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Conserved domains on  [gi|488617917|ref|WP_002554766|]
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MULTISPECIES: protein-glutamate O-methyltransferase CheR [Pseudomonas]

Protein Classification

CheR family methyltransferase( domain architecture ID 11442594)

CheR family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as chemotaxis protein methyltransferase that methylates membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:1904047
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
7-262 2.02e-83

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


:

Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 256.63  E-value: 2.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   7 RFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSPQEQQALIEAVIVPETWFFRYPESFVTLG-ML 85
Cdd:COG1352   11 RLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEALReEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  86 ARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAG--VDARQFKVDAIDISPFSIAKAEHGIYGKNSFRGSDTGFRE 163
Cdd:COG1352   91 LPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGgeLAGWRVEILATDISEEALEKARAGIYPERSLRGLPPEYLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 164 RYFNPVADGFEIADSVRACVSFQAGNLLDPKlASQVAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPAEGN 243
Cdd:COG1352  171 RYFTKEGGRYRIKPELREMVTFAQHNLLDDP-PPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESL 249
                        250
                 ....*....|....*....
gi 488617917 244 LLAGIGMRSIGIAQSFAFR 262
Cdd:COG1352  250 GGLSDLFEPVDKKGRFIYR 268
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
334-420 1.35e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.17  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 334 LANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSESLAQLAALLAAQGDSAGARR 413
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKA 143

                 ....*..
gi 488617917 414 LQDRAAR 420
Cdd:COG5010  144 ALQRALG 150
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
7-262 2.02e-83

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 256.63  E-value: 2.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   7 RFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSPQEQQALIEAVIVPETWFFRYPESFVTLG-ML 85
Cdd:COG1352   11 RLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEALReEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  86 ARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAG--VDARQFKVDAIDISPFSIAKAEHGIYGKNSFRGSDTGFRE 163
Cdd:COG1352   91 LPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGgeLAGWRVEILATDISEEALEKARAGIYPERSLRGLPPEYLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 164 RYFNPVADGFEIADSVRACVSFQAGNLLDPKlASQVAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPAEGN 243
Cdd:COG1352  171 RYFTKEGGRYRIKPELREMVTFAQHNLLDDP-PPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESL 249
                        250
                 ....*....|....*....
gi 488617917 244 LLAGIGMRSIGIAQSFAFR 262
Cdd:COG1352  250 GGLSDLFEPVDKKGRFIYR 268
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
4-241 3.73e-51

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: 173.24  E-value: 3.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917     4 DDSRFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSP--QEQQALIEAVIVPETWFFRYPESFVT 81
Cdd:smart00138   3 DFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRgeEELAELLDLMTTNETRFFRESKHFEA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917    82 L-GMLARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAGVDARQFKVD--AIDISPFSIAKAEHGIYGKNSFRGSD 158
Cdd:smart00138  83 LeEKVLPLLIASRRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKilATDIDLKALEKARAGIYPERELEDLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   159 TGFRERYFNPVADGFEIADSVRACVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIG 238
Cdd:smart00138 163 KALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLG-DFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFLG 241

                   ...
gi 488617917   239 PAE 241
Cdd:smart00138 242 HSE 244
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
69-241 2.18e-40

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: 142.42  E-value: 2.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   69 ETWFFRYPESFVTLGMLARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAGVDA--RQFKVDAIDISPFSIAKAEH 146
Cdd:pfam01739   2 ETRFFREPAHFEELKKYVLPLLAKAKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAarWDFKILATDIDLSVLEKARA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  147 GIYGKNSFRGSDTGFRERYFNP-VADGFEIADSVRACVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRQTQQHVFKVL 225
Cdd:pfam01739  82 GVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLDEYPPLG-DFDVIFCRNVLIYFDEETQRKILNRF 160
                         170
                  ....*....|....*.
gi 488617917  226 KQLTREDGLLFIGPAE 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSE 176
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
47-241 9.45e-31

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 119.45  E-value: 9.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  47 YWHLLVSSPQ--EQQALIEAVIVPETWFFRYPESFVTLGMLARERIASLagvrplRILSLPCSTGEEPYSIAMALFDA-G 123
Cdd:PRK10611  69 YLALLESNQNsaEWQAFINALTTNLTAFFREAHHFPILAEHARRRSGEY------RVWSAAASTGEEPYSIAMTLADTlG 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 124 VDARQFKVDAIDISPFSIAKAEHGIYGKNSFRGSDTGFRERYFNPVADGFEIADSVRA----CVSFQAGNLLDPKLASQV 199
Cdd:PRK10611 143 TAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQelanYVDFQQLNLLAKQWAVPG 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488617917 200 AYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPAE 241
Cdd:PRK10611 223 PFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
334-420 1.35e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.17  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 334 LANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSESLAQLAALLAAQGDSAGARR 413
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKA 143

                 ....*..
gi 488617917 414 LQDRAAR 420
Cdd:COG5010  144 ALQRALG 150
 
Name Accession Description Interval E-value
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
7-262 2.02e-83

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


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 256.63  E-value: 2.02e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   7 RFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSPQEQQALIEAVIVPETWFFRYPESFVTLG-ML 85
Cdd:COG1352   11 RLLELLRERTGIDLSDYKRALLERRLERRMRALGLDSFSEYLELLRSDPEELQALIDALTINVTEFFRDPEHFEALReEV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  86 ARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAG--VDARQFKVDAIDISPFSIAKAEHGIYGKNSFRGSDTGFRE 163
Cdd:COG1352   91 LPELLARRRAGRPLRIWSAGCSTGEEPYSLAMLLAEAGgeLAGWRVEILATDISEEALEKARAGIYPERSLRGLPPEYLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 164 RYFNPVADGFEIADSVRACVSFQAGNLLDPKlASQVAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPAEGN 243
Cdd:COG1352  171 RYFTKEGGRYRIKPELREMVTFAQHNLLDDP-PPFGRFDLIFCRNVLIYFDPELQRRVLRRFHDSLAPGGYLFLGHSESL 249
                        250
                 ....*....|....*....
gi 488617917 244 LLAGIGMRSIGIAQSFAFR 262
Cdd:COG1352  250 GGLSDLFEPVDKKGRFIYR 268
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
4-241 3.73e-51

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: 173.24  E-value: 3.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917     4 DDSRFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSP--QEQQALIEAVIVPETWFFRYPESFVT 81
Cdd:smart00138   3 DFRRFCVLIYSRTGIVLTDYKRTLLQSRLSRRLRVLGLKDFSEYLELLTSHRgeEELAELLDLMTTNETRFFRESKHFEA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917    82 L-GMLARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAGVDARQFKVD--AIDISPFSIAKAEHGIYGKNSFRGSD 158
Cdd:smart00138  83 LeEKVLPLLIASRRHGRRVRIWSAGCSTGEEPYSLAMLLAETLPKGREPDVKilATDIDLKALEKARAGIYPERELEDLP 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   159 TGFRERYFNPVADGFEIADSVRACVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIG 238
Cdd:smart00138 163 KALLARYFKEVEDKYRVKPELKERVRFAKHNLLAESPPLG-DFDLIFCRNVLIYFDEPTQRKLLNRFAEALKPGGYLFLG 241

                   ...
gi 488617917   239 PAE 241
Cdd:smart00138 242 HSE 244
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
69-241 2.18e-40

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: 142.42  E-value: 2.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917   69 ETWFFRYPESFVTLGMLARERIASLAGVRPLRILSLPCSTGEEPYSIAMALFDAGVDA--RQFKVDAIDISPFSIAKAEH 146
Cdd:pfam01739   2 ETRFFREPAHFEELKKYVLPLLAKAKNGKRVRIWSAGCSSGEEPYSLAMLLKETFPNAarWDFKILATDIDLSVLEKARA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  147 GIYGKNSFRGSDTGFRERYFNP-VADGFEIADSVRACVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRQTQQHVFKVL 225
Cdd:pfam01739  82 GVYPERELEGLPEELLRRYFEKtAGGGYTVKPEIKSMVLFEYLNLLDEYPPLG-DFDVIFCRNVLIYFDEETQRKILNRF 160
                         170
                  ....*....|....*.
gi 488617917  226 KQLTREDGLLFIGPAE 241
Cdd:pfam01739 161 AEKLKPGGYLFLGHSE 176
PRK10611 PRK10611
protein-glutamate O-methyltransferase CheR;
47-241 9.45e-31

protein-glutamate O-methyltransferase CheR;


Pssm-ID: 236725 [Multi-domain]  Cd Length: 287  Bit Score: 119.45  E-value: 9.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  47 YWHLLVSSPQ--EQQALIEAVIVPETWFFRYPESFVTLGMLARERIASLagvrplRILSLPCSTGEEPYSIAMALFDA-G 123
Cdd:PRK10611  69 YLALLESNQNsaEWQAFINALTTNLTAFFREAHHFPILAEHARRRSGEY------RVWSAAASTGEEPYSIAMTLADTlG 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 124 VDARQFKVDAIDISPFSIAKAEHGIYGKNSFRGSDTGFRERYFNPVADGFEIADSVRA----CVSFQAGNLLDPKLASQV 199
Cdd:PRK10611 143 TAPGRWKVFASDIDTEVLEKARSGIYRQEELKTLSPQQLQRYFMRGTGPHEGLVRVRQelanYVDFQQLNLLAKQWAVPG 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 488617917 200 AYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPAE 241
Cdd:PRK10611 223 PFDAIFCRNVMIYFDKTTQERILRRFVPLLKPDGLLFAGHSE 264
CheR_N pfam03705
CheR methyltransferase, all-alpha domain; CheR proteins are part of the chemotaxis signaling ...
7-55 6.68e-05

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: 40.11  E-value: 6.68e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 488617917    7 RFFSFLKERIGLDVTSVGEAIIERALRQRATAAHCPDSDAYWHLLVSSP 55
Cdd:pfam03705   5 RLLELIYRRTGIDLSDYKRSLLERRLSRRMRALGLDSFSEYLDLLRSDP 53
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
97-240 6.74e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  97 RPLRILSLPCSTGEepYSIAMAlfdagvDARQFKVDAIDISPFSIAKAehgiygknsfrgsdtgfRERyfnpvADGFEIA 176
Cdd:COG0500   26 KGGRVLDLGCGTGR--NLLALA------ARFGGRVIGIDLSPEAIALA-----------------RAR-----AAKAGLG 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488617917 177 DsvracVSFQAGNLLDPKLASQVAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFIGPA 240
Cdd:COG0500   76 N-----VEFLVADLAELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSAS 134
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
88-237 1.04e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.61  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  88 ERIASLAGVRP-LRILSLPCSTGeepysiAMALFDAGvdARQFKVDAIDISPFSIAKAehgiygknsfrgsdtgfRERyf 166
Cdd:COG2230   41 DLILRKLGLKPgMRVLDIGCGWG------GLALYLAR--RYGVRVTGVTLSPEQLEYA-----------------RER-- 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617917 167 npvADGFEIADSVRacvsFQAGNLLDpkLASQVAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDGLLFI 237
Cdd:COG2230   94 ---AAEAGLADRVE----VRLADYRD--LPADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
334-420 1.35e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.17  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 334 LANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSESLAQLAALLAAQGDSAGARR 413
Cdd:COG5010   64 YNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKA 143

                 ....*..
gi 488617917 414 LQDRAAR 420
Cdd:COG5010  144 ALQRALG 150
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
322-393 2.09e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.36  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617917 322 SEVSALLDRIAGLANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSE 393
Cdd:COG3914  110 DNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAE 181
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
86-237 2.37e-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: 38.05  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  86 ARERIASLAGVRP-LRILSLPCSTGEepYSIAMAlfdagvdARQFKVDAIDISPFSIAKAEHgiygknsfRGSDTGFRer 164
Cdd:COG2226   10 GREALLAALGLRPgARVLDLGCGTGR--LALALA-------ERGARVTGVDISPEMLELARE--------RAAEAGLN-- 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617917 165 yfnpvadgfeiadsvracVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRqtQQHVFKVLKQLTREDGLLFI 237
Cdd:COG2226   71 ------------------VEFVVGDAEDLPFPDG-SFDLVISSFVLHHLPD--PERALAEIARVLKPGGRLVV 122
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
324-427 3.51e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 324 VSALLDRIAGLANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSESLAQLAALLA 403
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALR 225
                         90       100
                 ....*....|....*....|....
gi 488617917 404 AQGDSAGARRLQDRAARGANKQGN 427
Cdd:COG3914  226 QACDWEVYDRFEELLAALARGPSE 249
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
334-423 3.85e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.83  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 334 LANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFYRKALYLQPQHSESLAQLAALLAAQGDSAGARR 413
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165
                         90
                 ....*....|
gi 488617917 414 LQDRAARGAN 423
Cdd:COG0457  166 LLEKLEAAAL 175
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
334-420 4.89e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917 334 LANEGKSAEAQAACERYLQQHEPVAQVFYWLGLLSEVEGSVAQAQGFyRKALYLQPQHSESLAQLAALLAAQGDSAGARR 413
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                 ....*..
gi 488617917 414 LQDRAAR 420
Cdd:COG3063   81 YLERALE 87
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
101-233 5.47e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.00  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617917  101 ILSLPCSTGEepYSIAMAlfdagvDARQFKVDAIDISPFSIAKAEHgiygknsfRGSDTGFReryfnpvadgfeiadsvr 180
Cdd:pfam13649   1 VLDLGCGTGR--LTLALA------RRGGARVTGVDLSPEMLERARE--------RAAEAGLN------------------ 46
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488617917  181 acVSFQAGNLLDPKLASQvAYDIVFCRNLVIYFDRQTQQHVFKVLKQLTREDG 233
Cdd:pfam13649  47 --VEFVQGDAEDLPFPDG-SFDLVVSSGVLHHLPDPDLEAALREIARVLKPGG 96
 
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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