|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
15-282 |
2.85e-150 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 421.84 E-value: 2.85e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 15 KLTLSDSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEHPEWQNFVNALTTNLTSFFR 94
Cdd:PRK10611 19 RLALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSAEWQAFINALTTNLTAFFR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 95 ETYHFPVLAEHARQRPNGYRVWCTAASTGEEPCSIAMTLDETLGSATGGPRVWASDIDTEVLAKAEAGVYRMSDLHSLTL 174
Cdd:PRK10611 99 EAHHFPILAEHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 175 VQKRHYFLRGSGENSDRVKVKPELLAAIHYQRLNLLDNSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDGLL 254
Cdd:PRK10611 179 QQLQRYFMRGTGPHEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLL 258
|
250 260
....*....|....*....|....*...
gi 505384520 255 FVGHSEHFNHPHIPLRLRGQSVYELTEA 282
Cdd:PRK10611 259 FAGHSENFSQLSREFYLRGQTVYGLSKD 286
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
17-277 |
5.80e-94 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 278.20 E-value: 5.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 17 TLSDSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEhpEWQNFVNALTTNLTSFFRET 96
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE--ELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 97 YHFPVLAEH------ARQRPNGY-RVWCTAASTGEEPCSIAMTLDETLGSATGGP-RVWASDIDTEVLAKAEAGVYRMSD 168
Cdd:COG1352 81 EHFEALREEvlpellARRRAGRPlRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRvEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 169 LHSLTLVQKRHYFLRgsgeNSDRVKVKPELLAAIHYQRLNLLDNSWPLpGPFDAIFCRNVMIYFDAPTQKRLLERFARML 248
Cdd:COG1352 161 LRGLPPEYLSRYFTK----EGGRYRIKPELREMVTFAQHNLLDDPPPF-GRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|..
gi 505384520 249 KPDGLLFVGHSEHFNHPH---IPLRLRGQSVY 277
Cdd:COG1352 236 APGGYLFLGHSESLGGLSdlfEPVDKKGRFIY 267
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
20-277 |
2.33e-90 |
|
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: 268.77 E-value: 2.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 20 DSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEHPEWQNFVNALTTNLTSFFRETYHF 99
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 100 PVLAEH-----ARQRPNG--YRVWCTAASTGEEPCSIAMTLDETLGSATGGP-RVWASDIDTEVLAKAEAGVYRMSDLHS 171
Cdd:smart00138 81 EALEEKvlpllIASRRHGrrVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDvKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 172 LTLVQKRHYFLRGsgenSDRVKVKPELLAAIHYQRLNLLDnSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPD 251
Cdd:smart00138 161 LPKALLARYFKEV----EDKYRVKPELKERVRFAKHNLLA-ESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPG 235
|
250 260
....*....|....*....|....*.
gi 505384520 252 GLLFVGHSEHFNHPHIPLRLRGQSVY 277
Cdd:smart00138 236 GYLFLGHSESLPGLTDKFEPIEGTVY 261
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
88-264 |
6.93e-64 |
|
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: 199.04 E-value: 6.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 88 NLTSFFRETYHFPVLAEHAR------QRPNGYRVWCTAASTGEEPCSIAMTLDETLGSATG-GPRVWASDIDTEVLAKAE 160
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLpllakaKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARwDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 161 AGVYRMSDLHSLTLVQKRHYFLRGSGensDRVKVKPELLAAIHYQRLNLLDnSWPLPGPFDAIFCRNVMIYFDAPTQKRL 240
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTAG---GGYTVKPEIKSMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKI 156
|
170 180
....*....|....*....|....
gi 505384520 241 LERFARMLKPDGLLFVGHSEHFNH 264
Cdd:pfam01739 157 LNRFAEKLKPGGYLFLGHSEALPG 180
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
133-256 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 133 LDetLGSATG----------GPRVWASDIDTEVLAKAEAGVYRmsdlhsltlvqkrhyflrgsgENSDRVKVKPEllaai 202
Cdd:cd02440 3 LD--LGCGTGalalalasgpGARVTGVDISPVALELARKAAAA---------------------LLADNVEVLKG----- 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 505384520 203 hyqrlNLLDNSWPLPGPFDAIFCRNVMIYFdAPTQKRLLERFARMLKPDGLLFV 256
Cdd:cd02440 55 -----DAEELPPEADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10611 |
PRK10611 |
protein-glutamate O-methyltransferase CheR; |
15-282 |
2.85e-150 |
|
protein-glutamate O-methyltransferase CheR;
Pssm-ID: 236725 [Multi-domain] Cd Length: 287 Bit Score: 421.84 E-value: 2.85e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 15 KLTLSDSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEHPEWQNFVNALTTNLTSFFR 94
Cdd:PRK10611 19 RLALSDAHFRRICQLIYQRAGIVLADHKREMVYNRLVRRLRSLGLNDFGQYLALLESNQNSAEWQAFINALTTNLTAFFR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 95 ETYHFPVLAEHARQRPNGYRVWCTAASTGEEPCSIAMTLDETLGSATGGPRVWASDIDTEVLAKAEAGVYRMSDLHSLTL 174
Cdd:PRK10611 99 EAHHFPILAEHARRRSGEYRVWSAAASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 175 VQKRHYFLRGSGENSDRVKVKPELLAAIHYQRLNLLDNSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDGLL 254
Cdd:PRK10611 179 QQLQRYFMRGTGPHEGLVRVRQELANYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLL 258
|
250 260
....*....|....*....|....*...
gi 505384520 255 FVGHSEHFNHPHIPLRLRGQSVYELTEA 282
Cdd:PRK10611 259 FAGHSENFSQLSREFYLRGQTVYGLSKD 286
|
|
| CheR |
COG1352 |
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms]; |
17-277 |
5.80e-94 |
|
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
Pssm-ID: 440963 [Multi-domain] Cd Length: 272 Bit Score: 278.20 E-value: 5.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 17 TLSDSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEhpEWQNFVNALTTNLTSFFRET 96
Cdd:COG1352 3 ELSDAEFERLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPE--ELQALIDALTINVTEFFRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 97 YHFPVLAEH------ARQRPNGY-RVWCTAASTGEEPCSIAMTLDETLGSATGGP-RVWASDIDTEVLAKAEAGVYRMSD 168
Cdd:COG1352 81 EHFEALREEvlpellARRRAGRPlRIWSAGCSTGEEPYSLAMLLAEAGGELAGWRvEILATDISEEALEKARAGIYPERS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 169 LHSLTLVQKRHYFLRgsgeNSDRVKVKPELLAAIHYQRLNLLDNSWPLpGPFDAIFCRNVMIYFDAPTQKRLLERFARML 248
Cdd:COG1352 161 LRGLPPEYLSRYFTK----EGGRYRIKPELREMVTFAQHNLLDDPPPF-GRFDLIFCRNVLIYFDPELQRRVLRRFHDSL 235
|
250 260 270
....*....|....*....|....*....|..
gi 505384520 249 KPDGLLFVGHSEHFNHPH---IPLRLRGQSVY 277
Cdd:COG1352 236 APGGYLFLGHSESLGGLSdlfEPVDKKGRFIY 267
|
|
| MeTrc |
smart00138 |
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ... |
20-277 |
2.33e-90 |
|
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: 268.77 E-value: 2.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 20 DSELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESHSEHPEWQNFVNALTTNLTSFFRETYHF 99
Cdd:smart00138 1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRGEEELAELLDLMTTNETRFFRESKHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 100 PVLAEH-----ARQRPNG--YRVWCTAASTGEEPCSIAMTLDETLGSATGGP-RVWASDIDTEVLAKAEAGVYRMSDLHS 171
Cdd:smart00138 81 EALEEKvlpllIASRRHGrrVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDvKILATDIDLKALEKARAGIYPERELED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 172 LTLVQKRHYFLRGsgenSDRVKVKPELLAAIHYQRLNLLDnSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPD 251
Cdd:smart00138 161 LPKALLARYFKEV----EDKYRVKPELKERVRFAKHNLLA-ESPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPG 235
|
250 260
....*....|....*....|....*.
gi 505384520 252 GLLFVGHSEHFNHPHIPLRLRGQSVY 277
Cdd:smart00138 236 GYLFLGHSESLPGLTDKFEPIEGTVY 261
|
|
| CheR |
pfam01739 |
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ... |
88-264 |
6.93e-64 |
|
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: 199.04 E-value: 6.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 88 NLTSFFRETYHFPVLAEHAR------QRPNGYRVWCTAASTGEEPCSIAMTLDETLGSATG-GPRVWASDIDTEVLAKAE 160
Cdd:pfam01739 1 NETRFFREPAHFEELKKYVLpllakaKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAARwDFKILATDIDLSVLEKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 161 AGVYRMSDLHSLTLVQKRHYFLRGSGensDRVKVKPELLAAIHYQRLNLLDnSWPLPGPFDAIFCRNVMIYFDAPTQKRL 240
Cdd:pfam01739 81 AGVYPERELEGLPEELLRRYFEKTAG---GGYTVKPEIKSMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKI 156
|
170 180
....*....|....*....|....
gi 505384520 241 LERFARMLKPDGLLFVGHSEHFNH 264
Cdd:pfam01739 157 LNRFAEKLKPGGYLFLGHSEALPG 180
|
|
| CheR_N |
pfam03705 |
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ... |
22-72 |
2.11e-12 |
|
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: 60.53 E-value: 2.11e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 505384520 22 ELQRIGQLIYRRAGIVVNAQKREMIFNRLSRRLRALGIDTFLEYISILESH 72
Cdd:pfam03705 2 EFERLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSD 52
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
202-252 |
1.60e-08 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 51.03 E-value: 1.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 505384520 202 IHYQRLNLLDnsWPLP-GPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDG 252
Cdd:pfam13649 47 VEFVQGDAED--LPFPdGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
133-256 |
4.12e-07 |
|
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: 48.09 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 133 LDetLGSATG---------GPRVWASDIDTEVLAKAEAgvyRMSDLHsltlvqkrhyflrgsgensdrvkvkpellaaIH 203
Cdd:COG2227 29 LD--VGCGTGrlalalarrGADVTGVDISPEALEIARE---RAAELN-------------------------------VD 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 505384520 204 YQRLNLLDnsWPLP-GPFDAIFCRNVMIYFDAPtqKRLLERFARMLKPDGLLFV 256
Cdd:COG2227 73 FVQGDLED--LPLEdGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLLLL 122
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
133-256 |
1.46e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 45.73 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 133 LDetLGSATG---------GPRVWASDIDTEVLAKAEAgvyrmsdlhslTLVQKRHYFLRGSGENsdrvkvkpellaaih 203
Cdd:pfam08241 1 LD--VGCGTGlltellarlGARVTGVDISPEMLELARE-----------KAPREGLTFVVGDAED--------------- 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 505384520 204 yqrLNLLDNSwplpgpFDAIFCRNVMIYFDAPtqKRLLERFARMLKPDGLLFV 256
Cdd:pfam08241 53 ---LPFPDNS------FDLVLSSEVLHHVEDP--ERALREIARVLKPGGILII 94
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
212-256 |
2.49e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 46.46 E-value: 2.49e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 505384520 212 NSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDGLLFV 256
Cdd:COG2230 111 RDLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
133-256 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 133 LDetLGSATG----------GPRVWASDIDTEVLAKAEAGVYRmsdlhsltlvqkrhyflrgsgENSDRVKVKPEllaai 202
Cdd:cd02440 3 LD--LGCGTGalalalasgpGARVTGVDISPVALELARKAAAA---------------------LLADNVEVLKG----- 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 505384520 203 hyqrlNLLDNSWPLPGPFDAIFCRNVMIYFdAPTQKRLLERFARMLKPDGLLFV 256
Cdd:cd02440 55 -----DAEELPPEADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLVL 102
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
206-254 |
1.20e-04 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 40.43 E-value: 1.20e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505384520 206 RLNLLDNSWPLPGPFDAIFCRNVMIYFDAPtqKRLLERFARMLKPDGLL 254
Cdd:pfam08242 52 ELFQLDLGELDPGSFDVVVASNVLHHLADP--RAVLRNIRRLLKPGGVL 98
|
|
| SmtA |
COG0500 |
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
199-256 |
2.01e-04 |
|
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];
Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 41.44 E-value: 2.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 505384520 199 LAAIHYQRLNLLDNSWPLPGPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDGLLFV 256
Cdd:COG0500 74 LGNVEFLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
215-270 |
2.18e-04 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 40.36 E-value: 2.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505384520 215 PLP-GPFDAIFCRNVMIYFDAPtqKRLLERFARMLKPDGLLFVghSEHFNHPHIPLR 270
Cdd:COG2226 82 PFPdGSFDLVISSFVLHHLPDP--ERALAEIARVLKPGGRLVV--VDFSPPDLAELE 134
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
216-254 |
6.38e-04 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 39.60 E-value: 6.38e-04
10 20 30
....*....|....*....|....*....|....*....
gi 505384520 216 LPGPFDAIFCRNVMIYFDAPtqKRLLERFARMLKPDGLL 254
Cdd:COG4976 104 PDGRFDLIVAADVLTYLGDL--AAVFAGVARALKPGGLF 140
|
|
| Methyltransf_23 |
pfam13489 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
185-272 |
2.39e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 37.79 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384520 185 SGENSDRVKVKPELLAAIHYQRLNLLDNSWPLPGPFDAIFCRNVMIYFDAPTqkRLLERFARMLKPDGLLFvgHSEHFNH 264
Cdd:pfam13489 46 SVTGVDPSPIAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPDPP--ALLRQIAALLKPGGLLL--LSTPLAS 121
|
....*...
gi 505384520 265 PHIPLRLR 272
Cdd:pfam13489 122 DEADRLLL 129
|
|
| COG4627 |
COG4627 |
Predicted SAM-depedendent methyltransferase [General function prediction only]; |
209-256 |
6.04e-03 |
|
Predicted SAM-depedendent methyltransferase [General function prediction only];
Pssm-ID: 443666 [Multi-domain] Cd Length: 161 Bit Score: 36.77 E-value: 6.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 505384520 209 LLDNSWPLP---GPFDAIFCRNVMIYFDAPTQKRLLERFARMLKPDGLLFV 256
Cdd:COG4627 33 VGDLTDPLPfpdNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRI 83
|
|
| |
