYRLVRRHLAPGGVLVVQATS 406
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
110-281 |
7.42e-32 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 124.56 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 110 KVLFQGKSDYQDVIVFQSATYGKV---LVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHA 186
Cdd:PRK03612 240 PVVYAEQTPYQRIVVTRRGNGRGPdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 187 SIEQIDMCEIDKMVVDVSKQFFPDVAI---GYEDPRVNLVIGDGVAFLKNAAEgSYDAVIVDSSDPIGPA--KeLFEKPF 261
Cdd:PRK03612 320 DVEQVTLVDLDPAMTELARTSPALRALnggALDDPRVTVVNDDAFNWLRKLAE-KFDVIIVDLPDPSNPAlgK-LYSVEF 397
|
170 180
....*....|....*....|
gi 145362282 262 FQSVARALRPGGVVCTQAES 281
Cdd:PRK03612 398 YRLLKRRLAPDGLLVVQSTS 417
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
111-281 |
1.93e-25 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 104.66 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 111 VLFQGKSDYQDVIVFQSATYGkvLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASIEQ 190
Cdd:PRK01581 99 NLFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLH 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 191 IDMCEIDKMVVDVSKQFFPDVAI---GYEDPRVNLVIGDGVAFLkNAAEGSYDAVIVDSSDPIGPA-KELFEKPFFQSVA 266
Cdd:PRK01581 177 VDLVDLDGSMINMARNVPELVSLnksAFFDNRVNVHVCDAKEFL-SSPSSLYDVIIIDFPDPATELlSTLYTSELFARIA 255
|
170
....*....|....*
gi 145362282 267 RALRPGGVVCTQAES 281
Cdd:PRK01581 256 TFLTEDGAFVCQSNS 270
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
90-144 |
1.49e-22 |
|
Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.
Pssm-ID: 407397 [Multi-domain] Cd Length: 53 Bit Score: 88.49 E-value: 1.49e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 145362282 90 GWFSEMSPmwPGEAHSLKVEKVLFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTE 144
Cdd:pfam17284 1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
167-278 |
2.18e-13 |
|
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: 65.53 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 167 KVLVIGGGDGGVLREVARHaSIEQIDMCEIDKMVVDVSKQffpdVAIGYEDPRVNLVIGDGVAFLKNaAEGSYDAVIVDs 246
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPE-ADESFDVIISD- 73
|
90 100 110
....*....|....*....|....*....|..
gi 145362282 247 sDPIGPAKELFEKpFFQSVARALRPGGVVCTQ 278
Cdd:cd02440 74 -PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
147-283 |
5.02e-11 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 61.98 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 147 ECAY-QEMITHLPLCsiPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFpdvAIGYEDPRVNLVIG 225
Cdd:PRK04457 50 ELAYtRAMMGFLLFN--PRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHF---ELPENGERFEVIEA 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 145362282 226 DGVAFLKNAAEgSYDAVIVDSSDPIGPAKELFEKPFFQSVARALRPGGVVCTqaeSLW 283
Cdd:PRK04457 125 DGAEYIAVHRH-STDVILVDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVV---NLW 178
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
108-301 |
1.47e-08 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 54.87 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 108 VEKVLFQGKSDYQDVIVFQSATYGKVLVLDGviQLTERDECAYQ-EMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHA 186
Cdd:PRK00536 17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 187 SieQIDMCEIDKMVVDVSKQFFPDVAIGYEDPRVNLvigdgVAFLKNAAEGSYDAVIVDSsdpigpakeLFEKPFFQSVA 266
Cdd:PRK00536 95 T--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTH-----AKQLLDLDIKKYDLIICLQ---------EPDIHKIDGLK 158
|
170 180 190
....*....|....*....|....*....|....*
gi 145362282 267 RALRPGGVVCTQAESLWLHMDIIEDIVSNCREIFK 301
Cdd:PRK00536 159 RMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFS 193
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
159-275 |
1.91e-08 |
|
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: 53.26 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 159 LCSIPNPKKVLVIGGGdGGV--------LREVARhasieqIDMCEIDKMVVDVSKQFFPDVaiGYEDpRVNLVIGDGVAF 230
Cdd:COG4122 11 LARLLGAKRILEIGTG-TGYstlwlaraLPDDGR------LTTIEIDPERAAIARENFARA--GLAD-RIRLILGDALEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 145362282 231 LKNAAEGSYDAVIVDSsdpigpAKELFeKPFFQSVARALRPGGVV 275
Cdd:COG4122 81 LPRLADGPFDLVFIDA------DKSNY-PDYLELALPLLRPGGLI 118
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
162-275 |
5.94e-08 |
|
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: 50.79 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 162 IPNPKKVLVIGGGDGGVLREVARHAsiEQIDMCEIDKMVVDVSKQFFPDVaigyedpRVNLVIGDGVAFlkNAAEGSYDA 241
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAEL-------NVDFVQGDLEDL--PLEDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 145362282 242 VIvdSSDPIgpakELFEKP--FFQSVARALRPGGVV 275
Cdd:COG2227 91 VI--CSEVL----EHLPDPaaLLRELARLLKPGGLL 120
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
153-299 |
1.04e-07 |
|
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification
Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 51.34 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 153 MITHLPlcsIPNPKKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIgyedPRVNLVIGDGvafLK 232
Cdd:COG2813 41 LLEHLP---EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGL----ENVEVLWSDG---LS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145362282 233 NAAEGSYDAVIvdsSDP---IGPA--KELFEKpFFQSVARALRPGGVVCTQAES-LWLHmDIIEDIVSNCREI 299
Cdd:COG2813 111 GVPDGSFDLIL---SNPpfhAGRAvdKEVAHA-LIADAARHLRPGGELWLVANRhLPYE-RKLEELFGNVEVL 178
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
168-273 |
4.75e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 47.17 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 168 VLVIGGGDGGVLREVARHASIeQIDMCEIDKMVVDVSKQFFPDvaigyEDPRVNLVIGDGVAFlkNAAEGSYDAVIvdSS 247
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRGGA-RVTGVDLSPEMLERARERAAE-----AGLNVEFVQGDAEDL--PFPDGSFDLVV--SS 70
|
90 100 110
....*....|....*....|....*....|
gi 145362282 248 DPIgpakELFEKP----FFQSVARALRPGG 273
Cdd:pfam13649 71 GVL----HHLPDPdleaALREIARVLKPGG 96
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
214-275 |
1.27e-06 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 49.14 E-value: 1.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362282 214 GYEDPRVNLVIGDGVAFLKNAAEGSYDAVIvdsSDP--IGPAKELFEKPFFQSVARALRPGGVV 275
Cdd:COG2521 179 ELANERIKIILGDASEVIKTFPDESFDAII---HDPprFSLAGELYSLEFYRELYRVLKPGGRL 239
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
149-276 |
2.73e-06 |
|
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: 46.14 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 149 AYQEMITHLplcSIPNPKKVLVIGGGDGGVLREVARHASieQIDMCEIDKMVVDVSKQFFPDvaigyEDPRVNLVIGDGV 228
Cdd:COG2226 10 GREALLAAL---GLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAE-----AGLNVEFVVGDAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 145362282 229 AFlkNAAEGSYDAVIvdSSDPIgpakELFEKP--FFQSVARALRPGGVVC 276
Cdd:COG2226 80 DL--PFPDGSFDLVI--SSFVL----HHLPDPerALAEIARVLKPGGRLV 121
|
|
| Methyltransf_30 |
pfam05430 |
S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine ... |
204-277 |
1.44e-05 |
|
S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase. It is often found in association with pfam01266, where it is responsible for catalysing the transfer of a methyl group from S-adenosyl-L-methionine to 5-aminomethyl-2-thiouridine to form 5-methylaminomethyl-2-thiouridine.
Pssm-ID: 398864 [Multi-domain] Cd Length: 124 Bit Score: 43.81 E-value: 1.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362282 204 SKQFFPDVAIGYEDPRVNLVIGDGVAFLKnAAEGSYDAVIVDssdPIGPAK--ELFEKPFFQSVARALRPGGVVCT 277
Cdd:pfam05430 17 PLAGCHRIEFAGGRVTLDLWFGDARAALP-ELDFKADAWFLD---GFSPAKnpEMWTEEFFALLARRSKPGGTLAT 88
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
169-275 |
5.63e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.58 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 169 LVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVaIGYEDPRVNLVIGDgvafLKNAAEGSYDAVIvdssd 248
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAAL-GLLNAVRVELFQLD----LGELDPGSFDVVV----- 70
|
90 100 110
....*....|....*....|....*....|..
gi 145362282 249 pigpAKELFE-----KPFFQSVARALRPGGVV 275
Cdd:pfam08242 71 ----ASNVLHhladpRAVLRNIRRLLKPGGVL 98
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
215-287 |
7.59e-05 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 43.61 E-value: 7.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362282 215 YEDPRVNLVIGDgvaFLKNAAEGSYDAVIVDSSDPIgpakELFEKpffqsVARALRPGGVVC------TQAESLWLHMD 287
Cdd:COG2519 140 GLPDNVELKLGD---IREGIDEGDVDAVFLDMPDPW----EALEA-----VAKALKPGGVLVayvptvNQVSKLVEALR 206
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
167-279 |
1.01e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 41.84 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 167 KVLVIGGGDGGVLREVARHA---------SIEQIDMCeidkmvvdvsKQFFpdVAIGYEDpRVNLVIGDgvaFLKNAAEG 237
Cdd:COG2230 54 RVLDIGCGWGGLALYLARRYgvrvtgvtlSPEQLEYA----------RERA--AEAGLAD-RVEVRLAD---YRDLPADG 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145362282 238 SYDAVIvdssdpigpAKELFE-------KPFFQSVARALRPGGVVCTQA 279
Cdd:COG2230 118 QFDAIV---------SIGMFEhvgpenyPAYFAKVARLLKPGGRLLLHT 157
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
145-282 |
1.97e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 41.83 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 145 RDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHASiEQIDMCEIDKMVVDVSKQFFPDVAIGyedpRVNLVI 224
Cdd:COG0500 7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG-GRVIGIDLSPEAIALARARAAKAGLG----NVEFLV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 145362282 225 GDgVAFLKNAAEGSYDAVIV-DSSDPIGPAKElfeKPFFQSVARALRPGGVVCTQAESL 282
Cdd:COG0500 82 AD-LAELDPLPAESFDLVVAfGVLHHLPPEER---EALLRELARALKPGGVLLLSASDA 136
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
166-302 |
2.54e-03 |
|
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.
Pssm-ID: 428349 [Multi-domain] Cd Length: 170 Bit Score: 37.96 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 166 KKVLVIGGGDGGVLREVARHASIEQIDMCEIDKMVVDVSKQFFPDVAIgyedPRVNLVIGDGvafLKNAAEGSYDAVIvd 245
Cdd:pfam05175 33 GKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGL----ENGEVVASDV---YSGVEDGKFDLII-- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145362282 246 SSDPIGPAKELFEK---PFFQSVARALRPGGvvctqaeSLWL----HM---DIIEDIVSNCREIFKG 302
Cdd:pfam05175 104 SNPPFHAGLATTYNvaqRFIADAKRHLRPGG-------ELWIvanrFLgypPLLEELFGNVEVVAKT 163
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
150-276 |
2.82e-03 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 38.06 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362282 150 YQEMITHLPlcsIPNPKKVLVIGGGDGGVLREVARHAsieqidmceiDKMV-VDVSKQFfpdVAIGYEDPR-VNLVIGDG 227
Cdd:COG4976 35 AEELLARLP---PGPFGRVLDLGCGTGLLGEALRPRG----------YRLTgVDLSEEM---LAKAREKGVyDRLLVADL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 145362282 228 VAFlkNAAEGSYDAVIvdSSDPIGPAKELfeKPFFQSVARALRPGGVVC 276
Cdd:COG4976 99 ADL--AEPDGRFDLIV--AADVLTYLGDL--AAVFAGVARALKPGGLFI 141
|
|
| |
