|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
1-286 |
0e+00 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 613.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 1 MTSSLPCGQTSLLLQMTERLALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSG 80
Cdd:PRK10611 1 MTSSLPCGQTSLLLQMTQRLALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 81 EWQAFINSLTTNLTAFFREAHHFPLLADHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVL 160
Cdd:PRK10611 81 EWQAFINALTTNLTAFFREAHHFPILAEHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 161 EKARSGIYRHEELKNLTPQQLQRYFMRGTGPHQGLVRVRQELANYVDFAPLNLLAKQYTVPGPFDAIFCRNVMIYFDQTT 240
Cdd:PRK10611 161 EKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446126486 241 QQEILRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQTVYALSKD 286
Cdd:PRK10611 241 QERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTVYGLSKD 286
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
24-284 |
3.07e-128 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 365.07 E-value: 3.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 24 DAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSGEWQAFINSLTTNLTAFFREAHHF 103
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 104 PLLADHA-------RRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTA-PGRWKVFASDIDTEVLEKARSGIYRHEELKN 175
Cdd:smart00138 81 EALEEKVlplliasRRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKGrEPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 176 LTPQQLQRYFMRGtgphQGLVRVRQELANYVDFAPLNLLAKQYtVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPD 255
Cdd:smart00138 161 LPKALLARYFKEV----EDKYRVKPELKERVRFAKHNLLAESP-PLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPG 235
|
250 260
....*....|....*....|....*....
gi 446126486 256 GLLFAGHSENFSHLERRFTLRGQTVYALS 284
Cdd:smart00138 236 GYLFLGHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
21-281 |
2.00e-106 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 310.17 E-value: 2.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 21 ALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHsgEWQAFINSLTTNLTAFFREA 100
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE--ELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 101 HHFPLLADH-------ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPG-RWKVFASDIDTEVLEKARSGIYRHEE 172
Cdd:COG1352 81 EHFEALREEvlpellaRRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGwRVEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 173 LKNLTPQQLQRYFMRgtgpHQGLVRVRQELANYVDFAPLNLLaKQYTVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLL 252
Cdd:COG1352 161 LRGLPPEYLSRYFTK----EGGRYRIKPELREMVTFAQHNLL-DDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|..
gi 446126486 253 KPDGLLFAGHSENFSHLERRFTL---RGQTVY 281
Cdd:COG1352 236 APGGYLFLGHSESLGGLSDLFEPvdkKGRFIY 267
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
92-278 |
9.95e-83 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 246.81 E-value: 9.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 92 NLTAFFREAHHFPLLADHAR------RRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPG-RWKVFASDIDTEVLEKAR 164
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLpllakaKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARwDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 165 SGIYRHEELKNLTPQQLQRYFMRGTGPHQglvRVRQELANYVDFAPLNLLAkQYTVPGPFDAIFCRNVMIYFDQTTQQEI 244
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTAGGGY---TVKPEIKSMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKI 156
|
170 180 190
....*....|....*....|....*....|....
gi 446126486 245 LRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQ 278
Cdd:pfam01739 157 LNRFAEKLKPGGYLFLGHSEALPGNPDKFKKVGS 190
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
118-259 |
1.68e-05 |
|
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: 42.80 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 118 RVWSAAASTGEepysIAMTLADTLGtapgrWKVFASDIDTEVLEKARSGIYRHEELKnltpqqlqryfmrgtgphqglVR 197
Cdd:cd02440 1 RVLDLGCGTGA----LALALASGPG-----ARVTGVDISPVALELARKAAAALLADN---------------------VE 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446126486 198 VRQELANYVDFAPlnllakqytvPGPFDAIFCRNVMIYFDQtTQQEILRRFVPLLKPDGLLF 259
Cdd:cd02440 51 VLKGDAEELPPEA----------DESFDVIISDPPLHHLVE-DLARFLEEARRLLKPGGVLV 101
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
1-286 |
0e+00 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 613.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 1 MTSSLPCGQTSLLLQMTERLALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSG 80
Cdd:PRK10611 1 MTSSLPCGQTSLLLQMTQRLALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 81 EWQAFINSLTTNLTAFFREAHHFPLLADHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVL 160
Cdd:PRK10611 81 EWQAFINALTTNLTAFFREAHHFPILAEHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 161 EKARSGIYRHEELKNLTPQQLQRYFMRGTGPHQGLVRVRQELANYVDFAPLNLLAKQYTVPGPFDAIFCRNVMIYFDQTT 240
Cdd:PRK10611 161 EKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446126486 241 QQEILRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQTVYALSKD 286
Cdd:PRK10611 241 QERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTVYGLSKD 286
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
24-284 |
3.07e-128 |
|
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.
Pssm-ID: 214534 [Multi-domain] Cd Length: 264 Bit Score: 365.07 E-value: 3.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 24 DAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHSGEWQAFINSLTTNLTAFFREAHHF 103
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 104 PLLADHA-------RRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTA-PGRWKVFASDIDTEVLEKARSGIYRHEELKN 175
Cdd:smart00138 81 EALEEKVlplliasRRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKGrEPDVKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 176 LTPQQLQRYFMRGtgphQGLVRVRQELANYVDFAPLNLLAKQYtVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPD 255
Cdd:smart00138 161 LPKALLARYFKEV----EDKYRVKPELKERVRFAKHNLLAESP-PLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPG 235
|
250 260
....*....|....*....|....*....
gi 446126486 256 GLLFAGHSENFSHLERRFTLRGQTVYALS 284
Cdd:smart00138 236 GYLFLGHSESLPGLTDKFEPIEGTVYFYS 264
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
21-281 |
2.00e-106 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 310.17 E-value: 2.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 21 ALSDAHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQHsgEWQAFINSLTTNLTAFFREA 100
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE--ELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 101 HHFPLLADH-------ARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPG-RWKVFASDIDTEVLEKARSGIYRHEE 172
Cdd:COG1352 81 EHFEALREEvlpellaRRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAGwRVEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 173 LKNLTPQQLQRYFMRgtgpHQGLVRVRQELANYVDFAPLNLLaKQYTVPGPFDAIFCRNVMIYFDQTTQQEILRRFVPLL 252
Cdd:COG1352 161 LRGLPPEYLSRYFTK----EGGRYRIKPELREMVTFAQHNLL-DDPPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|..
gi 446126486 253 KPDGLLFAGHSENFSHLERRFTL---RGQTVY 281
Cdd:COG1352 236 APGGYLFLGHSESLGGLSDLFEPvdkKGRFIY 267
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
92-278 |
9.95e-83 |
|
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.
Pssm-ID: 426403 Cd Length: 190 Bit Score: 246.81 E-value: 9.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 92 NLTAFFREAHHFPLLADHAR------RRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPG-RWKVFASDIDTEVLEKAR 164
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLpllakaKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARwDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 165 SGIYRHEELKNLTPQQLQRYFMRGTGPHQglvRVRQELANYVDFAPLNLLAkQYTVPGPFDAIFCRNVMIYFDQTTQQEI 244
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTAGGGY---TVKPEIKSMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKI 156
|
170 180 190
....*....|....*....|....*....|....
gi 446126486 245 LRRFVPLLKPDGLLFAGHSENFSHLERRFTLRGQ 278
Cdd:pfam01739 157 LNRFAEKLKPGGYLFLGHSEALPGNPDKFKKVGS 190
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
25-77 |
1.48e-15 |
|
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase.
Pssm-ID: 461017 [Multi-domain] Cd Length: 53 Bit Score: 69.39 E-value: 1.48e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446126486 25 AHFRRISQLIYQRAGIVLADHKRDMVYNRLVRRLRSLGLTDFGHYLNLLESNQ 77
Cdd:pfam03705 1 AEFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
118-259 |
1.68e-05 |
|
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: 42.80 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 118 RVWSAAASTGEepysIAMTLADTLGtapgrWKVFASDIDTEVLEKARSGIYRHEELKnltpqqlqryfmrgtgphqglVR 197
Cdd:cd02440 1 RVLDLGCGTGA----LALALASGPG-----ARVTGVDISPVALELARKAAAALLADN---------------------VE 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446126486 198 VRQELANYVDFAPlnllakqytvPGPFDAIFCRNVMIYFDQtTQQEILRRFVPLLKPDGLLF 259
Cdd:cd02440 51 VLKGDAEELPPEA----------DESFDVIISDPPLHHLVE-DLARFLEEARRLLKPGGVLV 101
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
148-259 |
2.72e-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: 42.70 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 148 WKVFASDIDTEVLEKARSgiyRHEELKnltpqqlqryfmrgtgphqglVRVRQELANYVDFAPlnllakqytvpGPFDAI 227
Cdd:COG2227 47 ADVTGVDISPEALEIARE---RAAELN---------------------VDFVQGDLEDLPLED-----------GSFDLV 91
|
90 100 110
....*....|....*....|....*....|..
gi 446126486 228 FCRNVMIYFDQttQQEILRRFVPLLKPDGLLF 259
Cdd:COG2227 92 ICSEVLEHLPD--PAALLRELARLLKPGGLLL 121
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
133-256 |
4.10e-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: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 133 IAMTLADTLGtapgrWKVFASDIDTEVLEKARsgiyrheelKNLTPQQLQryfmrgtgphqglVRVRQELANYVDFAPln 212
Cdd:pfam13649 11 LTLALARRGG-----ARVTGVDLSPEMLERAR---------ERAAEAGLN-------------VEFVQGDAEDLPFPD-- 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446126486 213 llakqytvpGPFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPDG 256
Cdd:pfam13649 62 ---------GSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
136-258 |
4.17e-05 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 41.58 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 136 TLADTLGTAPGRWKVFASDIDTEVLEKARsgiyrhEELKNLTPQQLQRyfmrgtgphqglvrvrqelanyVDFAPLNLLA 215
Cdd:pfam08242 9 TLLRALLEALPGLEYTGLDISPAALEAAR------ERLAALGLLNAVR----------------------VELFQLDLGE 60
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446126486 216 KQytvPGPFDAIFCRNVMIYFDQTtqQEILRRFVPLLKPDGLL 258
Cdd:pfam08242 61 LD---PGSFDVVVASNVLHHLADP--RAVLRNIRRLLKPGGVL 98
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
143-259 |
3.94e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 40.67 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 143 TAPGRWKVFASDIDTEVLEKARSgIYRHEELKNLTPQQlqryfmrgtgphqglvrvrqelANYVDFAPLNLlakqytvpG 222
Cdd:COG0500 45 AARFGGRVIGIDLSPEAIALARA-RAAKAGLGNVEFLV----------------------ADLAELDPLPA--------E 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 446126486 223 PFDAIFCRNVMIYFDQTTQQEILRRFVPLLKPDGLLF 259
Cdd:COG0500 94 SFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLL 130
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
78-259 |
4.20e-04 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 39.91 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 78 HSGEWQAFINSLTTNLTAFFReahhfpLLADHARRRSGEyRVWSAAASTGeepySIAMTLADTLGtapgrWKVFASDIDT 157
Cdd:COG2230 21 SCAYFEDPDDTLEEAQEAKLD------LILRKLGLKPGM-RVLDIGCGWG----GLALYLARRYG-----VRVTGVTLSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446126486 158 EVLEKARsgiyrheelknltpQQLQRYFMRGtgphqglvRVRQELANYVDFAPlnllakqytvPGPFDAIFCRNVMIYFD 237
Cdd:COG2230 85 EQLEYAR--------------ERAAEAGLAD--------RVEVRLADYRDLPA----------DGQFDAIVSIGMFEHVG 132
|
170 180
....*....|....*....|..
gi 446126486 238 QTTQQEILRRFVPLLKPDGLLF 259
Cdd:COG2230 133 PENYPAYFAKVARLLKPGGRLL 154
|
|
| |
