|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
1-263 |
1.47e-161 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 448.33 E-value: 1.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 1 MARHPYRRLRPAKSGFPEVGISEEGNIRSLHLGSDTIQSSMNLDHPSELVLSYSRAMMGWLLFTDAlPQHITQIGLGGGS 80
Cdd:PRK04457 1 MARHPYRRLRPAKAGFPEVGVSEEGGVRSLHLGSDTVQSSMRIDDPSELELAYTRAMMGFLLFNPR-PQHILQIGLGGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 81 FARWIDTYLPDTRQTAVDINPQVIAIARSLFELPFEGEKFEIIEADGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPF 160
Cdd:PRK04457 80 LAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 161 FRDCRNALSSDGIFVTNWWSGDKRYQRFIERLLSVFEGRVLELPAESHGNVAVMAFQSSPKEQNIDKLKKRADKLSNAYG 240
Cdd:PRK04457 160 FDDCRNALSSDGIFVVNLWSRDKRYDRYLERLESSFEGRVLELPAESHGNVAVFAFKSAPKELRWDKLRKRAKKLENEHG 239
|
250 260
....*....|....*....|...
gi 488159220 241 LDFHRMLAGLKASNPNNGKHFHL 263
Cdd:PRK04457 240 LDFHRFVAKLKASNPNTGKRLLL 262
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
28-216 |
2.49e-55 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 176.56 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 28 RSLHLGSDtIQSSMNLDhpselVLSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIA 107
Cdd:COG0421 4 RVLVLDGV-VQSTMELD-----EFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 108 RSLFELP---FEGEKFEIIEADGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVTNWWSGD-- 182
Cdd:COG0421 78 REYFPLLapaFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFyg 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 488159220 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 |
3.72e-12 |
|
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: 63.11 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 51 LSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARSLfeLP-----FEGEKFEIIEA 125
Cdd:pfam01564 2 FIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKF--LPslaigFQDPRVKVVIG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488159220 126 DGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 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 |
1.11e-05 |
|
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: 45.81 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 69 QHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARS-----------------LFElPFEGEKFEII-------- 123
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEEnaeknqlehrvefiqsnLFE-PLAGQKIDIIvsnppyid 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488159220 124 EADGAEYIKVFRHNTDVILVDGFDGEQIIdalveEPFFRDCRNALSSDGIFV 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 |
1.11e-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: 42.91 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 27 IRSLHLGSDTIQSS--MNLDH----------PSELVLSYSrAMMgwllftDALPQ-----------HItqiglGGGSFA- 82
Cdd:NF037959 222 IRVVDVSADPGGPArlMVLDHlahginarddPTVLFTPYA-AML------DELARlrmgradfsafFI-----GGGAYTl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 83 --RWIDTYlPDTRQTAVDINPQVIAIARSLFElpFEGEKFEIIEADG---------AEYikvfrhntDVILVDGFDGEQI 151
Cdd:NF037959 290 prAWAARR-PAGRITVAEIDPAVTRVAAEDFW--FDPASATVLHEDArralrrrpeERF--------DVIVGDAFTDIAV 358
|
170 180
....*....|....*....|....*.
gi 488159220 152 IDALVEEPFFRDCRNALSSDGIFVTN 177
Cdd:NF037959 359 PAHLVTREFFELVRARLTPDGVYLMN 384
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
74-176 |
4.22e-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: 35.87 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 74 IGLGGGSFARWIDTYlPDTRQTAVDINPQVIAIARSlFELPFEGEKFEIIEADGAEYIKVFRHNTDVILVDGFdgeqiID 153
Cdd:cd02440 5 LGCGTGALALALASG-PGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP-----LH 77
|
90 100
....*....|....*....|....*
gi 488159220 154 ALVEEP--FFRDCRNALSSDGIFVT 176
Cdd:cd02440 78 HLVEDLarFLEEARRLLKPGGVLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04457 |
PRK04457 |
polyamine aminopropyltransferase; |
1-263 |
1.47e-161 |
|
polyamine aminopropyltransferase;
Pssm-ID: 179854 [Multi-domain] Cd Length: 262 Bit Score: 448.33 E-value: 1.47e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 1 MARHPYRRLRPAKSGFPEVGISEEGNIRSLHLGSDTIQSSMNLDHPSELVLSYSRAMMGWLLFTDAlPQHITQIGLGGGS 80
Cdd:PRK04457 1 MARHPYRRLRPAKAGFPEVGVSEEGGVRSLHLGSDTVQSSMRIDDPSELELAYTRAMMGFLLFNPR-PQHILQIGLGGGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 81 FARWIDTYLPDTRQTAVDINPQVIAIARSLFELPFEGEKFEIIEADGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPF 160
Cdd:PRK04457 80 LAKFIYTYLPDTRQTAVEINPQVIAVARNHFELPENGERFEVIEADGAEYIAVHRHSTDVILVDGFDGEGIIDALCTQPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 161 FRDCRNALSSDGIFVTNWWSGDKRYQRFIERLLSVFEGRVLELPAESHGNVAVMAFQSSPKEQNIDKLKKRADKLSNAYG 240
Cdd:PRK04457 160 FDDCRNALSSDGIFVVNLWSRDKRYDRYLERLESSFEGRVLELPAESHGNVAVFAFKSAPKELRWDKLRKRAKKLENEHG 239
|
250 260
....*....|....*....|...
gi 488159220 241 LDFHRMLAGLKASNPNNGKHFHL 263
Cdd:PRK04457 240 LDFHRFVAKLKASNPNTGKRLLL 262
|
|
| SpeE |
COG0421 |
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
28-216 |
2.49e-55 |
|
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 176.56 E-value: 2.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 28 RSLHLGSDtIQSSMNLDhpselVLSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIA 107
Cdd:COG0421 4 RVLVLDGV-VQSTMELD-----EFEYHEMMAHVPLLFHPNPKRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 108 RSLFELP---FEGEKFEIIEADGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVTNWWSGD-- 182
Cdd:COG0421 78 REYFPLLapaFDDPRLRVVIGDGRAFLREAEESYDVIIVDLTDPVGPAEGLFTREFYEDCRRALKPGGVLVVNLGSPFyg 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 488159220 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 |
3.72e-12 |
|
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: 63.11 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 51 LSYSRAMMGWLLFTDALPQHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARSLfeLP-----FEGEKFEIIEA 125
Cdd:pfam01564 2 FIYHEMIAHVPLCSHPNPKKVLIIGGGDGGVLREVVKHPSVEKITLVDIDEKVIDFSKKF--LPslaigFQDPRVKVVIG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488159220 126 DGAEYIKVFRHNTDVILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 176
Cdd:pfam01564 80 DGFKFLKDYLNTFDVIIVDSTDPVGPAENLFSKPFFDLLKKALKEDGVFIT 130
|
|
| COG4262 |
COG4262 |
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
74-177 |
5.31e-09 |
|
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];
Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 56.03 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 74 IGLGGGSFARWIDTYlPDTRQ-TAVDINPQVIAIARSLFELP------FEGEKFEIIEADGAEYIKVFRHNTDVILVDGF 146
Cdd:COG4262 293 LGGGDGLAAREVLKY-PDVESvTLVDLDPEVTDLAKTNPFLRelnggaLNDPRVTVVNADAFQFLRETDEKYDVIIVDLP 371
|
90 100 110
....*....|....*....|....*....|..
gi 488159220 147 DGEQIIDA-LVEEPFFRDCRNALSSDGIFVTN 177
Cdd:COG4262 372 DPSNFSLGkLYSVEFYRLVRRHLAPGGVLVVQ 403
|
|
| PRK00811 |
PRK00811 |
polyamine aminopropyltransferase; |
97-176 |
1.20e-08 |
|
polyamine aminopropyltransferase;
Pssm-ID: 234843 [Multi-domain] Cd Length: 283 Bit Score: 54.39 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 97 VDINPQVIAIARSLFelP------FEGEKFEIIEADGAEYIKVFRHNTDVILVDGFD----GEqiidALVEEPFFRDCRN 166
Cdd:PRK00811 106 VEIDERVVEVCRKYL--PeiaggaYDDPRVELVIGDGIKFVAETENSFDVIIVDSTDpvgpAE----GLFTKEFYENCKR 179
|
90
....*....|
gi 488159220 167 ALSSDGIFVT 176
Cdd:PRK00811 180 ALKEDGIFVA 189
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
68-175 |
2.74e-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: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 68 PQHITQIGLGGGSFARWIDTYLPDTRQ-TAVDINPQVIAIARSLFELPFEGEKFEIIEADGAEYIKVFRHNT-DVILVDG 145
Cdd:COG4122 17 AKRILEIGTGTGYSTLWLARALPDDGRlTTIEIDPERAAIARENFARAGLADRIRLILGDALEVLPRLADGPfDLVFIDA 96
|
90 100 110
....*....|....*....|....*....|
gi 488159220 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 |
1.11e-05 |
|
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: 45.81 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 69 QHITQIGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARS-----------------LFElPFEGEKFEII-------- 123
Cdd:TIGR00536 116 LHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEEnaeknqlehrvefiqsnLFE-PLAGQKIDIIvsnppyid 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 488159220 124 EADGAEYIKVFRHNTDVILVDGFDGEQIIdalveEPFFRDCRNALSSDGIFV 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 |
1.11e-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: 42.91 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 27 IRSLHLGSDTIQSS--MNLDH----------PSELVLSYSrAMMgwllftDALPQ-----------HItqiglGGGSFA- 82
Cdd:NF037959 222 IRVVDVSADPGGPArlMVLDHlahginarddPTVLFTPYA-AML------DELARlrmgradfsafFI-----GGGAYTl 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 83 --RWIDTYlPDTRQTAVDINPQVIAIARSLFElpFEGEKFEIIEADG---------AEYikvfrhntDVILVDGFDGEQI 151
Cdd:NF037959 290 prAWAARR-PAGRITVAEIDPAVTRVAAEDFW--FDPASATVLHEDArralrrrpeERF--------DVIVGDAFTDIAV 358
|
170 180
....*....|....*....|....*.
gi 488159220 152 IDALVEEPFFRDCRNALSSDGIFVTN 177
Cdd:NF037959 359 PAHLVTREFFELVRARLTPDGVYLMN 384
|
|
| PLN02366 |
PLN02366 |
spermidine synthase |
68-176 |
1.45e-04 |
|
spermidine synthase
Pssm-ID: 215208 [Multi-domain] Cd Length: 308 Bit Score: 42.33 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 68 PQHITQIGLGGGSFARWIdtylpdTRQTAVD------INPQVIAIARSLF---ELPFEGEKFEIIEADGAEYIK-VFRHN 137
Cdd:PLN02366 92 PKKVLVVGGGDGGVLREI------ARHSSVEqidiceIDKMVIDVSKKFFpdlAVGFDDPRVNLHIGDGVEFLKnAPEGT 165
|
90 100 110
....*....|....*....|....*....|....*....
gi 488159220 138 TDVILVDGFDGEQIIDALVEEPFFRDCRNALSSDGIFVT 176
Cdd:PLN02366 166 YDAIIVDSSDPVGPAQELFEKPFFESVARALRPGGVVCT 204
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
74-175 |
2.92e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 38.80 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 74 IGLGGGSFARWIDTYLPDTrqTAVDINPQVIAIARSLfelpFEGEKFEIIEADgAEYIKvFRHNT-DVILvdgfdgeqII 152
Cdd:pfam08241 3 VGCGTGLLTELLARLGARV--TGVDISPEMLELAREK----APREGLTFVVGD-AEDLP-FPDNSfDLVL--------SS 66
|
90 100
....*....|....*....|....*..
gi 488159220 153 DAL--VEEP--FFRDCRNALSSDGIFV 175
Cdd:pfam08241 67 EVLhhVEDPerALREIARVLKPGGILI 93
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
74-174 |
4.28e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 38.50 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 74 IGLGGGSFARWIDTYLPDTRQTAVDINPQVIAIARSLFeLPFEGEKFEIIEADGAEYIKVFRHNTDVILVDGFdgeqiID 153
Cdd:pfam08242 3 IGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERL-AALGLLNAVRVELFQLDLGELDPGSFDVVVASNV-----LH 76
|
90 100
....*....|....*....|..
gi 488159220 154 ALVE-EPFFRDCRNALSSDGIF 174
Cdd:pfam08242 77 HLADpRAVLRNIRRLLKPGGVL 98
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
74-176 |
4.22e-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: 35.87 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488159220 74 IGLGGGSFARWIDTYlPDTRQTAVDINPQVIAIARSlFELPFEGEKFEIIEADGAEYIKVFRHNTDVILVDGFdgeqiID 153
Cdd:cd02440 5 LGCGTGALALALASG-PGARVTGVDISPVALELARK-AAAALLADNVEVLKGDAEELPPEADESFDVIISDPP-----LH 77
|
90 100
....*....|....*....|....*
gi 488159220 154 ALVEEP--FFRDCRNALSSDGIFVT 176
Cdd:cd02440 78 HLVEDLarFLEEARRLLKPGGVLVL 102
|
|
| |
