|
Name |
Accession |
Description |
Interval |
E-value |
| AdoMet_MTases super family |
cl17173 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
180-362 |
3.28e-23 |
|
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.).
The actual alignment was detected with superfamily member pfam01564:
Pssm-ID: 473071 [Multi-domain] Cd Length: 183 Bit Score: 96.23 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 180 LIYTETLMCRGVENY-EGKEICILGGGDGALLYELLKENP-KHVVMLEIDELVMQTCNKYLNVICGDVLEKRkgdqYEII 257
Cdd:pfam01564 2 FIYHEMIAHVPLCSHpNPKKVLIIGGGDGGVLREVVKHPSvEKITLVDIDEKVIDFSKKFLPSLAIGFQDPR----VKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 258 VGDCVEYLKKFIAegrKFDYVFGDLTDiPITDAPEgetwDFIRTIFEHSFKVLKPDGKYLTHGNgsTCKVQLRLFEEQLN 337
Cdd:pfam01564 78 IGDGFKFLKDYLN---TFDVIIVDSTD-PVGPAEN----LFSKPFFDLLKKALKEDGVFITQAE--SPWLHLELIINILK 147
|
170 180
....*....|....*....|....*..
gi 665410288 338 LLRpKVKFTTTKAF--VPSFMEEWLFY 362
Cdd:pfam01564 148 NGK-QVFPVVMPYVatIPTYPSGGWGF 173
|
|
| Spermine_synt_N super family |
cl38572 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
137-170 |
3.70e-08 |
|
Spermidine synthase tetramerization domain; This domain represents the N-terminal tetramerization domain from spermidine synthase.
The actual alignment was detected with superfamily member pfam17284:
Pssm-ID: 407397 [Multi-domain] Cd Length: 53 Bit Score: 49.58 E-value: 3.70e-08
10 20 30
....*....|....*....|....*....|....
gi 665410288 137 IEYDIDKVVFEARSPFQKIQIMHSKTLGNMLLLD 170
Cdd:pfam17284 13 LEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLD 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
180-362 |
3.28e-23 |
|
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: 96.23 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 180 LIYTETLMCRGVENY-EGKEICILGGGDGALLYELLKENP-KHVVMLEIDELVMQTCNKYLNVICGDVLEKRkgdqYEII 257
Cdd:pfam01564 2 FIYHEMIAHVPLCSHpNPKKVLIIGGGDGGVLREVVKHPSvEKITLVDIDEKVIDFSKKFLPSLAIGFQDPR----VKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 258 VGDCVEYLKKFIAegrKFDYVFGDLTDiPITDAPEgetwDFIRTIFEHSFKVLKPDGKYLTHGNgsTCKVQLRLFEEQLN 337
Cdd:pfam01564 78 IGDGFKFLKDYLN---TFDVIIVDSTD-PVGPAEN----LFSKPFFDLLKKALKEDGVFITQAE--SPWLHLELIINILK 147
|
170 180
....*....|....*....|....*..
gi 665410288 338 LLRpKVKFTTTKAF--VPSFMEEWLFY 362
Cdd:pfam01564 148 NGK-QVFPVVMPYVatIPTYPSGGWGF 173
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
141-323 |
2.64e-21 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 93.30 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 141 IDKVVFEARSPFQKIQIMHSKTLGNMLLLDELQNIAESD-LIYTETL----MCrgvENYEGKEICILGGGDGALLYELLK 215
Cdd:PRK00811 20 VKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDeFIYHEMMthvpLF---AHPNPKRVLIIGGGDGGTLREVLK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 216 -ENPKHVVMLEIDELVMQTCNKYLNVICGDVLE-KRkgdqYEIIVGDCVEYLKKFIAegrKFDYVFGDLTDiPITDApEG 293
Cdd:PRK00811 97 hPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDdPR----VELVIGDGIKFVAETEN---SFDVIIVDSTD-PVGPA-EG 167
|
170 180 190
....*....|....*....|....*....|
gi 665410288 294 EtwdFIRTIFEHSFKVLKPDGKYLTHgNGS 323
Cdd:PRK00811 168 L---FTKEFYENCKRALKEDGIFVAQ-SGS 193
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
164-361 |
9.11e-19 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 84.11 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 164 GNMLLLD-ELQNIAESD-LIYTETLM-----CRGvenyEGKEICILGGGDGALLYELLKENP-KHVVMLEIDELVMQTCN 235
Cdd:COG0421 3 GRVLVLDgVVQSTMELDeFEYHEMMAhvpllFHP----NPKRVLIIGGGDGGLARELLKHPPvERVDVVEIDPEVVELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 236 KYLNVICGDVLEKRkgdqYEIIVGDCVEYLKKFiaeGRKFDYVFGDLTDiPITDAPEGETWDFirtiFEHSFKVLKPDGK 315
Cdd:COG0421 79 EYFPLLAPAFDDPR----LRVVIGDGRAFLREA---EESYDVIIVDLTD-PVGPAEGLFTREF----YEDCRRALKPGGV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665410288 316 YLThgNGSTCKVQLRLFEEQLNLLR---PKVKFTTtkAFVPSFMEEWLF 361
Cdd:COG0421 147 LVV--NLGSPFYGLDLLRRVLATLRevfPHVVLYA--APVPTYGGGNVF 191
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
202-319 |
5.02e-09 |
|
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: 53.59 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 202 LGGGDGALLYELLKENPKHVVMLEIDELVMQTCNKylnvicgdVLEKRKGDQYEIIVGDCVEYLKKfiaEGRKFDYVFGD 281
Cdd:cd02440 5 LGCGTGALALALASGPGARVTGVDISPVALELARK--------AAAALLADNVEVLKGDAEELPPE---ADESFDVIISD 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 665410288 282 LTDIPITDAPegetWDFIRTIFEhsfkVLKPDGKYLTH 319
Cdd:cd02440 74 PPLHHLVEDL----ARFLEEARR----LLKPGGVLVLT 103
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
137-170 |
3.70e-08 |
|
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: 49.58 E-value: 3.70e-08
10 20 30
....*....|....*....|....*....|....
gi 665410288 137 IEYDIDKVVFEARSPFQKIQIMHSKTLGNMLLLD 170
Cdd:pfam17284 13 LEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLD 46
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
180-362 |
3.28e-23 |
|
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: 96.23 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 180 LIYTETLMCRGVENY-EGKEICILGGGDGALLYELLKENP-KHVVMLEIDELVMQTCNKYLNVICGDVLEKRkgdqYEII 257
Cdd:pfam01564 2 FIYHEMIAHVPLCSHpNPKKVLIIGGGDGGVLREVVKHPSvEKITLVDIDEKVIDFSKKFLPSLAIGFQDPR----VKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 258 VGDCVEYLKKFIAegrKFDYVFGDLTDiPITDAPEgetwDFIRTIFEHSFKVLKPDGKYLTHGNgsTCKVQLRLFEEQLN 337
Cdd:pfam01564 78 IGDGFKFLKDYLN---TFDVIIVDSTD-PVGPAEN----LFSKPFFDLLKKALKEDGVFITQAE--SPWLHLELIINILK 147
|
170 180
....*....|....*....|....*..
gi 665410288 338 LLRpKVKFTTTKAF--VPSFMEEWLFY 362
Cdd:pfam01564 148 NGK-QVFPVVMPYVatIPTYPSGGWGF 173
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
141-323 |
2.64e-21 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 93.30 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 141 IDKVVFEARSPFQKIQIMHSKTLGNMLLLDELQNIAESD-LIYTETL----MCrgvENYEGKEICILGGGDGALLYELLK 215
Cdd:PRK00811 20 VKKVLYEEKSPFQRIEIFETPEFGRLLALDGCVMTTERDeFIYHEMMthvpLF---AHPNPKRVLIIGGGDGGTLREVLK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 216 -ENPKHVVMLEIDELVMQTCNKYLNVICGDVLE-KRkgdqYEIIVGDCVEYLKKFIAegrKFDYVFGDLTDiPITDApEG 293
Cdd:PRK00811 97 hPSVEKITLVEIDERVVEVCRKYLPEIAGGAYDdPR----VELVIGDGIKFVAETEN---SFDVIIVDSTD-PVGPA-EG 167
|
170 180 190
....*....|....*....|....*....|
gi 665410288 294 EtwdFIRTIFEHSFKVLKPDGKYLTHgNGS 323
Cdd:PRK00811 168 L---FTKEFYENCKRALKEDGIFVAQ-SGS 193
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
164-361 |
9.11e-19 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 84.11 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 164 GNMLLLD-ELQNIAESD-LIYTETLM-----CRGvenyEGKEICILGGGDGALLYELLKENP-KHVVMLEIDELVMQTCN 235
Cdd:COG0421 3 GRVLVLDgVVQSTMELDeFEYHEMMAhvpllFHP----NPKRVLIIGGGDGGLARELLKHPPvERVDVVEIDPEVVELAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 236 KYLNVICGDVLEKRkgdqYEIIVGDCVEYLKKFiaeGRKFDYVFGDLTDiPITDAPEGETWDFirtiFEHSFKVLKPDGK 315
Cdd:COG0421 79 EYFPLLAPAFDDPR----LRVVIGDGRAFLREA---EESYDVIIVDLTD-PVGPAEGLFTREF----YEDCRRALKPGGV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665410288 316 YLThgNGSTCKVQLRLFEEQLNLLR---PKVKFTTtkAFVPSFMEEWLF 361
Cdd:COG0421 147 LVV--NLGSPFYGLDLLRRVLATLRevfPHVVLYA--APVPTYGGGNVF 191
|
|
| PLN02823 |
PLN02823 |
spermine synthase |
139-359 |
1.27e-17 |
|
spermine synthase
Pssm-ID: 178418 [Multi-domain] Cd Length: 336 Bit Score: 83.58 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 139 YDIDKVVFEARSPFQKIQIMHSKTLGNMLLLDELQNIAESD-LIYTETLMCRGVENY-EGKEICILGGGDGALLYELLKE 216
Cdd:PLN02823 45 YAVNSVLHTGTSEFQDIALVDTKPFGKVLIIDGKMQSAEADeFVYHESLVHPALLHHpNPKTVFIMGGGEGSTAREVLRH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 217 NP-KHVVMLEIDELVMQTCNKYLNVICGDVLEKRkgdqYEIIVGDCVEYLKKfiaEGRKFDYVFGDLTDiPITDAP--EG 293
Cdd:PLN02823 125 KTvEKVVMCDIDQEVVDFCRKHLTVNREAFCDKR----LELIINDARAELEK---RDEKFDVIIGDLAD-PVEGGPcyQL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 294 ETWDFirtiFEHSFKV-LKPDGKYLTHGNGSTCKVQLRLFEEQLNLLR---PKVKFTTtkAFVPSFMEEW 359
Cdd:PLN02823 197 YTKSF----YERIVKPkLNPGGIFVTQAGPAGILTHKEVFSSIYNTLRqvfKYVVPYT--AHVPSFADTW 260
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
139-314 |
2.98e-15 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 76.22 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 139 YDIDKVVFEARSPFQKIQIMHSKTLGNMLLLDELQNIAESD-LIYTETL----MCrGVENyeGKEICILGGGDGALLYEL 213
Cdd:PLN02366 33 LKVEKVLFQGKSDFQDVLVFESATYGKVLVLDGVIQLTERDeCAYQEMIthlpLC-SIPN--PKKVLVVGGGDGGVLREI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 214 LK-ENPKHVVMLEIDELVMQTCNKYL-NVICGdvlekRKGDQYEIIVGDCVEYLKKfIAEGrKFDYVFGDLTDiPITDAP 291
Cdd:PLN02366 110 ARhSSVEQIDICEIDKMVIDVSKKFFpDLAVG-----FDDPRVNLHIGDGVEFLKN-APEG-TYDAIIVDSSD-PVGPAQ 181
|
170 180
....*....|....*....|...
gi 665410288 292 EgetwDFIRTIFEHSFKVLKPDG 314
Cdd:PLN02366 182 E----LFEKPFFESVARALRPGG 200
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
202-319 |
5.02e-09 |
|
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: 53.59 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 202 LGGGDGALLYELLKENPKHVVMLEIDELVMQTCNKylnvicgdVLEKRKGDQYEIIVGDCVEYLKKfiaEGRKFDYVFGD 281
Cdd:cd02440 5 LGCGTGALALALASGPGARVTGVDISPVALELARK--------AAAALLADNVEVLKGDAEELPPE---ADESFDVIISD 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 665410288 282 LTDIPITDAPegetWDFIRTIFEhsfkVLKPDGKYLTH 319
Cdd:cd02440 74 PPLHHLVEDL----ARFLEEARR----LLKPGGVLVLT 103
|
|
| Spermine_synt_N |
pfam17284 |
Spermidine synthase tetramerization domain; This domain represents the N-terminal ... |
137-170 |
3.70e-08 |
|
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: 49.58 E-value: 3.70e-08
10 20 30
....*....|....*....|....*....|....
gi 665410288 137 IEYDIDKVVFEARSPFQKIQIMHSKTLGNMLLLD 170
Cdd:pfam17284 13 LEYKVEKVLYDEKSEYQDIEIFESKTFGNVLVLD 46
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
142-314 |
1.09e-07 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 53.72 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 142 DKVVFEARSPFQKIQIMHSKTLGNMLLLDELQNIAESDLIYTETL----MCRgveNYEGKEICILGGGDGALLYELLKEN 217
Cdd:COG4262 232 DPVVYSEQTPYQRIVVTRDKDDRRLYLNGNLQFSSLDEYRYHEALvhppMAA---HPRPRRVLVLGGGDGLAAREVLKYP 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 218 P-KHVVMLEIDELVMQTC--NKYLNVICGDVLEKRKgdqYEIIVGDCVEYLKKfiaEGRKFDYVFGDLTDiPITDAPeGE 294
Cdd:COG4262 309 DvESVTLVDLDPEVTDLAktNPFLRELNGGALNDPR---VTVVNADAFQFLRE---TDEKYDVIIVDLPD-PSNFSL-GK 380
|
170 180
....*....|....*....|..
gi 665410288 295 --TWDFIRTIFEHsfkvLKPDG 314
Cdd:COG4262 381 lySVEFYRLVRRH----LAPGG 398
|
|
| RlmK |
COG1092 |
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
252-336 |
8.46e-06 |
|
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 47.87 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 252 DQYEIIVGDCVEYLKKFIAEGRKFDYVFGDltdiPITDAP-EGETWDFIR---TIFEHSFKVLKPDGKYLThgngSTC-- 325
Cdd:COG1092 266 DRHEFVQADAFDWLRELAREGERFDLIILD----PPAFAKsKKDLFDAQRdykDLNRLALKLLAPGGILVT----SSCsr 337
|
90
....*....|.
gi 665410288 326 KVQLRLFEEQL 336
Cdd:COG1092 338 HFSLDLFLEIL 348
|
|
| PRK03612 |
PRK03612 |
polyamine aminopropyltransferase; |
142-284 |
9.63e-06 |
|
polyamine aminopropyltransferase;
Pssm-ID: 235139 [Multi-domain] Cd Length: 521 Bit Score: 47.91 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 142 DKVVFEARSPFQKIQIMHSK-TLGNM--LLLD-ELQnIAESD-LIYTETL----McRGVENYEgkEICILGGGDGALLYE 212
Cdd:PRK03612 239 DPVVYAEQTPYQRIVVTRRGnGRGPDlrLYLNgRLQ-FSSRDeYRYHEALvhpaM-AASARPR--RVLVLGGGDGLALRE 314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665410288 213 LLKENP-KHVVMLEIDELVMQTCNKY-----LNvicGDVLEKRKgdqYEIIVGDCVEYLKKFIAegrKFDYVFGDLTD 284
Cdd:PRK03612 315 VLKYPDvEQVTLVDLDPAMTELARTSpalraLN---GGALDDPR---VTVVNDDAFNWLRKLAE---KFDVIIVDLPD 383
|
|
| speE |
PRK01581 |
polyamine aminopropyltransferase; |
144-362 |
6.14e-05 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234961 [Multi-domain] Cd Length: 374 Bit Score: 44.96 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 144 VVFEARSPFQKIQIMHSKTLgNMLLLDELQNIAESDLIYTETL----MCRGVENyegKEICILGGGDGALLYELLK-ENP 218
Cdd:PRK01581 99 NLFAEKSNYQNINLLQVSDI-RLYLDKQLQFSSVDEQIYHEALvhpiMSKVIDP---KRVLILGGGDGLALREVLKyETV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 219 KHVVMLEIDELVMqtcNKYLNVICGDVLEKRK--GDQYEIIVGDCVEYLKKFIAegrkfdyvfgdLTDIPITDAPEGETw 296
Cdd:PRK01581 175 LHVDLVDLDGSMI---NMARNVPELVSLNKSAffDNRVNVHVCDAKEFLSSPSS-----------LYDVIIIDFPDPAT- 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665410288 297 DFIRTIFEHSF-----KVLKPDGKYLTHGNgSTCKVQLRLFEEQLNLLRPKVKFTTTKAFVPSFMEEWLFY 362
Cdd:PRK01581 240 ELLSTLYTSELfariaTFLTEDGAFVCQSN-SPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFH 309
|
|
| YhdJ |
COG0863 |
DNA modification methylase [Replication, recombination and repair]; |
256-314 |
2.41e-03 |
|
DNA modification methylase [Replication, recombination and repair];
Pssm-ID: 440623 Cd Length: 236 Bit Score: 39.52 E-value: 2.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665410288 256 IIVGDCVEYLKKFiaEGRKFDYVFgdlTDIP-------------ITDAPEGETW-DFIRTIFEHSFKVLKPDG 314
Cdd:COG0863 2 LICGDCLEVLKEL--PDESVDLIV---TDPPynlgkkyglgrreIGNELSFEEYlEFLREWLAECYRVLKPGG 69
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
202-314 |
3.88e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 36.77 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665410288 202 LGGGDGALLYELLKENPKHVVMLEIDELVMQTCNKYLnvicgdvleKRKGDQYEIIVGDcveyLKKFIAEGRKFDYVF-- 279
Cdd:pfam13649 4 LGCGTGRLTLALARRGGARVTGVDLSPEMLERARERA---------AEAGLNVEFVQGD----AEDLPFPDGSFDLVVss 70
|
90 100 110
....*....|....*....|....*....|....*
gi 665410288 280 GDLTDIPITDapegetwdfIRTIFEHSFKVLKPDG 314
Cdd:pfam13649 71 GVLHHLPDPD---------LEAALREIARVLKPGG 96
|
|
| |
