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Conserved domains on  [gi|1285033090|pdb|5NEN|B]
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Chain B, Lipase C

Protein Classification

putative HlyD family type I secretion protein( domain architecture ID 1000742)

putative HlyD family type I secretion protein similar to Escherichia coli hemolysin secretion protein D, an inner membrane protein involved in the transport of hemolysin A

Gene Ontology:  GO:0016020|GO:0005886|GO:0009306
TCDB:  8.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CusB_dom_1 super family cl46872
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 23-422 1.81e-106

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


The actual alignment was detected with superfamily member TIGR01843:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 423  Bit Score: 321.96  E-value: 1.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAE 102
Cdd:TIGR01843  24 FAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        103 RDGLSIVTFSPILDAVKDkPRVAEIIALQTQLFASRRQALQSEIDGYKQSMDGIRFQLKGLQ-DSRGNKQiQLSSLREQM 181
Cdd:TIGR01843 104 ADSQAAIEFPDDLLSAED-PAVPELIKGQQSLFESRKSTLRAQLELILAQIKQLEAELAGLQaQLQALRQ-QLEVISEEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        182 NSMKQLAADGYLPRNRYLEVQRQFAEVNSSIDETVGRIGQLQKQLLESQQRIDQRFADYQREVRTQLAQTQMDASEFRNK 261
Cdd:TIGR01843 182 EARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRER 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        262 LQMADFDLGNTAITSPVDGTVVGLNIFTQGGVVGAGDHLMDVVPSQATLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQNK 341
Cdd:TIGR01843 262 LNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        342 TPKIPGTVTLVSADRLVDKANGEPYYqmQVTVSPEGMKMLSGED---IKPGMPVEVFVKTGSRSLLSYLFKPILDRAHTS 418
Cdd:TIGR01843 342 YGILNGKVKSISPDTFTDERGGGPYY--RVRISIDQNTLGIGPKgleLSPGMPVTADIKTGERTVIEYLLKPITDSVQEA 419


                  ....
5NEN_B        419 LTEE 422
Cdd:TIGR01843 420 LRER 423
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 23-422 1.81e-106

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 321.96  E-value: 1.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAE 102
Cdd:TIGR01843  24 FAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        103 RDGLSIVTFSPILDAVKDkPRVAEIIALQTQLFASRRQALQSEIDGYKQSMDGIRFQLKGLQ-DSRGNKQiQLSSLREQM 181
Cdd:TIGR01843 104 ADSQAAIEFPDDLLSAED-PAVPELIKGQQSLFESRKSTLRAQLELILAQIKQLEAELAGLQaQLQALRQ-QLEVISEEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        182 NSMKQLAADGYLPRNRYLEVQRQFAEVNSSIDETVGRIGQLQKQLLESQQRIDQRFADYQREVRTQLAQTQMDASEFRNK 261
Cdd:TIGR01843 182 EARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRER 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        262 LQMADFDLGNTAITSPVDGTVVGLNIFTQGGVVGAGDHLMDVVPSQATLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQNK 341
Cdd:TIGR01843 262 LNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        342 TPKIPGTVTLVSADRLVDKANGEPYYqmQVTVSPEGMKMLSGED---IKPGMPVEVFVKTGSRSLLSYLFKPILDRAHTS 418
Cdd:TIGR01843 342 YGILNGKVKSISPDTFTDERGGGPYY--RVRISIDQNTLGIGPKgleLSPGMPVTADIKTGERTVIEYLLKPITDSVQEA 419


                  ....
5NEN_B        419 LTEE 422
Cdd:TIGR01843 420 LRER 423
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 23-378 6.83e-82

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 255.43  E-value: 6.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAE 102
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        103 RDglsivtfspildavkdkprvaeiialqtqlfasRRQALQSEIDGYKQSMDGIRFQLKGLQDSRGNKQIQLSSLREQMN 182
Cdd:pfam00529  81 LD---------------------------------RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        183 SMKQLAADGYLPRNRYLEVQRQFAEVNSSIDETVGRIGQLQKQllesqqrIDQRFADYQREVRTQLAQTQMDASEFRNKL 262
Cdd:pfam00529 128 RRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQ-------ITQSAAENQAEVRSELSGAQLQIAEAEAEL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        263 QMADFDLGNTAITSPVDGTVVGLNIFTQGGVVGAGDHLMDVVPSQaTLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQNKT 342
Cdd:pfam00529 201 KLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVPED-NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKT 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
5NEN_B        343 PKIPGTVTLVSAD----RLVDKANGEPYYQMQVTVSPEGM 378
Cdd:pfam00529 280 GRFTGVVVGISPDtgpvRVVVDKAQGPYYPLRIGLSAGAL 319
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
23-399 1.93e-38

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 142.11  E-value: 1.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B       23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRdqyyttlategrllae 102
Cdd:COG1566  26 AGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAE---------------- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      103 rdglsivtfspildavkdkprvAEIIALQTQLfasrrQALQSEIdgykqsmdGIRFQLKGLQDSRGNKQIQLSSLREQMN 182
Cdd:COG1566  90 ----------------------AQLAAAEAQL-----ARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQRELE 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      183 SMKQLAADGYLPRNRYLEVQRQFaevnssiDETVGRIGQLQKQLLESQQRIDQRfadyqrevrTQLAQTQMDASEFRNKL 262
Cdd:COG1566 135 RYQALYKKGAVSQQELDEARAAL-------DAAQAQLEAAQAQLAQAQAGLREE---------EELAAAQAQVAQAEAAL 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      263 QMADFDLGNTAITSPVDGTVVGLNIfTQGGVVGAGDHLMDVVPSQAtLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQnkt 342
Cdd:COG1566 199 AQAELNLARTTIRAPVDGVVTNLNV-EPGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGRVKPGQPVEVRVDAYPD--- 273

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5NEN_B      343 PKIPGTVTLVSADRLVDKA------NGEPYYQMQVTVSPEgmkmlSGEDIKPGMPVEVFVKTG 399
Cdd:COG1566 274 RVFEGKVTSISPGAGFTSPpknatgNVVQRYPVRIRLDNP-----DPEPLRPGMSATVEIDTE 331
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 44-73 2.60e-05

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 42.02  E-value: 2.60e-05
                        10        20        30
                ....*....|....*....|....*....|
5NEN_B       44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:cd06850  38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 36-80 2.46e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.19  E-value: 2.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
5NEN_B        36 VTVSGNRKTVQ--APASGIIKNIAVRDGDKVKAGEVLVQLsQVQAQA 80
Cdd:PRK11855 153 ITVETDKATMEipSPVAGVVKEIKVKVGDKVSVGSLLVVI-EVAAAA 198
 
Name Accession Description Interval E-value
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 23-422 1.81e-106

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 321.96  E-value: 1.81e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAE 102
Cdd:TIGR01843  24 FAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        103 RDGLSIVTFSPILDAVKDkPRVAEIIALQTQLFASRRQALQSEIDGYKQSMDGIRFQLKGLQ-DSRGNKQiQLSSLREQM 181
Cdd:TIGR01843 104 ADSQAAIEFPDDLLSAED-PAVPELIKGQQSLFESRKSTLRAQLELILAQIKQLEAELAGLQaQLQALRQ-QLEVISEEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        182 NSMKQLAADGYLPRNRYLEVQRQFAEVNSSIDETVGRIGQLQKQLLESQQRIDQRFADYQREVRTQLAQTQMDASEFRNK 261
Cdd:TIGR01843 182 EARRKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRER 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        262 LQMADFDLGNTAITSPVDGTVVGLNIFTQGGVVGAGDHLMDVVPSQATLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQNK 341
Cdd:TIGR01843 262 LNKARDRLQRLIIRSPVDGTVQSLKVHTVGGVVQPGETLMEIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        342 TPKIPGTVTLVSADRLVDKANGEPYYqmQVTVSPEGMKMLSGED---IKPGMPVEVFVKTGSRSLLSYLFKPILDRAHTS 418
Cdd:TIGR01843 342 YGILNGKVKSISPDTFTDERGGGPYY--RVRISIDQNTLGIGPKgleLSPGMPVTADIKTGERTVIEYLLKPITDSVQEA 419


                  ....
5NEN_B        419 LTEE 422
Cdd:TIGR01843 420 LRER 423
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 23-378 6.83e-82

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 255.43  E-value: 6.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAE 102
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        103 RDglsivtfspildavkdkprvaeiialqtqlfasRRQALQSEIDGYKQSMDGIRFQLKGLQDSRGNKQIQLSSLREQMN 182
Cdd:pfam00529  81 LD---------------------------------RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        183 SMKQLAADGYLPRNRYLEVQRQFAEVNSSIDETVGRIGQLQKQllesqqrIDQRFADYQREVRTQLAQTQMDASEFRNKL 262
Cdd:pfam00529 128 RRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQ-------ITQSAAENQAEVRSELSGAQLQIAEAEAEL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        263 QMADFDLGNTAITSPVDGTVVGLNIFTQGGVVGAGDHLMDVVPSQaTLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQNKT 342
Cdd:pfam00529 201 KLAKLDLERTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFVVPED-NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKT 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
5NEN_B        343 PKIPGTVTLVSAD----RLVDKANGEPYYQMQVTVSPEGM 378
Cdd:pfam00529 280 GRFTGVVVGISPDtgpvRVVVDKAQGPYYPLRIGLSAGAL 319
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
23-399 1.93e-38

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 142.11  E-value: 1.93e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B       23 FTRLDKGVASPGSVTVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRdqyyttlategrllae 102
Cdd:COG1566  26 AGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAE---------------- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      103 rdglsivtfspildavkdkprvAEIIALQTQLfasrrQALQSEIdgykqsmdGIRFQLKGLQDSRGNKQIQLSSLREQMN 182
Cdd:COG1566  90 ----------------------AQLAAAEAQL-----ARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQRELE 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      183 SMKQLAADGYLPRNRYLEVQRQFaevnssiDETVGRIGQLQKQLLESQQRIDQRfadyqrevrTQLAQTQMDASEFRNKL 262
Cdd:COG1566 135 RYQALYKKGAVSQQELDEARAAL-------DAAQAQLEAAQAQLAQAQAGLREE---------EELAAAQAQVAQAEAAL 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      263 QMADFDLGNTAITSPVDGTVVGLNIfTQGGVVGAGDHLMDVVPSQAtLVVDSRLKVDLFDKVYNGLPVDLMFTAFNQnkt 342
Cdd:COG1566 199 AQAELNLARTTIRAPVDGVVTNLNV-EPGEVVSAGQPLLTIVPLDD-LWVEAYVPETDLGRVKPGQPVEVRVDAYPD--- 273

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5NEN_B      343 PKIPGTVTLVSADRLVDKA------NGEPYYQMQVTVSPEgmkmlSGEDIKPGMPVEVFVKTG 399
Cdd:COG1566 274 RVFEGKVTSISPGAGFTSPpknatgNVVQRYPVRIRLDNP-----DPEPLRPGMSATVEIDTE 331
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 30-401 1.39e-13

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 71.51  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B       30 VASPGSVTVSgNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQYYTTLAtegrllaerdglsiv 109
Cdd:COG0845  12 VEATGTVEAR-REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQA--------------- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      110 tfspildavkdkprvaeiialqtqlfasrrqalqseidgykqsmdgirfqlkglqdsrgnkqiQLSSLREQMNSMKQLAA 189
Cdd:COG0845  76 ---------------------------------------------------------------QLELAKAELERYKALLK 92

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      190 DGYLprnrylevqrqfaevnssidetvgrigqlqkqlleSQQRIDQRFADYQRevrtqlAQTQMDASefRNKLQMADFDL 269
Cdd:COG0845  93 KGAV-----------------------------------SQQELDQAKAALDQ------AQAALAAA--QAALEQARANL 129

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      270 GNTAITSPVDGTVVGLNIfTQGGVVGAGDHLmdvvpsqATLVVDSRLKVDL------FDKVYNGLPVDLMFTAFnqnKTP 343
Cdd:COG0845 130 AYTTIRAPFDGVVGERNV-EPGQLVSAGTPL-------FTIADLDPLEVEFdvpesdLARLKVGQPVTVTLDAG---PGK 198

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
5NEN_B      344 KIPGTVTLVSADrlVDKANGepYYQMQVTVSPEGMKmlsgedIKPGMPVEVFVKTGSR 401
Cdd:COG0845 199 TFEGKVTFIDPA--VDPATR--TVRVRAELPNPDGL------LRPGMFVRVRIVLGER 246
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 274-389 3.49e-09

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 53.91  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B        274 ITSPVDGTVVGLNIfTQGGVVGAGDHLMDVVPsQATLVVDSRLKVDLFDKVYNGLPVDLmftAFNQNKTPKIPGTVTLVS 353
Cdd:pfam13437   2 IRAPVDGVVAELNV-EEGQVVQAGDPLATIVP-PDRLLVEAFVPAADLGSLKKGQKVTL---KLDPGSDYTLEGKVVRIS 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
5NEN_B        354 ADrlVDKANGepYYQMQVTVSPEGMkmlsGEDIKPG 389
Cdd:pfam13437  77 PT--VDPDTG--VIPVRVSIENPKT----PIPLLPG 104
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
44-88 3.90e-06

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 43.59  E-value: 3.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
5NEN_B         44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQ 88
Cdd:pfam13533   4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQ 48
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 33-89 1.08e-05

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 47.31  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
5NEN_B         33 PGSVtVSGNRKTVQAPASGIIKNIAVRDGDKVKAGEVLVQLSQVQAQAQVDSLRDQY 89
Cdd:TIGR01730  18 PGSL-EAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQL 73
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 44-73 2.60e-05

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 42.02  E-value: 2.60e-05
                        10        20        30
                ....*....|....*....|....*....|
5NEN_B       44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:cd06850  38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 44-82 3.98e-04

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 41.72  E-value: 3.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
5NEN_B         44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQ---LSQVQAQAQV 82
Cdd:pfam16576 110 TVYAPISGVVTELNVREGMYVQPGDTLFTiadLSTVWVEADV 151
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 44-73 1.38e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 41.22  E-value: 1.38e-03
                         10        20        30
                 ....*....|....*....|....*....|
5NEN_B        44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:COG1038 1115 TITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 36-80 2.46e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.19  E-value: 2.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
5NEN_B        36 VTVSGNRKTVQ--APASGIIKNIAVRDGDKVKAGEVLVQLsQVQAQA 80
Cdd:PRK11855 153 ITVETDKATMEipSPVAGVVKEIKVKVGDKVSVGSLLVVI-EVAAAA 198
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
126-263 3.03e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 3.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B      126 EIIALQTQLFASRRQ------ALQSEIDGYKQSMDGIRFQLKGLQDSRGNKQIQLSSLREQMNSMKQLAADGYLPRNRYL 199
Cdd:COG1340  33 ELNEELKELAEKRDElnaqvkELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSID 112

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5NEN_B      200 EVQRQFAEV-----NSSID-----ETVGRIGQLQKQLLESQQRIDQRfaDYQREVRTQLAQTQMDASEFRNKLQ 263
Cdd:COG1340 113 KLRKEIERLewrqqTEVLSpeeekELVEKIKELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIK 184
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 45-73 3.33e-03

Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 36.23  E-value: 3.33e-03
                        10        20
                ....*....|....*....|....*....
5NEN_B       45 VQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:cd06849  46 VEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 44-73 4.09e-03

Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.


Pssm-ID: 395290 [Multi-domain]  Cd Length: 73  Bit Score: 36.04  E-value: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|
5NEN_B         44 TVQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:pfam00364  44 EIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 68-262 7.17e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B          68 EVLVQLSQV--QAQAQVDSLRDQYyttLATEGRLLAERDGLSIVTF--SPILDAVKDKPRVAEIIALQTQLFASRRQALQ 143
Cdd:TIGR02168  782 AEIEELEAQieQLKEELKALREAL---DELRAELTLLNEEAANLRErlESLERRIAATERRLEDLEEQIEELSEDIESLA 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         144 SEIDGYKQSMDGIRFQLKGLQDSRGNKQIQLSSLREQM-NSMKQLAADgylpRNRYLEVQRQFAEVNSSIDETVGRIGQL 222
Cdd:TIGR02168  859 AEIEELEELIEELESELEALLNERASLEEALALLRSELeELSEELREL----ESKRSELRRELEELREKLAQLELRLEGL 934

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
5NEN_B         223 QKQLLESQQRIDQRFADYQREVRTQLAQTQMDASEFRNKL 262
Cdd:TIGR02168  935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 45-73 7.93e-03

Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 35.04  E-value: 7.93e-03
                        10        20
                ....*....|....*....|....*....
5NEN_B       45 VQAPASGIIKNIAVRDGDKVKAGEVLVQL 73
Cdd:COG0508  48 VPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 65-266 9.29e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 38.49  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B          65 KAGEVLVQLSQVQAQAQVDSLRDQYYTTLATEGRLLAERDGLSIVTFS--PILDAVKDKPRVAEIIAlqtQLFASRRQAL 142
Cdd:TIGR00606  341 EKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSerQIKNFHTLVIERQEDEA---KTAAQLCADL 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5NEN_B         143 QSEIDGYKQSMDGIRFQLKGLQDSRGNKQIQLSSLREQMNSMKQLAADGYLPRNRYLEVQRQF---------AEVNSSID 213
Cdd:TIGR00606  418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELrkaerelskAEKNSLTE 497

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
5NEN_B         214 ETVGRIGQLQKQ---LLESQQRIDQRFA--DYQREVRTQ---LAQTQMDASE--FRNKLQMAD 266
Cdd:TIGR00606  498 TLKKEVKSLQNEkadLDRKLRKLDQEMEqlNHHTTTRTQmemLTKDKMDKDEqiRKIKSRHSD 560
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 45-71 9.82e-03

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 36.41  E-value: 9.82e-03
                        10        20
                ....*....|....*....|....*..
5NEN_B       45 VQAPASGIIKNIAVRDGDKVKAGEVLV 71
Cdd:COG0511 107 IEAPVSGTVVEILVENGQPVEYGQPLF 133
 
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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