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Conserved domains on  [gi|15596434|ref|NP_249928|]
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multidrug resistance efflux pump [Pseudomonas aeruginosa PAO1]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

HlyD family secretion protein similar to Escherichia coli protein YhiI, Acinetobacter baumannii colistin resistance protein EmrA, and Burkholderia cepacia fusaric acid resistance protein FusE

Gene Ontology:  GO:0022857|GO:0016020|GO:0055085
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

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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 ...
 53-370 4.07e-61

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 TIGR00998:

Pssm-ID: 481212 [Multi-domain]  Cd Length: 334  Bit Score: 200.02  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    53 EGTDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQrlraaeaREAAAQAALEAQRAKLETLDRQL 132
Cdd:TIGR00998  31 ESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL-------ALAKAEANLAALVRQTKQLEITV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   133 LEQAQTISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAhqraraaarrasaeegrQRAAKDVLKSRR 212
Cdd:TIGR00998 104 QQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKA-----------------LLSAKAALNAAI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   213 REAEAALA--------QRQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVAN 284
Cdd:TIGR00998 167 QEQLNANQalvrgtplKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEAN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   285 YKETQLERIRPGQPVELEVDTFGR--RWRGRVDSVAPASGAVFALLPPDNATGNFTKIVQRFPVRIRLDADAAERGRLLP 362
Cdd:TIGR00998 247 FKETQLKNVRIGQPVTIRSDLYGSdvVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRI 326


                  ....*...
gi 15596434   363 GMSVIATV 370
Cdd:TIGR00998 327 GLSAEVEI 334
 
Name Accession Description Interval E-value
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
 53-370 4.07e-61

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 200.02  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    53 EGTDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQrlraaeaREAAAQAALEAQRAKLETLDRQL 132
Cdd:TIGR00998  31 ESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL-------ALAKAEANLAALVRQTKQLEITV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   133 LEQAQTISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAhqraraaarrasaeegrQRAAKDVLKSRR 212
Cdd:TIGR00998 104 QQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKA-----------------LLSAKAALNAAI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   213 REAEAALA--------QRQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVAN 284
Cdd:TIGR00998 167 QEQLNANQalvrgtplKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEAN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   285 YKETQLERIRPGQPVELEVDTFGR--RWRGRVDSVAPASGAVFALLPPDNATGNFTKIVQRFPVRIRLDADAAERGRLLP 362
Cdd:TIGR00998 247 FKETQLKNVRIGQPVTIRSDLYGSdvVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRI 326


                  ....*...
gi 15596434   363 GMSVIATV 370
Cdd:TIGR00998 327 GLSAEVEI 334
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
55-373 1.67e-59

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 195.65  E-value: 1.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  55 TDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRLRAAEAREAAAQAaleaqraKLETLDRQLLE 134
Cdd:COG1566  36 TADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEA-------QLARLEAELGA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 135 QAQtISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAHQ------RARAAARRASAEEGRQRAAKDVL 208
Cdd:COG1566 109 EAE-IAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDaaqaqlEAAQAQLAQAQAGLREEEELAAA 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 209 KSRRREAEAALAQrqaelqeaaaarelARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKET 288
Cdd:COG1566 188 QAQVAQAEAALAQ--------------AELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPET 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 289 QLERIRPGQPVELEVDTF-GRRWRGRVDSVAPASGAVFallPPDNATGNftkIVQRFPVRIRLDADaaERGRLLPGMSVI 367
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYpDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNP--DPEPLRPGMSAT 325


                ....*.
gi 15596434 368 ATVDTR 373
Cdd:COG1566 326 VEIDTE 331
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
50-378 3.76e-41

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 149.07  E-value: 3.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   50 RFLEGTDDAYVRADWVAVSAQVSGYVAEVLVaDDAD-VQAGDLLLRLDPRDFRQRLRAAEAReaaaqaaleaqrakLETL 128
Cdd:PRK15136  47 RHHQETDDAYVAGNQVQIMSQVSGSVTKVWA-DNTDfVKEGDVLVTLDPTDAEQAFEKAKTA--------------LANS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  129 DRQLLEQAQTISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENadaahqraraaarrasaeegrqraAKDVL 208
Cdd:PRK15136 112 VRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREELQH------------------------ARDAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  209 KSRRREAEAALAQ--------------RQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVV 274
Cdd:PRK15136 168 ASAQAQLDVAIQQynanqamilntpleDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVV 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  275 PLEQAYVVANYKETQLERIRPGQPVELEVDTFGR--RWRGRVDSVAPASGAVFALLPPDNATGNFTKIVQRFPVRIRLDA 352
Cdd:PRK15136 248 PATNLWVDANFKETQLANMRIGQPATITSDIYGDdvVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDA 327

                        330       340
                 ....*....|....*....|....*.
gi 15596434  353 DAAERGRLLPGMSVIATVDTREPDGA 378
Cdd:PRK15136 328 KQLAQHPLRIGLSTLVTVDTANRDGQ 353
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 53-317 4.04e-31

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: 120.61  E-value: 4.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    53 EGTDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRLRAAEAREAAAQAALEAQRAKLETLDRQL 132
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   133 LEQA---QTISRARADGEAARAEWRRAE-------TDWRRYRQLADEHATSRQRLENADAAHQRARAAARRASAEEGRQR 202
Cdd:pfam00529  89 SELAisrQDYDGATAQLRAAQAAVKAAQaqlaqaqIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   203 AAKDVL-KSRRREAEAALAQRQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRL-RQYVTPGLPLLAVVPLEQAY 280
Cdd:pfam00529 169 VQITQSaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15596434   281 VVANYKETQLERIRPGQPVELEVDTFGRRWRGRVDSV 317
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGV 285
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 67-95 6.29e-04

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: 37.78  E-value: 6.29e-04
                        10        20
                ....*....|....*....|....*....
gi 15596434  67 VSAQVSGYVAEVLVADDADVQAGDLLLRL 95
Cdd:cd06850  39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
8a0101 TIGR00998
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ...
 53-370 4.07e-61

efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]


Pssm-ID: 273385 [Multi-domain]  Cd Length: 334  Bit Score: 200.02  E-value: 4.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    53 EGTDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQrlraaeaREAAAQAALEAQRAKLETLDRQL 132
Cdd:TIGR00998  31 ESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL-------ALAKAEANLAALVRQTKQLEITV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   133 LEQAQTISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAhqraraaarrasaeegrQRAAKDVLKSRR 212
Cdd:TIGR00998 104 QQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKA-----------------LLSAKAALNAAI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   213 REAEAALA--------QRQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVAN 284
Cdd:TIGR00998 167 QEQLNANQalvrgtplKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEAN 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   285 YKETQLERIRPGQPVELEVDTFGR--RWRGRVDSVAPASGAVFALLPPDNATGNFTKIVQRFPVRIRLDADAAERGRLLP 362
Cdd:TIGR00998 247 FKETQLKNVRIGQPVTIRSDLYGSdvVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRI 326


                  ....*...
gi 15596434   363 GMSVIATV 370
Cdd:TIGR00998 327 GLSAEVEI 334
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
55-373 1.67e-59

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 195.65  E-value: 1.67e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  55 TDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRLRAAEAREAAAQAaleaqraKLETLDRQLLE 134
Cdd:COG1566  36 TADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEA-------QLARLEAELGA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 135 QAQtISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAHQ------RARAAARRASAEEGRQRAAKDVL 208
Cdd:COG1566 109 EAE-IAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDaaqaqlEAAQAQLAQAQAGLREEEELAAA 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 209 KSRRREAEAALAQrqaelqeaaaarelARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKET 288
Cdd:COG1566 188 QAQVAQAEAALAQ--------------AELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPET 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 289 QLERIRPGQPVELEVDTF-GRRWRGRVDSVAPASGAVFallPPDNATGNftkIVQRFPVRIRLDADaaERGRLLPGMSVI 367
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYpDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNP--DPEPLRPGMSAT 325


                ....*.
gi 15596434 368 ATVDTR 373
Cdd:COG1566 326 VEIDTE 331
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
50-378 3.76e-41

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 149.07  E-value: 3.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   50 RFLEGTDDAYVRADWVAVSAQVSGYVAEVLVaDDAD-VQAGDLLLRLDPRDFRQRLRAAEAReaaaqaaleaqrakLETL 128
Cdd:PRK15136  47 RHHQETDDAYVAGNQVQIMSQVSGSVTKVWA-DNTDfVKEGDVLVTLDPTDAEQAFEKAKTA--------------LANS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  129 DRQLLEQAQTISRARADGEAARAEWRRAETDWRRYRQLADEHATSRQRLENadaahqraraaarrasaeegrqraAKDVL 208
Cdd:PRK15136 112 VRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREELQH------------------------ARDAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  209 KSRRREAEAALAQ--------------RQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVV 274
Cdd:PRK15136 168 ASAQAQLDVAIQQynanqamilntpleDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVV 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  275 PLEQAYVVANYKETQLERIRPGQPVELEVDTFGR--RWRGRVDSVAPASGAVFALLPPDNATGNFTKIVQRFPVRIRLDA 352
Cdd:PRK15136 248 PATNLWVDANFKETQLANMRIGQPATITSDIYGDdvVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDA 327

                        330       340
                 ....*....|....*....|....*.
gi 15596434  353 DAAERGRLLPGMSVIATVDTREPDGA 378
Cdd:PRK15136 328 KQLAQHPLRIGLSTLVTVDTANRDGQ 353
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 65-378 6.31e-38

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: 138.92  E-value: 6.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  65 VAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQrlraaeareaaaqaaleaqrakletldrqlleqaqTISRARA 144
Cdd:COG0845  24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQA-----------------------------------ALAQAQA 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 145 DGEAARAEWRRAETDWRRYRQLADEHATSRQRLENadaahqraraaarrasaeegrQRAAKDVLKSRRREAEAALAQrqa 224
Cdd:COG0845  69 QLAAAQAQLELAKAELERYKALLKKGAVSQQELDQ---------------------AKAALDQAQAALAAAQAALEQ--- 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434 225 elqeaaaarelARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLERIRPGQPVELEVD 304
Cdd:COG0845 125 -----------ARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLD 193

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596434 305 TF-GRRWRGRVDSVAPAsgavfallpPDNATGNftkivqrFPVRIRLDADAaerGRLLPGMSVIATVDTREPDGA 378
Cdd:COG0845 194 AGpGKTFEGKVTFIDPA---------VDPATRT-------VRVRAELPNPD---GLLRPGMFVRVRIVLGERENA 249
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 53-317 4.04e-31

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: 120.61  E-value: 4.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    53 EGTDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRLRAAEAREAAAQAALEAQRAKLETLDRQL 132
Cdd:pfam00529   9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   133 LEQA---QTISRARADGEAARAEWRRAE-------TDWRRYRQLADEHATSRQRLENADAAHQRARAAARRASAEEGRQR 202
Cdd:pfam00529  89 SELAisrQDYDGATAQLRAAQAAVKAAQaqlaqaqIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   203 AAKDVL-KSRRREAEAALAQRQAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRL-RQYVTPGLPLLAVVPLEQAY 280
Cdd:pfam00529 169 VQITQSaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15596434   281 VVANYKETQLERIRPGQPVELEVDTFGRRWRGRVDSV 317
Cdd:pfam00529 249 VPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGV 285
PRK10476 PRK10476
multidrug transporter subunit MdtN;
55-370 2.37e-28

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 113.58  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   55 TDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRqrlraaeareaaaqAALEAQRAKLETLDRQLLE 134
Cdd:PRK10476  39 TDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYE--------------LTVAQAQADLALADAQIMT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  135 QAQTISRARADGEAARAEWRRAET-------DWRRYRQLADEHATSRQRLENADAAHQRARAAARRASAEEGRQRAAKDV 207
Cdd:PRK10476 105 TQRSVDAERSNAASANEQVERARAnaklatrTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAAAVGG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  208 LKS-----RRREAEAALAQRQaelqeaaaarelarhaLDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVV 282
Cdd:PRK10476 185 VDAlvaqrAAREAALAIAELH----------------LEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAI 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  283 ANYKETQLERIRPGQP--VELEVDTfGRRWRGRVDS----VAPASGAVFAL-LPPDNATGNFTKIVQRFPVRIRLDADAA 355
Cdd:PRK10476 249 ANFRETDLKNIRVGDCatVYSMIDR-GRPFEGKVDSigwgVLPDDGGNVPRgLPYVPRSINWVRVAQRFPVRIMLDKPDP 327

                        330
                 ....*....|....*
gi 15596434  356 ERGRLlpGMSVIATV 370
Cdd:PRK10476 328 ELFRI--GASAVVEL 340
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 65-378 5.61e-27

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: 109.33  E-value: 5.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    65 VAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFrqrlraaeareaaaqaaleaqrakletldrQLLEQAqtisrARA 144
Cdd:TIGR01730  27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY------------------------------QLALQA-----ALA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   145 DGEAARAEWRRAETDWRRYRQLADEHATSRQRLENadaahqraraaarrasaeegrQRAAKDVLKSRRREAEAALAQrqa 224
Cdd:TIGR01730  72 QLAAAEAQLELAQRSFERAERLVKRNAVSQADLDD---------------------AKAAVEAAQADLEAAKASLAS--- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   225 elqeaaaarelARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLERIRPGQPVELEVD 304
Cdd:TIGR01730 128 -----------AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELD 196

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596434   305 TF-GRRWRGRVDSVAPAsgavfallpPDNATGNFtkivqrfpvRIRLDADAAErGRLLPGMSVIATVDTREPDGA 378
Cdd:TIGR01730 197 ALpGEEFKGKLRFIDPR---------VDSGTGTV---------RVRATFPNPD-GRLLPGMFGRVTISLKVRSSA 252
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
 65-368 3.84e-14

ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.


Pssm-ID: 213754 [Multi-domain]  Cd Length: 327  Bit Score: 72.55  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434    65 VAVSAQVSGY---VAEVLVADDADVQAGDLLLRLDPRDFRQRLRAAEA----REAAAQAALEAQRAKLETLDRQLLEQAQ 137
Cdd:TIGR02971  14 VAVAAPSSGGtdrIKKLLVAEGDRVQAGQVLAELDSRPERTAELDVARtqldEAKARLAQVRAGAKKGEIAAQRAARAAA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   138 TISRARADGEAA----RAEWRRAETDWRRYRQLADEHATSRQRLENA----DAAHQRARAAARRASAEEGRQRAAKDVLK 209
Cdd:TIGR02971  94 KLFKDVAAQQATlnrlEAELETAQREVDRYRSLFRDGAVSASDLDSKalklRTAEEELEEALASRSEQIDGARAALASLA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   210 SRRREAEAALAQrqAELQEAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQyVTPGLPLLAVVPLEQAYVVANYKETQ 289
Cdd:TIGR02971 174 EEVRETDVDLAQ--AEVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGE-VIGSEGILEMGDTSQMYAVAEVYETD 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   290 LERIRPGQPVELEVDTFGRRWRGRVDSVAP--ASGAVFALLPPDNATgnfTKIVQrfpVRIRLDADAAERGRLLPGMSVI 367
Cdd:TIGR02971 251 INRVRVGQRATITSTALSGPLRGTVRRIGSliAKNDVLSTDPAADAD---ARVVE---VKIRLDPASSERVGRLTNLQVD 324


                  .
gi 15596434   368 A 368
Cdd:TIGR02971 325 V 325
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 245-366 3.56e-13

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: 67.92  E-value: 3.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   245 IRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLERIRPGQPVELEVDTF-GRRWRGRVDSVAPasga 323
Cdd:pfam16576 111 VYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALpGKTFEGKVDYIYP---- 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15596434   324 vfaLLPPDNATgnftkivqrfpVRIRLDADAAErGRLLPGMSV 366
Cdd:pfam16576 187 ---TLDPKTRT-----------VRVRIELPNPD-GRLKPGMFA 214
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
55-379 1.13e-11

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 65.15  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   55 TDDAYVRADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRlraaeareaaaqaaleaqrakletldrqlLE 134
Cdd:PRK10559  38 TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKA-----------------------------LA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  135 QAqtisraradgeaaraewrraETDWRRYRQLADE---HATSRQRLenadaahqraraAARRASAEEGRQraAKDVLKSR 211
Cdd:PRK10559  89 EA--------------------EADVAYYQVLAQEkrrEAGRRNRL------------GVQAMSREEIDQ--ANNVLQTV 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  212 RREAEAALAQRQAELQEaaaarelarhaLDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLE 291
Cdd:PRK10559 135 LHQLAKAQATRDLAKLD-----------LERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  292 RIRPGQPVELEVDTFGRRWRGRVDSVapASGAVFALLPPDN---ATGN----FTKIVQRFPVRIRLDadaAERGRLLPGM 364
Cdd:PRK10559 204 GVRPGYRAEITPLGSNKVLKGTVDSV--AAGVTNSSSTRDSkgmATIDsnleWVRLAQRVPVRIRLD---NQQGNLYPAG 278

                        330
                 ....*....|....*....
gi 15596434  365 S----VIATVDTREPDGAS 379
Cdd:PRK10559 279 TtatvVITGKQDRDASQDS 297
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 65-319 1.27e-10

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 61.90  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   65 VAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQrlraAEAREAAAQAALEAQRAKLETLDRQlleqaQTISRARA 144
Cdd:PRK03598  44 VNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYEN----ALMQAKANVSVAQAQLDLMLAGYRD-----EEIAQARA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  145 DGEAARAEWRRAETDWRRYRQLADEHATSRQRLENADAAHQRARAaarrasaeegRQRAAKDVLKSRRR--------EAE 216
Cdd:PRK03598 115 AVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQA----------TLKSAQDKLSQYREgnrpqdiaQAK 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  217 AALAQrqaelqeAAAARELARHALDDTEIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLERIRPG 296
Cdd:PRK03598 185 ASLAQ-------AQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPG 257

                        250       260
                 ....*....|....*....|....
gi 15596434  297 QPVELEVDTF-GRRWRGRVDSVAP 319
Cdd:PRK03598 258 RKVLLYTDGRpDKPYHGQIGFVSP 281
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 244-363 2.94e-10

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: 56.99  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   244 EIRAPFAGRVGQRKVRLRQYVTPGLPLLAVVPLEQAYVVANYKETQLERIRPGQPVELEVDTF-GRRWRGRVDSVAPAsg 322
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGsDYTLEGKVVRISPT-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15596434   323 avfallpPDNATgnftkivQRFPVRIRLDADAAERgRLLPG 363
Cdd:pfam13437  79 -------VDPDT-------GVIPVRVSIENPKTPI-PLLPG 104
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
65-101 1.42e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 42.04  E-value: 1.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 15596434    65 VAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFR 101
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQ 39
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
62-267 4.55e-05

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 45.17  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   62 ADWVAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPRDFRQRlraaeareaaaqaaleaqrakletldrqlLEQAQtisr 141
Cdd:PRK11556  85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVA-----------------------------LAQAQ---- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434  142 aradGEAA--RAEWRRAETDWRRYRQLADEHATSRQRLENadaahqraraaarrasaEEGRQRAAKDVLKSRrrEAEAAL 219
Cdd:PRK11556 132 ----GQLAkdQATLANARRDLARYQQLAKTNLVSRQELDA-----------------QQALVSETEGTIKAD--EASVAS 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15596434  220 AQrqaelqeaaaarelarHALDDTEIRAPFAGRVGQRKVRLRQYVTPG 267
Cdd:PRK11556 189 AQ----------------LQLDYSRITAPISGRVGLKQVDVGNQISSG 220
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 67-95 6.29e-04

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: 37.78  E-value: 6.29e-04
                        10        20
                ....*....|....*....|....*....
gi 15596434  67 VSAQVSGYVAEVLVADDADVQAGDLLLRL 95
Cdd:cd06850  39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 65-179 3.59e-03

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 38.99  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596434   65 VAVSAQVSGYVAEVLVADDADVQAGDLLLRLDPrdfrqrlraaeareaaaqaaleaqraklETLDRQLLEQAQTISRARA 144
Cdd:PRK11578  62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDP----------------------------EQAENQIKEVEATLMELRA 113

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15596434  145 DGEAARAEWRRAETDWRRYRQLADEHATSRQRLEN 179
Cdd:PRK11578 114 QRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDT 148
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 66-97 4.90e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 38.97  E-value: 4.90e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 15596434    66 AVSAQVSGYVAEVLVADDADVQAGDLLLRLDP 97
Cdd:PRK12999 1115 TITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
Biotin_lipoyl pfam00364
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ...
 67-95 9.44e-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: 34.50  E-value: 9.44e-03
                          10        20
                  ....*....|....*....|....*....
gi 15596434    67 VSAQVSGYVAEVLVADDADVQAGDLLLRL 95
Cdd:pfam00364  45 IPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
 
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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