|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
35-340 |
0e+00 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 639.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 35 GGEIKEPSCMSSIIPGWFSEISPMWPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMI 114
Cdd:PLN02366 2 AAPESEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 115 THLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLKNA 194
Cdd:PLN02366 82 THLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 195 AEGTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGSVNYAWTSVPTY 274
Cdd:PLN02366 162 PEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYAWTTVPTY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3176685 275 PSGVIGFMLCSSEGPQVDFKKPVSLIDTDESSIKSHCPLKYYNAEIHSAAFCLPSFAKKVIDSKAN 340
Cdd:PLN02366 242 PSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESLLT 307
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
51-330 |
6.04e-116 |
|
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: 336.32 E-value: 6.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 51 WFSEISPMwpGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLV 130
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 131 IGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLkNAAEGTYDAVIVDSSDPI 210
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFL-ADTENTFDVIIVDSTDPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 211 GPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKgSVNYAWTSVPTYPSGVIGFMLCsSEGPQ 290
Cdd:TIGR00417 158 GPAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFP-ITEYYTAAIPTYPSGLWTFTIA-SKNKY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 3176685 291 VDFKKPVSLIDTDESSIKshcpLKYYNAEIHSAAFCLPSF 330
Cdd:TIGR00417 236 RPLEVEIRRIKFEAEDGK----TKYYNPDIHKAAFVLPKW 271
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
107-288 |
8.04e-91 |
|
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: 269.19 E-value: 8.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 107 ECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGD 186
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 187 GVAFLKNAAEgTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKgSVNY 266
Cdd:pfam01564 81 GFKFLKDYLN-TFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP-VVMP 158
|
170 180
....*....|....*....|..
gi 3176685 267 AWTSVPTYPSGVIGFMLCSSEG 288
Cdd:pfam01564 159 YVATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
91-277 |
9.57e-80 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 241.66 E-value: 9.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 91 GKVLVLDGVIQLT-ERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFP 169
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 170 NVAVGYEDPRVNLIIGDGVAFLKNAAEgTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDII 249
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180
....*....|....*....|....*...
gi 3176685 250 EDIVSNCRDIFKGSVNYaWTSVPTYPSG 277
Cdd:COG0421 162 RRVLATLREVFPHVVLY-AAPVPTYGGG 188
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
127-238 |
1.25e-12 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 63.60 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 127 KVLVIGGGDGGVLREVARHsSVEQIDICEIDKMVVDVAKQyfpnVAVGYEDPRVNLIIGDGVAFLKNaAEGTYDAVIVDs 206
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPE-ADESFDVIISD- 73
|
90 100 110
....*....|....*....|....*....|..
gi 3176685 207 sDPIGPAKELFEKpFFESVNRALRPGGVVCTQ 238
Cdd:cd02440 74 -PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
131-234 |
5.09e-03 |
|
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.
Pssm-ID: 468290 [Multi-domain] Cd Length: 480 Bit Score: 38.67 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 131 IGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFpnvavgYEDP-RVNLIIGDGVAFLKNAAEGTYDAVIVDS-SD 208
Cdd:NF037959 282 IGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDF------WFDPaSATVLHEDARRALRRRPEERFDVIVGDAfTD 355
|
90 100
....*....|....*....|....*.
gi 3176685 209 PIGPAkELFEKPFFESVNRALRPGGV 234
Cdd:NF037959 356 IAVPA-HLVTREFFELVRARLTPDGV 380
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02366 |
PLN02366 |
spermidine synthase |
35-340 |
0e+00 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 639.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 35 GGEIKEPSCMSSIIPGWFSEISPMWPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMI 114
Cdd:PLN02366 2 AAPESEAKCHSTVIPGWFSEISPMWPGEAHSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 115 THLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLKNA 194
Cdd:PLN02366 82 THLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 195 AEGTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGSVNYAWTSVPTY 274
Cdd:PLN02366 162 PEGTYDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCTQAESMWLHMDLIEDLIAICRETFKGSVNYAWTTVPTY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3176685 275 PSGVIGFMLCSSEGPQVDFKKPVSLIDTDESSIKSHCPLKYYNAEIHSAAFCLPSFAKKVIDSKAN 340
Cdd:PLN02366 242 PSGVIGFVLCSKEGPAVDFKHPVNPIDKLEGAGKAKRPLKFYNSEVHRAAFCLPSFAKRELESLLT 307
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
48-336 |
2.26e-123 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 355.62 E-value: 2.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 48 IPGWFSEISPmwPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKK 127
Cdd:PRK00811 2 MELWFTETLT--DNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 128 VLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVG-YEDPRVNLIIGDGVAFLKNaAEGTYDAVIVDS 206
Cdd:PRK00811 80 VLIIGGGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLPEIAGGaYDDPRVELVIGDGIKFVAE-TENSFDVIIVDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 207 SDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGS-VNYAWtsVPTYPSGVIGFMLCS 285
Cdd:PRK00811 159 TDPVGPAEGLFTKEFYENCKRALKEDGIFVAQSGSPFYQADEIKDMHRKLKEVFPIVrPYQAA--IPTYPSGLWSFTFAS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 3176685 286 SEGPqvdfKKPVSLIDTDESSIKSHCPLKYYNAEIHSAAFCLPSFAKKVID 336
Cdd:PRK00811 237 KNDD----LKFLPLDVIEARFAERGIKTRYYNPELHKAAFALPQFVKDALK 283
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
51-330 |
6.04e-116 |
|
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: 336.32 E-value: 6.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 51 WFSEISPMwpGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLV 130
Cdd:TIGR00417 1 WFTEYHDK--NFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 131 IGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLkNAAEGTYDAVIVDSSDPI 210
Cdd:TIGR00417 79 IGGGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFL-ADTENTFDVIIVDSTDPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 211 GPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKgSVNYAWTSVPTYPSGVIGFMLCsSEGPQ 290
Cdd:TIGR00417 158 GPAETLFTKEFYELLKKALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFP-ITEYYTAAIPTYPSGLWTFTIA-SKNKY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 3176685 291 VDFKKPVSLIDTDESSIKshcpLKYYNAEIHSAAFCLPSF 330
Cdd:TIGR00417 236 RPLEVEIRRIKFEAEDGK----TKYYNPDIHKAAFVLPKW 271
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
107-288 |
8.04e-91 |
|
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: 269.19 E-value: 8.04e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 107 ECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGD 186
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 187 GVAFLKNAAEgTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKgSVNY 266
Cdd:pfam01564 81 GFKFLKDYLN-TFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP-VVMP 158
|
170 180
....*....|....*....|..
gi 3176685 267 AWTSVPTYPSGVIGFMLCSSEG 288
Cdd:pfam01564 159 YVATIPTYPSGGWGFTVCSKNP 180
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
91-277 |
9.57e-80 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 241.66 E-value: 9.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 91 GKVLVLDGVIQLT-ERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFP 169
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 170 NVAVGYEDPRVNLIIGDGVAFLKNAAEgTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDII 249
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEE-SYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180
....*....|....*....|....*...
gi 3176685 250 EDIVSNCRDIFKGSVNYaWTSVPTYPSG 277
Cdd:COG0421 162 RRVLATLREVFPHVVLY-AAPVPTYGGG 188
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
65-328 |
1.42e-57 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 189.51 E-value: 1.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 65 SLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVAR 144
Cdd:PLN02823 44 SYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 145 HSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLkNAAEGTYDAVIVDSSDPI--GPAKELFEKPFF 222
Cdd:PLN02823 124 HKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIINDARAEL-EKRDEKFDVIIGDLADPVegGPCYQLYTKSFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 223 ES-VNRALRPGGVVCTQA--ESLWLHMDIIEDIVSNCRDIFKGSVNYAwTSVPTYPSgVIGFMLcSSEGPQVDfkkpVSL 299
Cdd:PLN02823 203 ERiVKPKLNPGGIFVTQAgpAGILTHKEVFSSIYNTLRQVFKYVVPYT-AHVPSFAD-TWGWVM-ASDHPFAD----LSA 275
|
250 260 270
....*....|....*....|....*....|.
gi 3176685 300 IDTDeSSIKSHC--PLKYYNAEIHSAAFCLP 328
Cdd:PLN02823 276 EELD-SRIKERIdgELKYLDGETFSSAFALN 305
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
64-241 |
9.04e-48 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 166.19 E-value: 9.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 64 HSLKVEKILFQGKSDYQDVIVFQSATYgKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVA 143
Cdd:COG4262 227 QKLYGDPVVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 144 RHSSVEQIDICEIDKMVVDVAKQ--YFPNVAVG-YEDPRVNLIIGDGVAFLKNAAEgTYDAVIVDSSDP--IGPAKeLFE 218
Cdd:COG4262 306 KYPDVESVTLVDLDPEVTDLAKTnpFLRELNGGaLNDPRVTVVNADAFQFLRETDE-KYDVIIVDLPDPsnFSLGK-LYS 383
|
170 180
....*....|....*....|...
gi 3176685 219 KPFFESVNRALRPGGVVCTQAES 241
Cdd:COG4262 384 VEFYRLVRRHLAPGGVLVVQATS 406
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
70-241 |
6.26e-32 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 124.95 E-value: 6.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 70 KILFQGKSDYQDVIVFQSATYGKV---LVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHS 146
Cdd:PRK03612 240 PVVYAEQTPYQRIVVTRRGNGRGPdlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 147 SVEQIDICEIDKMVVDVAKQYFPNVAV---GYEDPRVNLIIGDGVAFLKNAAEgTYDAVIVDSSDPIGPA--KeLFEKPF 221
Cdd:PRK03612 320 DVEQVTLVDLDPAMTELARTSPALRALnggALDDPRVTVVNDDAFNWLRKLAE-KFDVIIVDLPDPSNPAlgK-LYSVEF 397
|
170 180
....*....|....*....|
gi 3176685 222 FESVNRALRPGGVVCTQAES 241
Cdd:PRK03612 398 YRLLKRRLAPDGLLVVQSTS 417
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
71-241 |
5.46e-26 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 106.59 E-value: 5.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 71 ILFQGKSDYQDVIVFQSATYGkvLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQ 150
Cdd:PRK01581 99 NLFAEKSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLH 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 151 IDICEIDKMVVDVAKQYFPNVAV---GYEDPRVNLIIGDGVAFLkNAAEGTYDAVIVDSSDPIGPA-KELFEKPFFESVN 226
Cdd:PRK01581 177 VDLVDLDGSMINMARNVPELVSLnksAFFDNRVNVHVCDAKEFL-SSPSSLYDVIIIDFPDPATELlSTLYTSELFARIA 255
|
170
....*....|....*
gi 3176685 227 RALRPGGVVCTQAES 241
Cdd:PRK01581 256 TFLTEDGAFVCQSNS 270
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
50-104 |
1.54e-23 |
|
Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.
Pssm-ID: 407397 [Multi-domain] Cd Length: 53 Bit Score: 91.57 E-value: 1.54e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 3176685 50 GWFSEISPmwPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTE 104
Cdd:pfam17284 1 GWFTEIHD--LGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
68-335 |
7.47e-13 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 67.58 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 68 VEKILFQGKSDYQDVIVFQSATYGKVLVLDGviQLTERDECAYQ-EMITHLPLCSISNPKKVLVIGGGDGGVLREVARHS 146
Cdd:PRK00536 17 IEAKLLDVRSEHNILEIFKSKDFGEIAMLNK--QLLFKNFLHIEsELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 147 SveQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIigdgvAFLKNAAEGTYDAVIVDSsdpigpakeLFEKPFFESVN 226
Cdd:PRK00536 95 T--HVDFVQADEKILDSFISFFPHFHEVKNNKNFTHA-----KQLLDLDIKKYDLIICLQ---------EPDIHKIDGLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 227 RALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKgsvnyawTSVPTYPSGVI----GFMLCSSE-GPQVDFKKPVslID 301
Cdd:PRK00536 159 RMLKEDGVFISVAKHPLLEHVSMQNALKNMGDFFS-------IAMPFVAPLRIlsnkGYIYASFKtHPLKDLMLQK--IE 229
|
250 260 270
....*....|....*....|....*....|....
gi 3176685 302 TDESsikshcpLKYYNAEIHSAAFCLPSFAKKVI 335
Cdd:PRK00536 230 ALKS-------VRYYNEDIHRAAFALPKNLQEVF 256
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
127-238 |
1.25e-12 |
|
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).
Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 63.60 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 127 KVLVIGGGDGGVLREVARHsSVEQIDICEIDKMVVDVAKQyfpnVAVGYEDPRVNLIIGDGVAFLKNaAEGTYDAVIVDs 206
Cdd:cd02440 1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPE-ADESFDVIISD- 73
|
90 100 110
....*....|....*....|....*....|..
gi 3176685 207 sDPIGPAKELFEKpFFESVNRALRPGGVVCTQ 238
Cdd:cd02440 74 -PPLHHLVEDLAR-FLEEARRLLKPGGVLVLT 103
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
119-235 |
5.46e-12 |
|
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: 63.28 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 119 LCSISNPKKVLVIGGGdGGV----LREVARHSSveQIDICEIDKMVVDVAKQYFpnVAVGYEDpRVNLIIGDGVAFLKNA 194
Cdd:COG4122 11 LARLLGAKRILEIGTG-TGYstlwLARALPDDG--RLTTIEIDPERAAIARENF--ARAGLAD-RIRLILGDALEVLPRL 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 3176685 195 AEGTYDAVIVDSsdpigpAKELFeKPFFESVNRALRPGGVV 235
Cdd:COG4122 85 ADGPFDLVFIDA------DKSNY-PDYLELALPLLRPGGLI 118
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
124-243 |
6.55e-12 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 64.68 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 124 NPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFpnvAVGYEDPRVNLIIGDGVAFLKNAAEGTyDAVI 203
Cdd:PRK04457 66 RPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHF---ELPENGERFEVIEADGAEYIAVHRHST-DVIL 141
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 3176685 204 VDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTqaeSLW 243
Cdd:PRK04457 142 VDGFDGEGIIDALCTQPFFDDCRNALSSDGIFVV---NLW 178
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
122-235 |
9.88e-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: 50.02 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 122 ISNPKKVLVIGGGDGGVLREVARHssVEQIDICEIDKMVVDVAKQYFPNVavgyedpRVNLIIGDGVAFlkNAAEGTYDA 201
Cdd:COG2227 22 LPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL-------NVDFVQGDLEDL--PLEDGSFDL 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 3176685 202 VIvdSSDPIgpakELFEKP--FFESVNRALRPGGVV 235
Cdd:COG2227 91 VI--CSEVL----EHLPDPaaLLRELARLLKPGGLL 120
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
128-233 |
2.64e-07 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 47.94 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 128 VLVIGGGDGGVLREVARH--SSVEQIDICEidKMVvDVAKQYFpnvavGYEDPRVNLIIGDGVAFlkNAAEGTYDAVIvd 205
Cdd:pfam13649 1 VLDLGCGTGRLTLALARRggARVTGVDLSP--EML-ERARERA-----AEAGLNVEFVQGDAEDL--PFPDGSFDLVV-- 68
|
90 100 110
....*....|....*....|....*....|..
gi 3176685 206 SSDPIgpakELFEKP----FFESVNRALRPGG 233
Cdd:pfam13649 69 SSGVL----HHLPDPdleaALREIARVLKPGG 96
|
|
| COG2521 |
COG2521 |
Predicted archaeal methyltransferase [General function prediction only]; |
126-235 |
1.64e-06 |
|
Predicted archaeal methyltransferase [General function prediction only];
Pssm-ID: 442011 [Multi-domain] Cd Length: 285 Bit Score: 48.75 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 126 KKVLVIGGGDGGVLREVARHSsVEQIDICEIDKMVVDVAKQ--YFPnvavGYEDPRVNLIIGDGVAFLKNAAEGTYDAVI 203
Cdd:COG2521 134 DRVLDTCTGLGYTAIEALKRG-AREVITVEKDPNVLELAELnpWSR----ELANERIKIILGDASEVIKTFPDESFDAII 208
|
90 100 110
....*....|....*....|....*....|....
gi 3176685 204 vdsSDP--IGPAKELFEKPFFESVNRALRPGGVV 235
Cdd:COG2521 209 ---HDPprFSLAGELYSLEFYRELYRVLKPGGRL 239
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
109-236 |
6.56e-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: 45.37 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 109 AYQEMITHLPLcsiSNPKKVLVIGGGDGGVLREVARHSSveQIDICEIDKMVVDVAKQYFPNvavgyEDPRVNLIIGDGV 188
Cdd:COG2226 10 GREALLAALGL---RPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELARERAAE-----AGLNVEFVVGDAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 3176685 189 AFlkNAAEGTYDAVIvdSSDPIgpakELFEKP--FFESVNRALRPGGVVC 236
Cdd:COG2226 80 DL--PFPDGSFDLVI--SSFVL----HHLPDPerALAEIARVLKPGGRLV 121
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
162-247 |
2.15e-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: 45.15 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 162 DVAKQyfpNVAVGYEDPRVNLIIGDgvaFLKNAAEGTYDAVIVDSSDPIgpakelfekPFFESVNRALRPGGVVC----- 236
Cdd:COG2519 130 EIARK---NLERFGLPDNVELKLGD---IREGIDEGDVDAVFLDMPDPW---------EALEAVAKALKPGGVLVayvpt 194
|
90
....*....|..
gi 3176685 237 -TQAESLWLHMD 247
Cdd:COG2519 195 vNQVSKLVEALR 206
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
129-235 |
7.96e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.20 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 129 LVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFpNVAVGYEDPRVNLIIGDgvafLKNAAEGTYDAVIvdssd 208
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERL-AALGLLNAVRVELFQLD----LGELDPGSFDVVV----- 70
|
90 100 110
....*....|....*....|....*....|..
gi 3176685 209 pigpAKELFE-----KPFFESVNRALRPGGVV 235
Cdd:pfam08242 71 ----ASNVLHhladpRAVLRNIRRLLKPGGVL 98
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
113-259 |
1.20e-04 |
|
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: 42.48 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 113 MITHLPlcsISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQyfpNVAVgYEDPRVNLIIGDGvafLK 192
Cdd:COG2813 41 LLEHLP---EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARA---NAAA-NGLENVEVLWSDG---LS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3176685 193 NAAEGTYDAVIvdsSDP---IGPA--KELFEKpFFESVNRALRPGGVVCTQAES-LWLHmDIIEDIVSNCRDI 259
Cdd:COG2813 111 GVPDGSFDLIL---SNPpfhAGRAvdKEVAHA-LIADAARHLRPGGELWLVANRhLPYE-RKLEELFGNVEVL 178
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
127-239 |
1.51e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 41.45 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 127 KVLVIGGGDGGVLREVARH---------SSVEQIDIceidkmvvdvAKQYFpnVAVGYEDpRVNLIIGDgvaFLKNAAEG 197
Cdd:COG2230 54 RVLDIGCGWGGLALYLARRygvrvtgvtLSPEQLEY----------ARERA--AEAGLAD-RVEVRLAD---YRDLPADG 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 3176685 198 TYDAVIvdssdpigpAKELFE-------KPFFESVNRALRPGGVVCTQA 239
Cdd:COG2230 118 QFDAIV---------SIGMFEhvgpenyPAYFAKVARLLKPGGRLLLHT 157
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
105-242 |
2.60e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 41.44 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 105 RDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVAR--HSSVEQIDICEIdkmVVDVAKQyfpnVAVGYEDPRVNL 182
Cdd:COG0500 7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAArfGGRVIGIDLSPE---AIALARA----RAAKAGLGNVEF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3176685 183 IIGDgVAFLKNAAEGTYDAVIV-DSSDPIGPAKElfeKPFFESVNRALRPGGVVCTQAESL 242
Cdd:COG0500 80 LVAD-LAELDPLPAESFDLVVAfGVLHHLPPEER---EALLRELARALKPGGVLLLSASDA 136
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
110-236 |
1.06e-03 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 39.60 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 110 YQEMITHLPlcsISNPKKVLVIGGGDGGVLREVA-RHSSVEQIDICEidKMVvDVAKQyfpnvavgyEDPRVNLIIGDGV 188
Cdd:COG4976 35 AEELLARLP---PGPFGRVLDLGCGTGLLGEALRpRGYRLTGVDLSE--EML-AKARE---------KGVYDRLLVADLA 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 3176685 189 AFlkNAAEGTYDAVIvdSSDPIGPAKELfeKPFFESVNRALRPGGVVC 236
Cdd:COG4976 100 DL--AEPDGRFDLIV--AADVLTYLGDL--AAVFAGVARALKPGGLFI 141
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
125-235 |
1.67e-03 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 37.50 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 125 PKKVLVIGGGDGGVLREVARH---SSVEQIDICEidKMVvDVAKQYFPNVAVgyedprvnlIIGDGVAFlknAAEGTYDA 201
Cdd:COG4106 2 PRRVLDLGCGTGRLTALLAERfpgARVTGVDLSP--EML-ARARARLPNVRF---------VVADLRDL---DPPEPFDL 66
|
90 100 110
....*....|....*....|....*....|....*....
gi 3176685 202 VIVDSS-----DPigpaKELFEKpffesVNRALRPGGVV 235
Cdd:COG4106 67 VVSNAAlhwlpDH----AALLAR-----LAAALAPGGVL 96
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
131-234 |
5.09e-03 |
|
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major Facilitator Superfamily) transporter domain and a C-terminal spermidine synthase (SpdSyn)-like domain. The encoding genes usually near the genes encoding S-adenosylmethionine decarboxylase (AdoMetDC) on many bacterial genomes. It has been shown in Shewanella oneidensis that the fused protein aminopropylates a substrate other than putrescine, and has a role outside of polyamine biosynthesis.
Pssm-ID: 468290 [Multi-domain] Cd Length: 480 Bit Score: 38.67 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 131 IGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFpnvavgYEDP-RVNLIIGDGVAFLKNAAEGTYDAVIVDS-SD 208
Cdd:NF037959 282 IGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDF------WFDPaSATVLHEDARRALRRRPEERFDVIVGDAfTD 355
|
90 100
....*....|....*....|....*.
gi 3176685 209 PIGPAkELFEKPFFESVNRALRPGGV 234
Cdd:NF037959 356 IAVPA-HLVTREFFELVRARLTPDGV 380
|
|
| FtsJ |
pfam01728 |
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
177-262 |
8.66e-03 |
|
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 36.80 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3176685 177 DPRVNLIIGD-----GVAFLKNAAEGTYDAVIVDSSDPIGPAKELFE-------KPFFESVNRALRPGGVVCTQAeslwL 244
Cdd:pfam01728 63 DPGVTFIQGDirdpeTLDLLEELLGRKVDLVLSDGSPFISGNKVLDHlrsldlvKAALEVALELLRKGGNFVCKV----F 138
|
90
....*....|....*...
gi 3176685 245 HMDIIEDIVSNCRDIFKG 262
Cdd:pfam01728 139 QGEDFSELLYLLKLGFEK 156
|
|
| |
