|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
1-263 |
2.16e-161 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 447.95 E-value: 2.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 1 MARHPYRRLRPAKSGFPEVGISEEGNIRSLHLGSDTVQSSMNLDHPSELVLSYSRAMMGWLLFTDAlPQHITQIGLGGGS 80
Cdd:PRK04457 1 MARHPYRRLRPAKAGFPEVGVSEEGGVRSLHLGSDTVQSSMRIDDPSELELAYTRAMMGFLLFNPR-PQHILQIGLGGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 81 FARWIDTYLPDTRQTAVDINPQVIAIARNLFELPFEGEKFEIIEADGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPF 160
Cdd:PRK04457 80 LAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 161 FRDCRNALSSDGIFVTNWWSGDKRYQRFIERLLSVFEGRVLELPAESHGNVAVMAFQSSPKEQNIDKLKKRADKLSNAYG 240
Cdd:PRK04457 160 FDDCRNALSSDGIFVVNLWSRDKRYDRYLERLESSFEGRVLELPAESHGNVAVFAFKSAPKELRWDKLRKRAKKLENEHG 239
|
250 260
....*....|....*....|...
gi 1523361231 241 LDFHRMLAGLKASNPNNGKHFHL 263
Cdd:PRK04457 240 LDFHRFVAKLKASNPNTGKRLLL 262
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
28-216 |
6.55e-55 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 175.40 E-value: 6.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 28 RSLHLGSDtVQSSMNLDhpselVLSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIA 107
Cdd:COG0421 4 RVLVLDGV-VQSTMELD-----EFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 108 RNLFELP---FEGEKFEIIEADGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVTNWWSGD-- 182
Cdd:COG0421 78 REYFPLLapaFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFyg 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1523361231 183 -KRYQRFIERLLSVFEGRVL---ELPAESHGNVAVMAF 216
Cdd:COG0421 158 lDLLRRVLATLREVFPHVVLyaaPVPTYGGGNVFLLAL 195
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
51-176 |
2.44e-11 |
|
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: 60.80 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 51 LSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARNLfeLP-----FEGEKFEIIEA 125
Cdd:pfam01564 2 FIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKF--LPslaigFQDPRVKVVIG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1523361231 126 DGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 176
Cdd:pfam01564 80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFIT 130
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
69-175 |
2.80e-06 |
|
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 47.35 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 69 QHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIAR-----------------NLFElPFEGEKFEII-------- 123
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEenaeknqlehrvefiqsNLFE-PLAGQKIDIIvsnppyid 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1523361231 124 EADGAEYIKVFRHNTDIILVDGFDGEQIIdalveEPFFRDCRNALSSDGIFV 175
Cdd:TIGR00536 195 EEDLADLPNVVRFEPLLALVGGDDGLNIL-----RQIIELAPDYLKPNGFLV 241
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
27-177 |
2.08e-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: 42.14 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 27 IRSLHLGSDTVQSS--MNLDH----------PSELVLSYSrAMMgwllftDALPQ-----------HItqiglGGGSFA- 82
Cdd:NF037959 222 IRVVDVSADPGGPArlMVLDHlahginarddPTVLFTPYA-AML------DELARlrmgradfsafFI-----GGGAYTl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 83 --RWIDTYlPDTRQTAVDINPQVIAIARNLFElpFEGEKFEIIEADG---------AEYikvfrhntDIILVDGFDGEQI 151
Cdd:NF037959 290 prAWAARR-PAGRITVAEIDPAVTRVAAEDFW--FDPASATVLHEDArralrrrpeERF--------DVIVGDAFTDIAV 358
|
170 180
....*....|....*....|....*.
gi 1523361231 152 IDALVEEPFFRDCRNALSSDGIFVTN 177
Cdd:NF037959 359 PAHLVTREFFELVRARLTPDGVYLMN 384
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
74-176 |
5.82e-03 |
|
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: 35.48 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 74 IGLGGGSFARWIDTYlPDTRQTAVDINPQVIAIARNlFELPFEGEKFEIIEADGAEYIKVFRHNTDIILVDGFdgeqiID 153
Cdd:cd02440 5 LGCGTGALALALASG-PGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP-----LH 77
|
90 100
....*....|....*....|....*
gi 1523361231 154 ALVEEP--FFRDCRNALSSDGIFVT 176
Cdd:cd02440 78 HLVEDLarFLEEARRLLKPGGVLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
1-263 |
2.16e-161 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 447.95 E-value: 2.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 1 MARHPYRRLRPAKSGFPEVGISEEGNIRSLHLGSDTVQSSMNLDHPSELVLSYSRAMMGWLLFTDAlPQHITQIGLGGGS 80
Cdd:PRK04457 1 MARHPYRRLRPAKAGFPEVGVSEEGGVRSLHLGSDTVQSSMRIDDPSELELAYTRAMMGFLLFNPR-PQHILQIGLGGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 81 FARWIDTYLPDTRQTAVDINPQVIAIARNLFELPFEGEKFEIIEADGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPF 160
Cdd:PRK04457 80 LAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 161 FRDCRNALSSDGIFVTNWWSGDKRYQRFIERLLSVFEGRVLELPAESHGNVAVMAFQSSPKEQNIDKLKKRADKLSNAYG 240
Cdd:PRK04457 160 FDDCRNALSSDGIFVVNLWSRDKRYDRYLERLESSFEGRVLELPAESHGNVAVFAFKSAPKELRWDKLRKRAKKLENEHG 239
|
250 260
....*....|....*....|...
gi 1523361231 241 LDFHRMLAGLKASNPNNGKHFHL 263
Cdd:PRK04457 240 LDFHRFVAKLKASNPNTGKRLLL 262
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
28-216 |
6.55e-55 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 175.40 E-value: 6.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 28 RSLHLGSDtVQSSMNLDhpselVLSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIA 107
Cdd:COG0421 4 RVLVLDGV-VQSTMELD-----EFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 108 RNLFELP---FEGEKFEIIEADGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVTNWWSGD-- 182
Cdd:COG0421 78 REYFPLLapaFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFyg 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1523361231 183 -KRYQRFIERLLSVFEGRVL---ELPAESHGNVAVMAF 216
Cdd:COG0421 158 lDLLRRVLATLREVFPHVVLyaaPVPTYGGGNVFLLAL 195
|
|
| Spermine_synth |
pfam01564 |
Spermine/spermidine synthase domain; Spermine and spermidine are polyamines. This family ... |
51-176 |
2.44e-11 |
|
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: 60.80 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 51 LSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARNLfeLP-----FEGEKFEIIEA 125
Cdd:pfam01564 2 FIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKF--LPslaigFQDPRVKVVIG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1523361231 126 DGAEYIKVFRHNTDIILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 176
Cdd:pfam01564 80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFIT 130
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
74-177 |
8.81e-09 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 55.26 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 74 IGLGGGSFARWIDTYlPDTRQ-TAVDINPQVIAIARNLFELP------FEGEKFEIIEADGAEYIKVFRHNTDIILVDGF 146
Cdd:COG4262 293 LGGGDGLAAREVLKY-PDVESvTLVDLDPEVTDLAKTNPFLRelnggaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLP 371
|
90 100 110
....*....|....*....|....*....|..
gi 1523361231 147 DGEQIIDA-LVEEPFFRDCRNALSSDGIFVTN 177
Cdd:COG4262 372 DPSNFSLGkLYSVEFYRLVRRHLAPGGVLVVQ 403
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
97-176 |
4.18e-08 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 52.85 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 97 VDINPQVIAIARNLFelP------FEGEKFEIIEADGAEYIKVFRHNTDIILVDGFD----GEqiidALVEEPFFRDCRN 166
Cdd:PRK00811 106 VEIDERVVEVCRKYL--PeiaggaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDpvgpAE----GLFTKEFYENCKR 179
|
90
....*....|
gi 1523361231 167 ALSSDGIFVT 176
Cdd:PRK00811 180 ALKEDGIFVA 189
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
68-175 |
2.77e-06 |
|
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: 46.33 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 68 PQHITQIGLGGGSFARWIDTYLPDTRQ-TAVDINPQVIAIARNLFELPFEGEKFEIIEADGAEYIKVFRHNT-DIILVDG 145
Cdd:COG4122 17 AKRILEIGTGTGYSTLWLARALPDDGRlTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADGPfDLVFIDA 96
|
90 100 110
....*....|....*....|....*....|
gi 1523361231 146 fDGEQIIDalveepFFRDCRNALSSDGIFV 175
Cdd:COG4122 97 -DKSNYPD------YLELALPLLRPGGLIV 119
|
|
| hemK_fam |
TIGR00536 |
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
69-175 |
2.80e-06 |
|
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]
Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 47.35 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 69 QHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIAR-----------------NLFElPFEGEKFEII-------- 123
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEenaeknqlehrvefiqsNLFE-PLAGQKIDIIvsnppyid 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1523361231 124 EADGAEYIKVFRHNTDIILVDGFDGEQIIdalveEPFFRDCRNALSSDGIFV 175
Cdd:TIGR00536 195 EEDLADLPNVVRFEPLLALVGGDDGLNIL-----RQIIELAPDYLKPNGFLV 241
|
|
| MFS_SpdSyn |
NF037959 |
fused MFS/spermidine synthase; Proteins of this family are fusion of a N-terminal MFS (Major ... |
27-177 |
2.08e-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: 42.14 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 27 IRSLHLGSDTVQSS--MNLDH----------PSELVLSYSrAMMgwllftDALPQ-----------HItqiglGGGSFA- 82
Cdd:NF037959 222 IRVVDVSADPGGPArlMVLDHlahginarddPTVLFTPYA-AML------DELARlrmgradfsafFI-----GGGAYTl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 83 --RWIDTYlPDTRQTAVDINPQVIAIARNLFElpFEGEKFEIIEADG---------AEYikvfrhntDIILVDGFDGEQI 151
Cdd:NF037959 290 prAWAARR-PAGRITVAEIDPAVTRVAAEDFW--FDPASATVLHEDArralrrrpeERF--------DVIVGDAFTDIAV 358
|
170 180
....*....|....*....|....*.
gi 1523361231 152 IDALVEEPFFRDCRNALSSDGIFVTN 177
Cdd:NF037959 359 PAHLVTREFFELVRARLTPDGVYLMN 384
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
68-176 |
3.26e-04 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 41.17 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 68 PQHITQIGLGGGSFARWIdtylpdTRQTAVD------INPQVIAIARNLF---ELPFEGEKFEIIEADGAEYIK-VFRHN 137
Cdd:PLN02366 92 PKKVLVVGGGDGGVLREI------ARHSSVEqidiceIDKMVIDVSKKFFpdlAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
|
90 100 110
....*....|....*....|....*....|....*....
gi 1523361231 138 TDIILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 176
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCT 204
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
74-174 |
3.38e-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: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 74 IGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARNLFeLPFEGEKFEIIEADGAEYIKVFRHNTDIILVDGFdgeqiID 153
Cdd:pfam08242 3 IGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERL-AALGLLNAVRVELFQLDLGELDPGSFDVVVASNV-----LH 76
|
90 100
....*....|....*....|..
gi 1523361231 154 ALVE-EPFFRDCRNALSSDGIF 174
Cdd:pfam08242 77 HLADpRAVLRNIRRLLKPGGVL 98
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
74-175 |
5.57e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 38.03 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 74 IGLGGGSFARWIDTYLPDTrqTAVDINPQVIAIARNLfelpFEGEKFEIIEADgAEYIKvFRHNT-DIILvdgfdgeqII 152
Cdd:pfam08241 3 VGCGTGLLTELLARLGARV--TGVDISPEMLELAREK----APREGLTFVVGD-AEDLP-FPDNSfDLVL--------SS 66
|
90 100
....*....|....*....|....*..
gi 1523361231 153 DAL--VEEP--FFRDCRNALSSDGIFV 175
Cdd:pfam08241 67 EVLhhVEDPerALREIARVLKPGGILI 93
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
74-176 |
5.82e-03 |
|
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: 35.48 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523361231 74 IGLGGGSFARWIDTYlPDTRQTAVDINPQVIAIARNlFELPFEGEKFEIIEADGAEYIKVFRHNTDIILVDGFdgeqiID 153
Cdd:cd02440 5 LGCGTGALALALASG-PGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP-----LH 77
|
90 100
....*....|....*....|....*
gi 1523361231 154 ALVEEP--FFRDCRNALSSDGIFVT 176
Cdd:cd02440 78 HLVEDLarFLEEARRLLKPGGVLVL 102
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