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Conserved domains on  [gi|124494323|gb|ABN13216|]
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methyl-accepting chemotaxis protein methyltransferase [Bacillus subtilis]

Protein Classification

protein-glutamate O-methyltransferase( domain architecture ID 12190911)

protein-glutamate O-methyltransferase such as CheR, which catalyzes methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 1-254 7.91e-107

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: 309.60  E-value: 7.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323     1 MDTYSVFTTKWKQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQ--ALLNETLDRMTINVSEFYRNYKRW 78
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRgeEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323    79 EVLETAILPLI----KNGKPLKIWSAACSTGEEPYTLAMLLDQQKSL---PGFQILATDIDEKALEKAKKGVYQERSLQE 151
Cdd:smart00138  81 EALEEKVLPLLiasrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKgrePDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323   152 VPSSVKDRYFTQNANRsYEVKAEIKKNITFKKHNLLADRY-EQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLF 230
Cdd:smart00138 161 LPKALLARYFKEVEDK-YRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLF 239

                          250       260
                   ....*....|....*....|....*
gi 124494323   231 VGSTEQIFNPE-KFGLAPADTFFYQ 254
Cdd:smart00138 240 LGHSESLPGLTdKFEPIEGTVYFYS 264
 
Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 1-254 7.91e-107

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: 309.60  E-value: 7.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323     1 MDTYSVFTTKWKQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQ--ALLNETLDRMTINVSEFYRNYKRW 78
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRgeEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323    79 EVLETAILPLI----KNGKPLKIWSAACSTGEEPYTLAMLLDQQKSL---PGFQILATDIDEKALEKAKKGVYQERSLQE 151
Cdd:smart00138  81 EALEEKVLPLLiasrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKgrePDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323   152 VPSSVKDRYFTQNANRsYEVKAEIKKNITFKKHNLLADRY-EQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLF 230
Cdd:smart00138 161 LPKALLARYFKEVEDK-YRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLF 239

                          250       260
                   ....*....|....*....|....*
gi 124494323   231 VGSTEQIFNPE-KFGLAPADTFFYQ 254
Cdd:smart00138 240 LGHSESLPGLTdKFEPIEGTVYFYS 264
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
12-256 1.91e-103

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 301.31  E-value: 1.91e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  12 KQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQALLNETLDRMTINVSEFYRNYKRWEVLETAILP-LIK 90
Cdd:COG1352   17 RERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEALREEVLPeLLA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  91 N---GKPLKIWSAACSTGEEPYTLAMLLDQQKSLPG---FQILATDIDEKALEKAKKGVYQERSLQEVPSSVKDRYFTQN 164
Cdd:COG1352   97 RrraGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAgwrVEILATDISEEALEKARAGIYPERSLRGLPPEYLSRYFTKE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 165 ANRsYEVKAEIKKNITFKKHNLLAD-RYEQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTEQIFNPEKf 243
Cdd:COG1352  177 GGR-YRIKPELREMVTFAQHNLLDDpPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESLGGLSD- 254

                        250
                 ....*....|....*.
gi 124494323 244 GLAPAD---TFFYQKR 256
Cdd:COG1352  255 LFEPVDkkgRFIYRKR 270
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 67-248 1.01e-79

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: 237.95  E-value: 1.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323   67 NVSEFYRNYKRWEVLETAILPLI---KNGKPLKIWSAACSTGEEPYTLAMLLDQ--QKSLP-GFQILATDIDEKALEKAK 140
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLakaKNGKRVRIWSAGCSSGEEPYSLAMLLKEtfPNAARwDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  141 KGVYQERSLQEVPSSVKDRYFTQNANRSYEVKAEIKKNITFKKHNLLA-DRYEQDFDLIVCRNVFIYFTESAKEELYLKM 219
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDeYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 124494323  220 AHSLKKNGVLFVGSTEQIF-NPEKFGLAPA 248
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPgNPDKFKKVGS 190
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
29-235 1.06e-35

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 128.31  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  29 RRLTSLyekkGFQSFKDFAAALEKD------QALLNEtldrMTINVSEFYRNYKRWEVLetAILPLIKNGKpLKIWSAAC 102
Cdd:PRK10611  56 RRLRSL----GLNDFGQYLALLESNqnsaewQAFINA----LTTNLTAFFREAHHFPIL--AEHARRRSGE-YRVWSAAA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 103 STGEEPYTLAMLL-DQQKSLPG-FQILATDIDEKALEKAKKGVYQERSLQEVPSSVKDRYFTQNANrSYE----VKAEIK 176
Cdd:PRK10611 125 STGEEPYSIAMTLaDTLGTAPGrWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTG-PHEglvrVRQELA 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124494323 177 KNITFKKHNLLADRY--EQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTE 235
Cdd:PRK10611 204 NYVDFQQLNLLAKQWavPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
 
Name Accession Description Interval E-value
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 1-254 7.91e-107

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: 309.60  E-value: 7.91e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323     1 MDTYSVFTTKWKQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQ--ALLNETLDRMTINVSEFYRNYKRW 78
Cdd:smart00138   1 DADFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRgeEELAELLDLMTTNETRFFRESKHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323    79 EVLETAILPLI----KNGKPLKIWSAACSTGEEPYTLAMLLDQQKSL---PGFQILATDIDEKALEKAKKGVYQERSLQE 151
Cdd:smart00138  81 EALEEKVLPLLiasrRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKgrePDVKILATDIDLKALEKARAGIYPERELED 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323   152 VPSSVKDRYFTQNANRsYEVKAEIKKNITFKKHNLLADRY-EQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLF 230
Cdd:smart00138 161 LPKALLARYFKEVEDK-YRVKPELKERVRFAKHNLLAESPpLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLF 239

                          250       260
                   ....*....|....*....|....*
gi 124494323   231 VGSTEQIFNPE-KFGLAPADTFFYQ 254
Cdd:smart00138 240 LGHSESLPGLTdKFEPIEGTVYFYS 264
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
12-256 1.91e-103

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 301.31  E-value: 1.91e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  12 KQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQALLNETLDRMTINVSEFYRNYKRWEVLETAILP-LIK 90
Cdd:COG1352   17 RERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEALREEVLPeLLA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  91 N---GKPLKIWSAACSTGEEPYTLAMLLDQQKSLPG---FQILATDIDEKALEKAKKGVYQERSLQEVPSSVKDRYFTQN 164
Cdd:COG1352   97 RrraGRPLRIWSAGCSTGEEPYSLAMLLAEAGGELAgwrVEILATDISEEALEKARAGIYPERSLRGLPPEYLSRYFTKE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 165 ANRsYEVKAEIKKNITFKKHNLLAD-RYEQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTEQIFNPEKf 243
Cdd:COG1352  177 GGR-YRIKPELREMVTFAQHNLLDDpPPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESLGGLSD- 254

                        250
                 ....*....|....*.
gi 124494323 244 GLAPAD---TFFYQKR 256
Cdd:COG1352  255 LFEPVDkkgRFIYRKR 270
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 67-248 1.01e-79

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: 237.95  E-value: 1.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323   67 NVSEFYRNYKRWEVLETAILPLI---KNGKPLKIWSAACSTGEEPYTLAMLLDQ--QKSLP-GFQILATDIDEKALEKAK 140
Cdd:pfam01739   1 NETRFFREPAHFEELKKYVLPLLakaKNGKRVRIWSAGCSSGEEPYSLAMLLKEtfPNAARwDFKILATDIDLSVLEKAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  141 KGVYQERSLQEVPSSVKDRYFTQNANRSYEVKAEIKKNITFKKHNLLA-DRYEQDFDLIVCRNVFIYFTESAKEELYLKM 219
Cdd:pfam01739  81 AGVYPERELEGLPEELLRRYFEKTAGGGYTVKPEIKSMVLFEYLNLLDeYPPLGDFDVIFCRNVLIYFDEETQRKILNRF 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 124494323  220 AHSLKKNGVLFVGSTEQIF-NPEKFGLAPA 248
Cdd:pfam01739 161 AEKLKPGGYLFLGHSEALPgNPDKFKKVGS 190
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
29-235 1.06e-35

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 128.31  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  29 RRLTSLyekkGFQSFKDFAAALEKD------QALLNEtldrMTINVSEFYRNYKRWEVLetAILPLIKNGKpLKIWSAAC 102
Cdd:PRK10611  56 RRLRSL----GLNDFGQYLALLESNqnsaewQAFINA----LTTNLTAFFREAHHFPIL--AEHARRRSGE-YRVWSAAA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 103 STGEEPYTLAMLL-DQQKSLPG-FQILATDIDEKALEKAKKGVYQERSLQEVPSSVKDRYFTQNANrSYE----VKAEIK 176
Cdd:PRK10611 125 STGEEPYSIAMTLaDTLGTAPGrWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTG-PHEglvrVRQELA 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124494323 177 KNITFKKHNLLADRY--EQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFVGSTE 235
Cdd:PRK10611 204 NYVDFQQLNLLAKQWavPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
 12-54 4.75e-09

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: 51.28  E-value: 4.75e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 124494323   12 KQLTGVDLTLYKEAQMKRRLTSLYEKKGFQSFKDFAAALEKDQ 54
Cdd:pfam03705  11 YRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-227 4.33e-07

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.79  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  100 AACSTGeepYTLAMLLDQqkslPGFQILATDIDEKALEKAKKgvyqerslqevpssvkdRYFTQNANrsyevkaeikknI 179
Cdd:pfam13649   4 LGCGTG---RLTLALARR----GGARVTGVDLSPEMLERARE-----------------RAAEAGLN------------V 47

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 124494323  180 TFKKHNLLADRYEQD-FDLIVCRNVFIYFTESAKEELYLKMAHSLKKNG 227
Cdd:pfam13649  48 EFVQGDAEDLPFPDGsFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-235 4.98e-07

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.46  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  74 NYKRWEVLETAILPLIKNGKPLKIWSAACSTGeepyTLAMLLDQQkslpGFQILATDIDEKALEKAK-KGVYqerslqev 152
Cdd:COG4976   27 GYEAPALLAEELLARLPPGPFGRVLDLGCGTG----LLGEALRPR----GYRLTGVDLSEEMLAKAReKGVY-------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 153 pssvkDRYFTQNANRsyevkaeikknitfkkhnlLADRYEQdFDLIVCRNVFIYFteSAKEELYLKMAHSLKKNGvLFVG 232
Cdd:COG4976   91 -----DRLLVADLAD-------------------LAEPDGR-FDLIVAADVLTYL--GDLAAVFAGVARALKPGG-LFIF 142


                 ...
gi 124494323 233 STE 235
Cdd:COG4976  143 SVE 145
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
102-231 7.48e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.36  E-value: 7.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 102 CSTGeepYTLAMLLDQqksLPGFQILATDIDEKALEKAKkgvyqerslQEVPssvkdryftqnanrsyevkaeikkNITF 181
Cdd:COG4106   10 CGTG---RLTALLAER---FPGARVTGVDLSPEMLARAR---------ARLP------------------------NVRF 50

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 124494323 182 KKHNLLADRYEQDFDLIVCRNVFIYFTEsaKEELYLKMAHSLKKNGVLFV 231
Cdd:COG4106   51 VVADLRDLDPPEPFDLVVSNAALHWLPD--HAALLARLAAALAPGGVLAV 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 74-231 1.00e-06

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: 46.55  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  74 NYKRWEV-LETAILPLIKNGKplKIWSAACSTGeepYTLAMLLDQqkslpGFQILATDIDEKALEKAKKgvyqerslqev 152
Cdd:COG2227    6 ARDFWDRrLAALLARLLPAGG--RVLDVGCGTG---RLALALARR-----GADVTGVDISPEALEIARE----------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 153 pssvkdryftqnanrsyevKAEiKKNITFKKHNLLA-DRYEQDFDLIVCRNVFIYFTESakEELYLKMAHSLKKNGVLFV 231
Cdd:COG2227   65 -------------------RAA-ELNVDFVQGDLEDlPLEDGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGLLLL 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 93-231 4.76e-06

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.06  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323  93 KPLKIWSAACSTGeepyTLAMLLDQqksLPGFQILATDIDEKALEKAKKgvyqerslqevpssvkdryftqnanrsyEVK 172
Cdd:COG0500   26 KGGRVLDLGCGTG----RNLLALAA---RFGGRVIGIDLSPEAIALARA----------------------------RAA 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124494323 173 AEIKKNITFKKHNL--LADRYEQDFDLIVCRNVFIYFTESAKEELYLKMAHSLKKNGVLFV 231
Cdd:COG0500   71 KAGLGNVEFLVADLaeLDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 119-200 1.53e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.99  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124494323 119 KSLPGFQILATDIDEKALEKAKKgvyqerslqevpssvkdryftqNAnrsyevKAEIKKNITFKKHNLLADRYEQDFDLI 198
Cdd:PRK09328 128 KERPDAEVTAVDISPEALAVARR----------------------NA------KHGLGARVEFLQGDWFEPLPGGRFDLI 179


                 ..
gi 124494323 199 VC 200
Cdd:PRK09328 180 VS 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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