|
Name |
Accession |
Description |
Interval |
E-value |
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
1-360 |
0e+00 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 704.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 1 MPKHRKQSKIKIYRITNYKKDKRSELDSNKFELEQQAVENKQDKQGKQ--------------DNQVQSENVVIVPTDSHN 66
Cdd:PRK01581 1 MPKHRKQSKIKIYRITSYKKDKRSELDSNKFELEQQLVENKQDKQGKQykqdrgiqyaetkqDNQVQSENVVIVPTDSHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 67 LDIWDEISLKEIQAGEHTNLFAEQSNYQNINLLQVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGG 146
Cdd:PRK01581 81 LDIWDEISLKEIQAGEHTNLFAEKSNYQNINLLQVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 147 DGLALREVLKYETVLHVDLVDLDGSMIDMARNVPELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATE 226
Cdd:PRK01581 161 DGLALREVLKYETVLHVDLVDLDGSMINMARNVPELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 227 LLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSVYVLDQ 306
Cdd:PRK01581 241 LLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQ 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447046698 307 IEQLYVVPTPRTLPSLLFPLFQFKEEHLEQRNFALLNSESNLILHQCYKKEMEF 360
Cdd:PRK01581 321 IEQLYVVPTPRTLPSLLFPLFQFKEEHLEQRNFALLNSESNLILHQCYKKEMEF 374
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
86-276 |
1.16e-78 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 247.47 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVS-DIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVD 164
Cdd:COG4262 235 VYSEQTPYQRIVVTRDKdDRRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVESVT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 165 LVDLDGSMIDMARNVPELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATELLSTLYTSELFARIATFL 244
Cdd:COG4262 315 LVDLDPEVTDLAKTNPFLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGKLYSVEFYRLVRRHL 394
|
170 180 190
....*....|....*....|....*....|..
gi 447046698 245 TEDGAFVCQSNSPADAPLVYWSIGNTIEHAGL 276
Cdd:COG4262 395 APGGVLVVQATSPYFAPKAFWCIAKTLEAAGF 426
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
86-302 |
2.99e-40 |
|
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: 142.95 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 163
Cdd:TIGR00417 20 LYHEKSEFQDLEIFETEAFgnVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 164 DLVDLDGSMIDMARN-VPELvslnKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATElLSTLYTSELFARIAT 242
Cdd:TIGR00417 100 TLVDIDEKVIELSRKyLPNL----AGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGP-AETLFTKEFYELLKK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447046698 243 FLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTD-WGFHIAANSVY 302
Cdd:TIGR00417 175 ALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGlWTFTIASKNKY 235
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
119-297 |
2.82e-35 |
|
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: 127.05 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 119 EQIYHEALVH-PIMSKViDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMAR-NVPELvslnKSAFFDNRVN 196
Cdd:pfam01564 1 EFIYHEMIAHvPLCSHP-NPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKkFLPSL----AIGFQDPRVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 197 THVCDAKEFLSSPSSLYDVIIIDFPDPATeLLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGL 276
Cdd:pfam01564 76 VVIGDGFKFLKDYLNTFDVIIVDSTDPVG-PAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP 154
|
170 180
....*....|....*....|..
gi 447046698 277 TVKSYHTIVPSFGTD-WGFHIA 297
Cdd:pfam01564 155 VVMPYVATIPTYPSGgWGFTVC 176
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
139-253 |
2.89e-06 |
|
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: 45.50 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 139 RVLILGGGDGLALREVLKYEtVLHVDLVDLDGSMIDMARNvpelvslNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIII 218
Cdd:cd02440 1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPPEADESFDVIIS 72
|
90 100 110
....*....|....*....|....*....|....*
gi 447046698 219 DFPDPATELLstlyTSELFARIATFLTEDGAFVCQ 253
Cdd:cd02440 73 DPPLHHLVED----LARFLEEARRLLKPGGVLVLT 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
1-360 |
0e+00 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 704.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 1 MPKHRKQSKIKIYRITNYKKDKRSELDSNKFELEQQAVENKQDKQGKQ--------------DNQVQSENVVIVPTDSHN 66
Cdd:PRK01581 1 MPKHRKQSKIKIYRITSYKKDKRSELDSNKFELEQQLVENKQDKQGKQykqdrgiqyaetkqDNQVQSENVVIVPTDSHN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 67 LDIWDEISLKEIQAGEHTNLFAEQSNYQNINLLQVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGG 146
Cdd:PRK01581 81 LDIWDEISLKEIQAGEHTNLFAEKSNYQNINLLQVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 147 DGLALREVLKYETVLHVDLVDLDGSMIDMARNVPELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATE 226
Cdd:PRK01581 161 DGLALREVLKYETVLHVDLVDLDGSMINMARNVPELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPATE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 227 LLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSVYVLDQ 306
Cdd:PRK01581 241 LLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSAYVLDQ 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447046698 307 IEQLYVVPTPRTLPSLLFPLFQFKEEHLEQRNFALLNSESNLILHQCYKKEMEF 360
Cdd:PRK01581 321 IEQLYVVPTPRTLPSLLFPLFQFKEEHLEQRNFALLNSESNLILHQCYKKEMEF 374
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
87-352 |
3.11e-93 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 287.89 E-value: 3.11e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 87 FAEQSNYQNINL-----LQVSDIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVL 161
Cdd:PRK03612 243 YAEQTPYQRIVVtrrgnGRGPDLRLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPDVE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 162 HVDLVDLDGSMIDMARNVPELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATELLSTLYTSELFARIA 241
Cdd:PRK03612 323 QVTLVDLDPAMTELARTSPALRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPSNPALGKLYSVEFYRLLK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 242 TFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGtDWGFHIAANSVYVLDQIEQLYVVPTpRTL-P 320
Cdd:PRK03612 403 RRLAPDGLLVVQSTSPYFAPKAFWSIEATLEAAGLATTPYHVNVPSFG-EWGFVLAGAGARPPLAVPTELPVPL-RFLdP 480
|
250 260 270
....*....|....*....|....*....|..
gi 447046698 321 SLLFPLFQFKeehleqRNFALLNSESNLILHQ 352
Cdd:PRK03612 481 ALLAAAFVFP------KDMRRREVEPNTLNNP 506
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
86-276 |
1.16e-78 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 247.47 E-value: 1.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVS-DIRLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVD 164
Cdd:COG4262 235 VYSEQTPYQRIVVTRDKdDRRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVESVT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 165 LVDLDGSMIDMARNVPELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATELLSTLYTSELFARIATFL 244
Cdd:COG4262 315 LVDLDPEVTDLAKTNPFLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSLGKLYSVEFYRLVRRHL 394
|
170 180 190
....*....|....*....|....*....|..
gi 447046698 245 TEDGAFVCQSNSPADAPLVYWSIGNTIEHAGL 276
Cdd:COG4262 395 APGGVLVVQATSPYFAPKAFWCIAKTLEAAGF 426
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
106-297 |
5.27e-44 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 150.36 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 106 LYLDKQLQFS-SVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMARnvpELVS 184
Cdd:COG0421 6 LVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAR---EYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 185 LNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATeLLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVY 264
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVG-PAEGLFTREFYEDCRRALKPGGVLVVNLGSPFYGLDLL 161
|
170 180 190
....*....|....*....|....*....|...
gi 447046698 265 WSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIA 297
Cdd:COG0421 162 RRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
83-310 |
1.26e-41 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 148.29 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 83 HTNLFAEQSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETV 160
Cdd:PLN02823 48 NSVLHTGTSEFQDIALVDTKPFgkVLIIDGKMQSAEADEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 161 LHVDLVDLDGSMIDMARnvpELVSLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDP-ATELLSTLYTSELFAR 239
Cdd:PLN02823 128 EKVVMCDIDQEVVDFCR---KHLTVNREAFCDKRLELIINDARAELEKRDEKFDVIIGDLADPvEGGPCYQLYTKSFYER 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447046698 240 IA-TFLTEDGAFVCQSnSPA---DAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAANSVYVLDQIEQL 310
Cdd:PLN02823 205 IVkPKLNPGGIFVTQA-GPAgilTHKEVFSSIYNTLRQVFKYVVPYTAHVPSFADTWGWVMASDHPFADLSAEEL 278
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
86-257 |
1.99e-41 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 146.45 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVSDI-RLY-LDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 163
Cdd:PRK00811 24 LYEEKSPFQRIEIFETPEFgRLLaLDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIGGGDGGTLREVLKHPSVEKI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 164 DLVDLDGSMIDMARN-VPElvsLNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPA--TELlstLYTSELFARI 240
Cdd:PRK00811 104 TLVEIDERVVEVCRKyLPE---IAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPVgpAEG---LFTKEFYENC 177
|
170
....*....|....*..
gi 447046698 241 ATFLTEDGAFVCQSNSP 257
Cdd:PRK00811 178 KRALKEDGIFVAQSGSP 194
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
86-302 |
2.99e-40 |
|
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: 142.95 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVSDI--RLYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 163
Cdd:TIGR00417 20 LYHEKSEFQDLEIFETEAFgnVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIGGGDGGVLREVLKHKSVESA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 164 DLVDLDGSMIDMARN-VPELvslnKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIIIDFPDPATElLSTLYTSELFARIAT 242
Cdd:TIGR00417 100 TLVDIDEKVIELSRKyLPNL----AGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPVGP-AETLFTKEFYELLKK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447046698 243 FLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTD-WGFHIAANSVY 302
Cdd:TIGR00417 175 ALNPDGIFVAQSESPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYPSGlWTFTIASKNKY 235
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
119-297 |
2.82e-35 |
|
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: 127.05 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 119 EQIYHEALVH-PIMSKViDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMAR-NVPELvslnKSAFFDNRVN 196
Cdd:pfam01564 1 EFIYHEMIAHvPLCSHP-NPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKkFLPSL----AIGFQDPRVK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 197 THVCDAKEFLSSPSSLYDVIIIDFPDPATeLLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGL 276
Cdd:pfam01564 76 VVIGDGFKFLKDYLNTFDVIIVDSTDPVG-PAENLFSKPFFDLLKKALKEDGVFITQAESPWLHLELIINILKNGKQVFP 154
|
170 180
....*....|....*....|..
gi 447046698 277 TVKSYHTIVPSFGTD-WGFHIA 297
Cdd:pfam01564 155 VVMPYVATIPTYPSGgWGFTVC 176
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
86-257 |
1.99e-26 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 107.04 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 86 LFAEQSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETVLHV 163
Cdd:PLN02366 39 LFQGKSDFQDVLVFESATYGkvLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 164 DLVDLDGSMIDMARN-VPELVslnkSAFFDNRVNTHVCDAKEFL-SSPSSLYDVIIIDFPD---PATELLSTLYtselFA 238
Cdd:PLN02366 119 DICEIDKMVIDVSKKfFPDLA----VGFDDPRVNLHIGDGVEFLkNAPEGTYDAIIVDSSDpvgPAQELFEKPF----FE 190
|
170
....*....|....*....
gi 447046698 239 RIATFLTEDGAFVCQSNSP 257
Cdd:PLN02366 191 SVARALRPGGVVCTQAESM 209
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
137-253 |
1.13e-06 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 46.36 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 137 PKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMAR-NVPelvslnksaffdnRVNTHVCDAKEFlsSPSSLYDV 215
Cdd:COG4106 2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARaRLP-------------NVRFVVADLRDL--DPPEPFDL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 447046698 216 IIIDF-----PDPAtellstlytsELFARIATFLTEDGAFVCQ 253
Cdd:COG4106 67 VVSNAalhwlPDHA----------ALLARLAAALAPGGVLAVQ 99
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
139-253 |
2.89e-06 |
|
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: 45.50 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 139 RVLILGGGDGLALREVLKYEtVLHVDLVDLDGSMIDMARNvpelvslNKSAFFDNRVNTHVCDAKEFLSSPSSLYDVIII 218
Cdd:cd02440 1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK-------AAAALLADNVEVLKGDAEELPPEADESFDVIIS 72
|
90 100 110
....*....|....*....|....*....|....*
gi 447046698 219 DFPDPATELLstlyTSELFARIATFLTEDGAFVCQ 253
Cdd:cd02440 73 DPPLHHLVED----LARFLEEARRLLKPGGVLVLT 103
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
137-281 |
2.80e-05 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 44.22 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 137 PKRVLILGGGDGLALREVLKYetVLHVDLVDLDGSMIDMARnvpelvslNKSAffdnRVNTHVCDAKEFLSSPSSlYDVI 216
Cdd:COG4976 47 FGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAR--------EKGV----YDRLLVADLADLAEPDGR-FDLI 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447046698 217 IidfpdpATELLStlYTSEL---FARIATFLTEDGAFVCQSNSpADAPLVYWSIGNTIEH----AGLTVKSY 281
Cdd:COG4976 112 V------AADVLT--YLGDLaavFAGVARALKPGGLFIFSVED-ADGSGRYAHSLDYVRDllaaAGFEVPGL 174
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
118-251 |
5.43e-05 |
|
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: 42.31 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 118 DEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYetVLHVDLVDLDGSMIDMARnvpelvslnkSAFFDNRVNT 197
Cdd:COG2227 6 ARDFWDRRLAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIAR----------ERAAELNVDF 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447046698 198 HVCDAKEFLSSPSSlYDVII-----IDFPDPAtellstlytsELFARIATFLTEDGAFV 251
Cdd:COG2227 74 VQGDLEDLPLEDGS-FDLVIcsevlEHLPDPA----------ALLRELARLLKPGGLLL 121
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
140-248 |
5.59e-05 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 41.40 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 140 VLILGGGDGLALREVLKYeTVLHVDLVDLDGSMIDMARnvpelvslNKSAFFDNRVNTHVCDAkEFLSSPSSLYDVIIID 219
Cdd:pfam13649 1 VLDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERAR--------ERAAEAGLNVEFVQGDA-EDLPFPDGSFDLVVSS 70
|
90 100
....*....|....*....|....*....
gi 447046698 220 FpdpATELLSTLYTSELFARIATFLTEDG 248
Cdd:pfam13649 71 G---VLHHLPDPDLEAALREIARVLKPGG 96
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
137-277 |
9.38e-05 |
|
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: 41.90 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 137 PKRVLILGGGDGLALREVLKYETvlHVDLVDLDGSMIDMARnvpelvslNKSAFFDNRVNTHVCDAkEFLSSPSSLYDVI 216
Cdd:COG2226 23 GARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELAR--------ERAAEAGLNVEFVVGDA-EDLPFPDGSFDLV 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447046698 217 II-----DFPDPAtellstlytsELFARIATFLTEDGAFVCQSNSPADAplvyWSIGNTIEHAGLT 277
Cdd:COG2226 92 ISsfvlhHLPDPE----------RALAEIARVLKPGGRLVVVDFSPPDL----AELEELLAEAGFE 143
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
141-248 |
5.16e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 38.89 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 141 LILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMARNvpELVSLNKSAFFdnRVNTHVCDAKEFLSSPsslYDVIIidf 220
Cdd:pfam08242 1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARE--RLAALGLLNAV--RVELFQLDLGELDPGS---FDVVV--- 70
|
90 100
....*....|....*....|....*....
gi 447046698 221 pdpATELLSTL-YTSELFARIATFLTEDG 248
Cdd:pfam08242 71 ---ASNVLHHLaDPRAVLRNIRRLLKPGG 96
|
|
| speE |
PRK00536 |
spermidine synthase; Provisional |
108-257 |
5.59e-04 |
|
spermidine synthase; Provisional
Pssm-ID: 134311 [Multi-domain] Cd Length: 262 Bit Score: 41.00 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 108 LDKQLQFSSVdEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETvlHVDLVDLDGSMIDmarnvpELVSLNK 187
Cdd:PRK00536 45 LNKQLLFKNF-LHIESELLAHMGGCTKKELKEVLIVDGFDLELAHQLFKYDT--HVDFVQADEKILD------SFISFFP 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 188 SaFFDNRVNTHVCDAKEFLSSPSSLYDVIIidfpdpATELLSTLYTSELFAriatFLTEDGAFVCQSNSP 257
Cdd:PRK00536 116 H-FHEVKNNKNFTHAKQLLDLDIKKYDLII------CLQEPDIHKIDGLKR----MLKEDGVFISVAKHP 174
|
|
| Trm11 |
COG1041 |
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ... |
166-284 |
8.76e-04 |
|
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440663 [Multi-domain] Cd Length: 172 Bit Score: 39.55 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 166 VDLDGSMIDMARNvpelvslNKSAFFDNRVNTHVCDAKEfLSSPSSLYDVIIIDFP-----DPATELLSTLYTSelFARI 240
Cdd:COG1041 54 SDIDPKMVEGARE-------NLEHYGYEDADVIRGDARD-LPLADESVDAIVTDPPygrssKISGEELLELYEK--ALEE 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 447046698 241 ATFLTEDGAFVCQSnSPADaplvywsIGNTIEHAGLTVKSYHTI 284
Cdd:COG1041 124 AARVLKPGGRVVIV-TPRD-------IDELLEEAGFKVLERHEQ 159
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
136-217 |
2.17e-03 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 38.97 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 136 DPKRVLILGGGDGLALREVLKYETVLHVDLVDLDGSMIDMA-RNvpelVSLNKsafFDNRVNTHVCDAKEFLSS-PSSLY 213
Cdd:COG4123 37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELArRN----VALNG---LEDRITVIHGDLKEFAAElPPGSF 109
|
....
gi 447046698 214 DVII 217
Cdd:COG4123 110 DLVV 113
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
136-258 |
2.46e-03 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 38.74 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447046698 136 DPKRVLILGGGDGLALREVLKyETVLHVDLVDLDGSMIDMARNvpelvsLNKSAFFDNrVNTHVCDAKEFLSSPSSLYDV 215
Cdd:COG0500 26 KGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARA------RAAKAGLGN-VEFLVADLAELDPLPAESFDL 97
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 447046698 216 IIIDFpdpATELLSTLYTSELFARIATFLTEDGAFVCQSNSPA 258
Cdd:COG0500 98 VVAFG---VLHHLPPEEREALLRELARALKPGGVLLLSASDAA 137
|
|
| |
