|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02823 |
PLN02823 |
spermine synthase |
1-331 |
0e+00 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 637.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 1 MFGNGFPEIHKATSPTQTLHSNQQDCHWYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAER 80
Cdd:PLN02823 5 VHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 81 DEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIK 160
Cdd:PLN02823 85 DEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 161 DAKAELEKREEKFDIIVGDLADPVEGGPCYQLYTKSFYQNILKPKLSPNGIFVTQAGPAGIFTHKEVFTSIYNTMKQVFK 240
Cdd:PLN02823 165 DARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 241 YVKAYTAHVPSFADTWGWVMASDHEF-DVEVDEMDRRIEERVNGELMYLNAPSFVSAATLNKTISLALEKETEVYSEENA 319
Cdd:PLN02823 245 YVVPYTAHVPSFADTWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
|
330
....*....|..
gi 145334519 320 RFIHGHGVAYRH 331
Cdd:PLN02823 325 RFIHGHGTAAKA 336
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
28-289 |
1.34e-76 |
|
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: 236.17 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegG 187
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 188 PCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASDHEF 266
Cdd:TIGR00417 159 PAETLFTKEFYEL-LKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235
|
250 260
....*....|....*....|....*
gi 145334519 267 D-VEVDemDRRI-EERVNGELMYLN 289
Cdd:TIGR00417 236 RpLEVE--IRRIkFEAEDGKTKYYN 258
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
66-261 |
1.26e-73 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 225.48 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 66 GKVLVIDGKMQSA-ERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLT 144
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 145 VNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNIlKPKLSPNGIFVTQAGpaGIFTH 224
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYEDC-RRALKPGGVLVVNLG--SPFYG 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334519 225 KEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMA 261
Cdd:COG0421 158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
82-267 |
1.14e-50 |
|
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: 166.34 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 82 EFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKD 161
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 162 AKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKY 241
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155
|
170 180
....*....|....*....|....*..
gi 145334519 242 VKAYTAHVPSFAD-TWGWVMASDHEFD 267
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPLK 182
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
107-215 |
7.57e-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: 44.34 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 107 GGGEGSAAREILKHTtIEKVVMCDIDQEVVDFCRRfltvNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLAdpveg 186
Cdd:cd02440 6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75
|
90 100
....*....|....*....|....*....
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQ 215
Cdd:cd02440 76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
92-250 |
8.48e-04 |
|
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: 40.98 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 92 PALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFcnkklELVIKDAKAELEKR-E 170
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWFDPASA-----TVLHEDARRALRRRpE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 171 EKFDIIVGD----LADPveggpcYQLYTKSFYQnILKPKLSPNGIFVTQAgpagI--FTHKEVFTSIYNTMKQVFKYVKA 244
Cdd:NF037959 343 ERFDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVVEV 411
|
....*.
gi 145334519 245 YTAHVP 250
Cdd:NF037959 412 WTEARP 417
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02823 |
PLN02823 |
spermine synthase |
1-331 |
0e+00 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 637.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 1 MFGNGFPEIHKATSPTQTLHSNQQDCHWYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAER 80
Cdd:PLN02823 5 VHGNGTSHITAVATPTAALASNYAKSLWYEEEIEDDLRWSYAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 81 DEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIK 160
Cdd:PLN02823 85 DEFVYHESLVHPALLHHPNPKTVFIMGGGEGSTAREVLRHKTVEKVVMCDIDQEVVDFCRKHLTVNREAFCDKRLELIIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 161 DAKAELEKREEKFDIIVGDLADPVEGGPCYQLYTKSFYQNILKPKLSPNGIFVTQAGPAGIFTHKEVFTSIYNTMKQVFK 240
Cdd:PLN02823 165 DARAELEKRDEKFDVIIGDLADPVEGGPCYQLYTKSFYERIVKPKLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRQVFK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 241 YVKAYTAHVPSFADTWGWVMASDHEF-DVEVDEMDRRIEERVNGELMYLNAPSFVSAATLNKTISLALEKETEVYSEENA 319
Cdd:PLN02823 245 YVVPYTAHVPSFADTWGWVMASDHPFaDLSAEELDSRIKERIDGELKYLDGETFSSAFALNKTVRQALANETHVYTEENA 324
|
330
....*....|..
gi 145334519 320 RFIHGHGVAYRH 331
Cdd:PLN02823 325 RFIHGHGTAAKA 336
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
28-290 |
1.15e-90 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 272.41 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:PRK00811 5 WFTETLTDNYGQSFRVKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDEFIYHEMMTHVPLFAHPNPKRVLIIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFL-TVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVeg 186
Cdd:PRK00811 85 GGDGGTLREVLKHPSVEKITLVEIDERVVEVCRKYLpEIAGGAYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDPV-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQAG-PagiFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASD- 263
Cdd:PRK00811 163 GPAEGLFTKEFYENCKR-ALKEDGIFVAQSGsP---FYQADEIKDMHRKLKEVFPIVRPYQAAIPTYpSGLWSFTFASKn 238
|
250 260
....*....|....*....|....*...
gi 145334519 264 HEFD-VEVDEMDRRIEERvNGELMYLNA 290
Cdd:PRK00811 239 DDLKfLPLDVIEARFAER-GIKTRYYNP 265
|
|
| speE |
TIGR00417 |
spermidine synthase; the SpeE subunit of spermidine synthase catalysesthe reaction (putrescine ... |
28-289 |
1.34e-76 |
|
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: 236.17 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMG 107
Cdd:TIGR00417 1 WFTEYHDKNFGLTMKVDKVLYHEKSEFQDLEIFETEAFGNVLVLDGVVQTTERDEFIYHEMITHVPLFTHPNPKHVLVIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 108 GGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegG 187
Cdd:TIGR00417 81 GGDGGVLREVLKHKSVESATLVDIDEKVIELSRKYLPNLAGSYDDPRVKLVIDDGFKFLADTENTFDVIIVDSTDPV--G 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 188 PCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSF-ADTWGWVMASDHEF 266
Cdd:TIGR00417 159 PAETLFTKEFYEL-LKKALNPDGIFVAQSE--SPWLQLELIIDLKRKLKEAFPITEYYTAAIPTYpSGLWTFTIASKNKY 235
|
250 260
....*....|....*....|....*
gi 145334519 267 D-VEVDemDRRI-EERVNGELMYLN 289
Cdd:TIGR00417 236 RpLEVE--IRRIkFEAEDGKTKYYN 258
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
66-261 |
1.26e-73 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 225.48 E-value: 1.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 66 GKVLVIDGKMQSA-ERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLT 144
Cdd:COG0421 3 GRVLVLDGVVQSTmELDEFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 145 VNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNIlKPKLSPNGIFVTQAGpaGIFTH 224
Cdd:COG0421 83 LLAPAFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPV--GPAEGLFTREFYEDC-RRALKPGGVLVVNLG--SPFYG 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334519 225 KEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMA 261
Cdd:COG0421 158 LDLLRRVLATLREVFPHVVLYAAPVPTYGGGNVFLLA 194
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
46-261 |
2.09e-56 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 190.82 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 46 VLHQGTSEYQDIALLDTKR-FGKV--LVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTT 122
Cdd:PRK03612 241 VVYAEQTPYQRIVVTRRGNgRGPDlrLYLNGRLQFSSRDEYRYHEALVHPAMAASARPRRVLVLGGGDGLALREVLKYPD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 123 IEKVVMCDIDQEVVDFCR---RFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADP--VEGGpcyQLYTKSF 197
Cdd:PRK03612 321 VEQVTLVDLDPAMTELARtspALRALNGGALDDPRVTVVNDDAFNWLRKLAEKFDVIIVDLPDPsnPALG---KLYSVEF 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334519 198 YqNILKPKLSPNGIFVTQAGPAgiFTHKEVFTSIYNTMKQVFKYVKAYTAHVPSFADtWGWVMA 261
Cdd:PRK03612 398 Y-RLLKRRLAPDGLLVVQSTSP--YFAPKAFWSIEATLEAAGLATTPYHVNVPSFGE-WGFVLA 457
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
46-239 |
6.37e-53 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 179.68 E-value: 6.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 46 VLHQGTSEYQDIALLDTKRFgKVLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEK 125
Cdd:COG4262 234 VVYSEQTPYQRIVVTRDKDD-RRLYLNGNLQFSSLDEYRYHEALVHPPMAAHPRPRRVLVLGGGDGLAAREVLKYPDVES 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 126 VVMCDIDQEVVDFCRR---FLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVEGGPcYQLYTKSFYQnIL 202
Cdd:COG4262 313 VTLVDLDPEVTDLAKTnpfLRELNGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLPDPSNFSL-GKLYSVEFYR-LV 390
|
170 180 190
....*....|....*....|....*....|....*..
gi 145334519 203 KPKLSPNGIFVTQAGPAgiFTHKEVFTSIYNTMKQVF 239
Cdd:COG4262 391 RRHLAPGGVLVVQATSP--YFAPKAFWCIAKTLEAAG 425
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
82-267 |
1.14e-50 |
|
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: 166.34 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 82 EFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKD 161
Cdd:pfam01564 1 EFIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKFLPSLAIGFQDPRVKVVIGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 162 AKAELEKREEKFDIIVGDLADPVegGPCYQLYTKSFYQNiLKPKLSPNGIFVTQAGpaGIFTHKEVFTSIYNTMKQVFKY 241
Cdd:pfam01564 81 GFKFLKDYLNTFDVIIVDSTDPV--GPAENLFSKPFFDL-LKKALKEDGVFITQAE--SPWLHLELIINILKNGKQVFPV 155
|
170 180
....*....|....*....|....*..
gi 145334519 242 VKAYTAHVPSFAD-TWGWVMASDHEFD 267
Cdd:pfam01564 156 VMPYVATIPTYPSgGWGFTVCSKNPLK 182
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
21-297 |
1.13e-48 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 165.20 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 21 SNQQDCH------WYEETiddDLKW-----SFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAERDEFIYHECL 89
Cdd:PLN02366 5 ESEAKCHstvipgWFSEI---SPMWpgeahSLKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDECAYQEMI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 90 IHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFCNKKLELVIKDAKAELEK- 168
Cdd:PLN02366 82 THLPLCSIPNPKKVLVVGGGDGGVLREIARHSSVEQIDICEIDKMVIDVSKKFFPDLAVGFDDPRVNLHIGDGVEFLKNa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 169 REEKFDIIVGDLADPVegGPCYQLYTKSFYQNILKpKLSPNGIFVTQAgpAGIFTHKEVFTSIYNTMKQVFK----YvkA 244
Cdd:PLN02366 162 PEGTYDAIIVDSSDPV--GPAQELFEKPFFESVAR-ALRPGGVVCTQA--ESMWLHMDLIEDLIAICRETFKgsvnY--A 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334519 245 YTAhVPSF-ADTWGWVMASDHEFDVEVDEMDRRIEE-----RVNGELMYLNA---------PSFVSAA 297
Cdd:PLN02366 235 WTT-VPTYpSGVIGFVLCSKEGPAVDFKHPVNPIDKlegagKAKRPLKFYNSevhraafclPSFAKRE 301
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
44-263 |
3.09e-34 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 128.93 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 44 NSVLHQgTSEYQDIALLDTKRFGkvLVIDGKMQSAERDEFIYHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTI 123
Cdd:PRK01581 98 TNLFAE-KSNYQNINLLQVSDIR--LYLDKQLQFSSVDEQIYHEALVHPIMSKVIDPKRVLILGGGDGLALREVLKYETV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 124 EKVVMCDIDQEVVDFCR---RFLTVNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLADPVEgGPCYQLYTKSFYQN 200
Cdd:PRK01581 175 LHVDLVDLDGSMINMARnvpELVSLNKSAFFDNRVNVHVCDAKEFLSSPSSLYDVIIIDFPDPAT-ELLSTLYTSELFAR 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334519 201 ILKpKLSPNGIFVTQA-GPAGIfthKEVFTSIYNTMKQVFKYVKAYTAHVPSFADTWGWVMASD 263
Cdd:PRK01581 254 IAT-FLTEDGAFVCQSnSPADA---PLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHIAAN 313
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
28-79 |
4.57e-11 |
|
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: 57.29 E-value: 4.57e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 145334519 28 WYEETIDDDLKWSFALNSVLHQGTSEYQDIALLDTKRFGKVLVIDGKMQSAE 79
Cdd:pfam17284 2 WFTEIHDLGQALEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLDGVVQLTE 53
|
|
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
94-214 |
1.30e-08 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 55.05 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 94 LLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDafcNKKLELVIKDAKAELEKREEKF 173
Cdd:PRK04457 61 LLFNPRPQHILQIGLGGGSLAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPEN---GERFEVIEADGAEYIAVHRHST 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 145334519 174 DIIVGDLADpvEGGPCYQLYTKSFYQNIlKPKLSPNGIFVT 214
Cdd:PRK04457 138 DVILVDGFD--GEGIIDALCTQPFFDDC-RNALSSDGIFVV 175
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
107-215 |
7.57e-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: 44.34 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 107 GGGEGSAAREILKHTtIEKVVMCDIDQEVVDFCRRfltvNSDAFCNKKLELVIKDAKAELEKREEKFDIIVGDLAdpveg 186
Cdd:cd02440 6 GCGTGALALALASGP-GARVTGVDISPVALELARK----AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP----- 75
|
90 100
....*....|....*....|....*....
gi 145334519 187 GPCYQLYTKSFYQNILKpKLSPNGIFVTQ 215
Cdd:cd02440 76 LHHLVEDLARFLEEARR-LLKPGGVLVLT 103
|
|
| TRM1 |
COG1867 |
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ... |
125-183 |
2.15e-04 |
|
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 441472 Cd Length: 383 Bit Score: 42.55 E-value: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 145334519 125 KVVMCDIDQEVVDFCRRFLTVNSDAFCnkklELVIKDAKAELEKREEKFDIIvgDLaDP 183
Cdd:COG1867 82 KVTLNDIDPEAVELIRENLELNGLEDV----EVYNRDANALLHELGRRFDVV--DL-DP 133
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
92-250 |
8.48e-04 |
|
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: 40.98 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 92 PALLFHPNPKTVFIMGGGEGSAAREILKHTTIEKVVMCDIDQEVVDFCRRFLTVNSDAFcnkklELVIKDAKAELEKR-E 170
Cdd:NF037959 268 ARLRMGRADFSAFFIGGGAYTLPRAWAARRPAGRITVAEIDPAVTRVAAEDFWFDPASA-----TVLHEDARRALRRRpE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 171 EKFDIIVGD----LADPveggpcYQLYTKSFYQnILKPKLSPNGIFVTQAgpagI--FTHKEVFTSIYNTMKQVFKYVKA 244
Cdd:NF037959 343 ERFDVIVGDaftdIAVP------AHLVTREFFE-LVRARLTPDGVYLMNV----IdhADRLRALAALVATLREVFPVVEV 411
|
....*.
gi 145334519 245 YTAHVP 250
Cdd:NF037959 412 WTEARP 417
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
107-177 |
4.71e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 36.00 E-value: 4.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334519 107 GGGEGSAAREILKHTTIEkVVMCDIDQEVVDFCRRFLtvnsdAFCNKKLELVIKDAkAELEKREEKFDIIV 177
Cdd:pfam13649 5 GCGTGRLTLALARRGGAR-VTGVDLSPEMLERARERA-----AEAGLNVEFVQGDA-EDLPFPDGSFDLVV 68
|
|
| PIN_FAM120B-like |
cd18672 |
FEN-like PIN domains of FAM120B (family with sequence similarity 120B) and related proteins; ... |
68-141 |
4.72e-03 |
|
FEN-like PIN domains of FAM120B (family with sequence similarity 120B) and related proteins; FAM120B (also known as CCPG, "constitutive coactivator of PPAR-gamma", PGCC1, "PPARgamma constitutive coactivator 1") is a constitutive coactivator of peroxisome proliferator-activated receptor (PPARgamma) that promotes adipogenesis in a PPARgamma-dependent manner. This subfamily belongs to the structure-specific, 5' nuclease family (FEN-like) that catalyzes hydrolysis of DNA duplex-containing nucleic acid structures during DNA replication, repair, and recombination. Canonical members of the FEN-like family possess a PIN domain with a two-helical structure insert (also known as the helical arch, helical clamp or I domain) of variable length (approximately 16 to 800 residues), the helical arch/clamp region is involved in DNA binding. The PIN domain belongs to a large nuclease superfamily. The structural properties of the PIN domain indicate its putative active center, consisting of invariant acidic amino acid residues (putative metal-binding residues), is geometrically similar in the active center of structure-specific 5' nucleases, PIN-domain ribonucleases of eukaryotic rRNA editing proteins, and bacterial toxins of toxin-antitoxin (TA) operons.
Pssm-ID: 350239 [Multi-domain] Cd Length: 210 Bit Score: 37.66 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334519 68 VLVIDGKMQSAERDEFI---------YHECLIHPALLFHPNPKTVFIMGGGEGSAAREILKHTTIEkvVMC---DIDQEV 135
Cdd:cd18672 83 VFFFDGVVESQKRDEWVkrrlknnkkVSKVFNHIKKKGTQPPKNLFFLPSGLATFTRFALRSLGVE--VICsmdEADQEV 160
|
....*.
gi 145334519 136 VDFCRR 141
Cdd:cd18672 161 ASYCRQ 166
|
|
|