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Conserved domains on  [gi|2711983576|ref|WP_339394141|]
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CheR family methyltransferase, partial [Brevibacterium metallidurans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10611 super family cl35932
protein-glutamate O-methyltransferase CheR;
1-164 6.19e-123

protein-glutamate O-methyltransferase CheR;


The actual alignment was detected with superfamily member PRK10611:

Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 347.11  E-value: 6.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   1 ASTGEEPYSIAITFGDALGERLSSSQIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGTGPHQGLVRVRQELA 80
Cdd:PRK10611  124 ASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  81 TRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQTVYGL 160
Cdd:PRK10611  204 NYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283


                  ....
gi 2711983576 161 TKEK 164
Cdd:PRK10611  284 SKDR 287
 
Name Accession Description Interval E-value
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
1-164 6.19e-123

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 347.11  E-value: 6.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   1 ASTGEEPYSIAITFGDALGERLSSSQIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGTGPHQGLVRVRQELA 80
Cdd:PRK10611  124 ASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  81 TRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQTVYGL 160
Cdd:PRK10611  204 NYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283


                  ....
gi 2711983576 161 TKEK 164
Cdd:PRK10611  284 SKDR 287
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 1-158 2.87e-63

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: 195.20  E-value: 2.87e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576    1 ASTGEEPYSIAITFGDALG-ERLSSSQIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGtgphQGLVRVRQEL 79
Cdd:smart00138 108 CSTGEEPYSLAMLLAETLPkGREPDVKILATDIDLKALEKARAGIYPERELEDLPKALLARYFKEV----EDKYRVKPEL 183

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2711983576   80 ATRVNFQPLNLLAPeWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQTVY 158
Cdd:smart00138 184 KERVRFAKHNLLAE-SPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFLGHSESLPGLTDKFEPIEGTVY 261
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
2-150 3.91e-60

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 187.29  E-value: 3.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   2 STGEEPYSIAITFGDALGERLSSS-QIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRgtgpHQGLVRVRQELA 80
Cdd:COG1352   112 STGEEPYSLAMLLAEAGGELAGWRvEILATDISEEALEKARAGIYPERSLRGLPPEYLSRYFTK----EGGRYRIKPELR 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  81 TRVNFQPLNLLAPEWALpGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDF 150
Cdd:COG1352   188 EMVTFAQHNLLDDPPPF-GRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESLGGLSDLF 256
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 2-155 4.71e-58

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: 179.40  E-value: 4.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   2 STGEEPYSIAITFGDALGERLSSS-QIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGTGPHQglvRVRQELA 80
Cdd:pfam01739  40 SSGEEPYSLAMLLKETFPNAARWDfKILATDIDLSVLEKARAGVYPERELEGLPEELLRRYFEKTAGGGY---TVKPEIK 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2711983576  81 TRVNFQPLNLLApEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQ 155
Cdd:pfam01739 117 SMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKILNRFAEKLKPGGYLFLGHSEALPGNPDKFKKVGS 190
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-136 7.03e-06

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: 7.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2711983576  74 RVRQELATRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFdKPTQERILRRFVPLLKPGGLLF 136
Cdd:cd02440    40 AAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
1-164 6.19e-123

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 347.11  E-value: 6.19e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   1 ASTGEEPYSIAITFGDALGERLSSSQIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGTGPHQGLVRVRQELA 80
Cdd:PRK10611  124 ASTGEEPYSIAMTLADTLGTAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQELA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  81 TRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQTVYGL 160
Cdd:PRK10611  204 NYVDFQQLNLLAKQWAVPGPFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSENFSQLSREFYLRGQTVYGL 283


                  ....
gi 2711983576 161 TKEK 164
Cdd:PRK10611  284 SKDR 287
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 1-158 2.87e-63

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: 195.20  E-value: 2.87e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576    1 ASTGEEPYSIAITFGDALG-ERLSSSQIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGtgphQGLVRVRQEL 79
Cdd:smart00138 108 CSTGEEPYSLAMLLAETLPkGREPDVKILATDIDLKALEKARAGIYPERELEDLPKALLARYFKEV----EDKYRVKPEL 183

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2711983576   80 ATRVNFQPLNLLAPeWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQTVY 158
Cdd:smart00138 184 KERVRFAKHNLLAE-SPPLGDFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFLGHSESLPGLTDKFEPIEGTVY 261
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
2-150 3.91e-60

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 187.29  E-value: 3.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   2 STGEEPYSIAITFGDALGERLSSS-QIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRgtgpHQGLVRVRQELA 80
Cdd:COG1352   112 STGEEPYSLAMLLAEAGGELAGWRvEILATDISEEALEKARAGIYPERSLRGLPPEYLSRYFTK----EGGRYRIKPELR 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  81 TRVNFQPLNLLAPEWALpGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDF 150
Cdd:COG1352   188 EMVTFAQHNLLDDPPPF-GRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESLGGLSDLF 256
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 2-155 4.71e-58

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: 179.40  E-value: 4.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576   2 STGEEPYSIAITFGDALGERLSSS-QIWASDIDTQVLEKAEAGIYRHEDLRTLTPAQMQRYFLRGTGPHQglvRVRQELA 80
Cdd:pfam01739  40 SSGEEPYSLAMLLKETFPNAARWDfKILATDIDLSVLEKARAGVYPERELEGLPEELLRRYFEKTAGGGY---TVKPEIK 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2711983576  81 TRVNFQPLNLLApEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFAGHSENFSQISRDFYLRGQ 155
Cdd:pfam01739 117 SMVLFEYLNLLD-EYPPLGDFDVIFCRNVLIYFDEETQRKILNRFAEKLKPGGYLFLGHSEALPGNPDKFKKVGS 190
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 58-136 4.99e-08

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: 48.86  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  58 MQRYFLRGTG--PHQGLVRVRQELATRVNFQPLNLLAPEWALP-GPFDAIFCRNVMIYFDKPtqERILRRFVPLLKPGGL 134
Cdd:COG2227    42 LARRGADVTGvdISPEALEIARERAAELNVDFVQGDLEDLPLEdGSFDLVICSEVLEHLPDP--AALLRELARLLKPGGL 119


                  ..
gi 2711983576 135 LF 136
Cdd:COG2227   120 LL 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
77-137 2.95e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.36  E-value: 2.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2711983576  77 QELATRVNFQPLNLLapEWALPGPFDAIFCRNVMIYFdkPTQERILRRFVPLLKPGGLLFA 137
Cdd:COG4106    42 RARLPNVRFVVADLR--DLDPPEPFDLVVSNAALHWL--PDHAALLARLAAALAPGGVLAV 98
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 13-135 3.18e-07

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 46.21  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  13 TFGDALGERLSSSQIWASDIDTQVLEKAEagiyrhedlrtltpaqmQRyflrgtgphqgLVRVRQELATRVNFQPLNLLA 92
Cdd:pfam08242   9 TLLRALLEALPGLEYTGLDISPAALEAAR-----------------ER-----------LAALGLLNAVRVELFQLDLGE 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2711983576  93 PEwalPGPFDAIFCRNVMIYFDKPtqERILRRFVPLLKPGGLL 135
Cdd:pfam08242  61 LD---PGSFDVVVASNVLHHLADP--RAVLRNIRRLLKPGGVL 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 82-133 4.11e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 45.63  E-value: 4.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2711983576  82 RVNFQPLNLLAPEWAlPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGG 133
Cdd:pfam13649  46 NVEFVQGDAEDLPFP-DGSFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-136 7.03e-06

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: 7.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2711983576  74 RVRQELATRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFdKPTQERILRRFVPLLKPGGLLF 136
Cdd:cd02440    40 AAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHL-VEDLARFLEEARRLLKPGGVLV 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 74-136 9.72e-06

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 9.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2711983576  74 RVRQE-LATRVNFQPLNLLapEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLF 136
Cdd:COG2230    93 RAAEAgLADRVEVRLADYR--DLPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-163 1.34e-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: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  74 RVRQELATRVNFQPLNLLAPEWALPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGLLFaghsenFSQISRDFYLR 153
Cdd:COG0500    68 RAAKAGLGNVEFLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLL------LSASDAAAALS 141

                          90
                  ....*....|
gi 2711983576 154 GQTVYGLTKE 163
Cdd:COG0500   142 LARLLLLATA 151
DUF938 pfam06080
Protein of unknown function (DUF938); This family consists of several hypothetical proteins ...
 55-150 2.30e-04

Protein of unknown function (DUF938); This family consists of several hypothetical proteins from both prokaryotes and eukaryotes. The function of this family is unknown.


Pssm-ID: 253548  Cd Length: 201  Bit Score: 39.75  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2711983576  55 PAQMQRYFLRGTGPHQGLVRVRQELATRVNFQPLNLLAPewaLPGPFDAIFCRNVMIYFDKPTQERILRRFVPLLKPGGL 134
Cdd:pfam06080  57 PDPNLRGSIAAWADQQGLRNLRPPLHLDVTRPPWPVEAP---APASYDAIFSINMIHISPWSCVEGLFRGAGRLLPPGGV 133

                          90       100
                  ....*....|....*....|.
gi 2711983576 135 L-----FAGHSENFSQISRDF 150
Cdd:pfam06080 134 LyiygpYNQDGELTSDSNRDF 154
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
96-160 1.10e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2711983576  96 ALPGPFDAIFCRNVMIYFDKPtqERILRRFVPLLKPGGLLF----AGHSENFSQISRDFYLR-----GQTVYGL 160
Cdd:COG4976   103 EPDGRFDLIVAADVLTYLGDL--AAVFAGVARALKPGGLFIfsveDADGSGRYAHSLDYVRDllaaaGFEVPGL 174
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 101-136 1.16e-03

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.49  E-value: 1.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2711983576 101 FDAIFCRNVMIYFDKPtqERILRRFVPLLKPGGLLF 136
Cdd:pfam08241  60 FDLVLSSEVLHHVEDP--ERALREIARVLKPGGILI 93
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 96-136 2.16e-03

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: 36.51  E-value: 2.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2711983576  96 ALP---GPFDAIFCRNVMIYFDKPtqERILRRFVPLLKPGGLLF 136
Cdd:COG2226    80 DLPfpdGSFDLVISSFVLHHLPDP--ERALAEIARVLKPGGRLV 121
 
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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