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Conserved domains on  [gi|501229677|ref|WP_012272695|]
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MULTISPECIES: efflux RND transporter periplasmic adaptor subunit [Pseudomonas]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

CATH:  2.40.50.100|2.40.420.20|2.40.30.170|1.10.287.470
Gene Ontology:  GO:0016020|GO:0055085|GO:0022857|GO:0042802
PubMed:  32073314
TCDB:  2.A.6

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 198-423 9.73e-25

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: 103.87  E-value: 9.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 198 PVRQTALAPAQIVSRQAQIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLR-----SRADVLGKEVAVADAELV--- 269
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQaalaqAQAQLAAAQAQLELAKAEler 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 270 --------AASQRAFDnpQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGVAVFSDPNdwLGKPVSTGERIMQV 341
Cdd:COG0845   87 ykallkkgAVSQQELD--QAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 342 ADPAQPAMQIQLAVADAIALEPGAEVTLFLTAYPLSPLKGKVLETSYQarpADDGVVAYRLLASIDEHAAHARLGLHGTA 421
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPA---VDPATRTVRVRAELPNPDGLLRPGMFVRV 239


                 ..
gi 501229677 422 KL 423
Cdd:COG0845  240 RI 241
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 198-423 9.73e-25

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: 103.87  E-value: 9.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 198 PVRQTALAPAQIVSRQAQIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLR-----SRADVLGKEVAVADAELV--- 269
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQaalaqAQAQLAAAQAQLELAKAEler 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 270 --------AASQRAFDnpQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGVAVFSDPNdwLGKPVSTGERIMQV 341
Cdd:COG0845   87 ykallkkgAVSQQELD--QAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 342 ADPAQPAMQIQLAVADAIALEPGAEVTLFLTAYPLSPLKGKVLETSYQarpADDGVVAYRLLASIDEHAAHARLGLHGTA 421
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPA---VDPATRTVRVRAELPNPDGLLRPGMFVRV 239


                 ..
gi 501229677 422 KL 423
Cdd:COG0845  240 RI 241
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 198-318 8.56e-10

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: 59.74  E-value: 8.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  198 PVRQTALAPAQI-VSRQAQIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLRSRADVLGKEVAVADAELVAA----- 271
Cdd:pfam00529   3 PLTKGVEAPGRVvVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLqaeld 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 501229677  272 ---------SQRAFDNPQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGV 318
Cdd:pfam00529  83 rlqaleselAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGI 138
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 217-273 2.79e-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: 41.63  E-value: 2.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501229677 217 VTSPIDGVINQVQVRPNQPVEAGTPLFALD----ETTLRSRADvlG--KEVAVADAELVAASQ 273
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEamkmENEVTAPVA--GvvKEILVKEGDQVEAGQ 62
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
175-403 9.59e-04

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 41.32  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 175 GRWRPSRRQVLLVALLFGALLLVPVRQTALAPAQIVS------------------------RQAQiVTSPIDGVINQVQV 230
Cdd:PRK09578   1 YEWARRRRLLLAALVALFVLAGCGKGDSDAAAAAPREatvvtvrptsvpmtvelpgrldayRQAE-VRARVAGIVTARTY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 231 RPNQPVEAGTPLFALDETTLRSRADVLGKEVAVADAELVAASQR-------AFDNPQSKGELTLLQGRAQQRRAELAAVQ 303
Cdd:PRK09578  80 EEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKrrryddlVRDRAVSERDYTEAVADERQAKAAVASAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 304 AQLKRTQ-------VLAPRAGVA----------VFSDPndwlGKPVSTGERI----MQVADPAQPAMQIQLAV----ADA 358
Cdd:PRK09578 160 AELARAQlqldyatVTAPIDGRArralvtegalVGQDQ----ATPLTTVEQLdpiyVNFSQPAADVEALRRAVksgrATG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 501229677 359 IAlEPGAEVTLFLTAYPLSPLKGKVLETSYQARPADDgVVAYRLL 403
Cdd:PRK09578 236 IA-QQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTD-TVAMRAL 278
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 198-423 9.73e-25

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: 103.87  E-value: 9.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 198 PVRQTALAPAQIVSRQAQIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLR-----SRADVLGKEVAVADAELV--- 269
Cdd:COG0845    7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQaalaqAQAQLAAAQAQLELAKAEler 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 270 --------AASQRAFDnpQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGVAVFSDPNdwLGKPVSTGERIMQV 341
Cdd:COG0845   87 ykallkkgAVSQQELD--QAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 342 ADPAQPAMQIQLAVADAIALEPGAEVTLFLTAYPLSPLKGKVLETSYQarpADDGVVAYRLLASIDEHAAHARLGLHGTA 421
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPA---VDPATRTVRVRAELPNPDGLLRPGMFVRV 239


                 ..
gi 501229677 422 KL 423
Cdd:COG0845  240 RI 241
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
180-423 3.61e-18

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 85.10  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 180 SRRQVLLVALLFGALLLVPVRQTALAPAQIVSRQAQI------VTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLRSR 253
Cdd:COG1566    5 KKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVearvvtVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 254 ADVLGKEVAVADAELV-------------------------------------------AASQRAFDN------------ 278
Cdd:COG1566   85 LAQAEAQLAAAEAQLArleaelgaeaeiaaaeaqlaaaqaqldlaqreleryqalykkgAVSQQELDEaraaldaaqaql 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 279 -------------PQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGV--AVFSDPNDWlgkpVSTGERIMQVAD 343
Cdd:COG1566  165 eaaqaqlaqaqagLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVvtNLNVEPGEV----VSAGQPLLTIVP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 344 PAQPAMQIQLAVADAIALEPGAEVTLFLTAYPLSPLKGKVLETSYQARPADDGVVA-------YRLLASIDEHAAHA-RL 415
Cdd:COG1566  241 LDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNAtgnvvqrYPVRIRLDNPDPEPlRP 320


                 ....*...
gi 501229677 416 GLHGTAKL 423
Cdd:COG1566  321 GMSATVEI 328
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 198-318 8.56e-10

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: 59.74  E-value: 8.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  198 PVRQTALAPAQI-VSRQAQIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLRSRADVLGKEVAVADAELVAA----- 271
Cdd:pfam00529   3 PLTKGVEAPGRVvVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLqaeld 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 501229677  272 ---------SQRAFDNPQSKGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGV 318
Cdd:pfam00529  83 rlqaleselAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGI 138
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 311-407 8.81e-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: 52.75  E-value: 8.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  311 VLAPRAGVAVFSDPndWLGKPVSTGERIMQVADPAQPAMQIQLAVADAIALEPGAEVTLFLTAYPLSPLKGKVletSYQA 390
Cdd:pfam13437   2 IRAPVDGVVAELNV--EEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKV---VRIS 76

                          90
                  ....*....|....*..
gi 501229677  391 RPADDGVVAYRLLASID 407
Cdd:pfam13437  77 PTVDPDTGVIPVRVSIE 93
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 217-302 4.47e-06

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: 45.05  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  217 VTSPIDGVINQVQVRPNQPVEAGTPLFAL-DETTLRSRAdvlgkevavadaeLVAASQRAFDNPQSKGELTLLQGRAQQR 295
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEA-------------FVPAADLGSLKKGQKVTLKLDPGSDYTL 68


                  ....*..
gi 501229677  296 RAELAAV 302
Cdd:pfam13437  69 EGKVVRI 75
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 212-383 7.04e-06

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: 46.73  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  212 RQAQIVTSPIDGVINQVQVR-PNQPVEAGTPLFaldettlrsraDVLGKEVAVADAELVAASQRAfdNPQSKGELTllqG 290
Cdd:pfam16576  17 RRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLA-----------ELYSPELVAAQQEYLLALRSG--DALSKSELL---R 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  291 RAQQR-------RAELAAVQAQ---LKRTQVLAPRAGVAVFSDPNDwlGKPVSTGERIMQVADPAQPAMQIQLAVADAIA 360
Cdd:pfam16576  81 AARQRlrllgmpEAQIAELERTgkvQPTVTVYAPISGVVTELNVRE--GMYVQPGDTLFTIADLSTVWVEADVPEQDLAL 158

                         170       180
                  ....*....|....*....|...
gi 501229677  361 LEPGAEVTLFLTAYPLSPLKGKV 383
Cdd:pfam16576 159 VKVGQPAEVTLPALPGKTFEGKV 181
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 217-273 2.79e-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: 41.63  E-value: 2.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501229677 217 VTSPIDGVINQVQVRPNQPVEAGTPLFALD----ETTLRSRADvlG--KEVAVADAELVAASQ 273
Cdd:cd06850    2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEamkmENEVTAPVA--GvvKEILVKEGDQVEAGQ 62
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 217-245 2.40e-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: 39.32  E-value: 2.40e-04
                         10        20
                 ....*....|....*....|....*....
gi 501229677 217 VTSPIDGVINQVQVRPNQPVEAGTPLFAL 245
Cdd:cd06850   39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
175-403 9.59e-04

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 41.32  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 175 GRWRPSRRQVLLVALLFGALLLVPVRQTALAPAQIVS------------------------RQAQiVTSPIDGVINQVQV 230
Cdd:PRK09578   1 YEWARRRRLLLAALVALFVLAGCGKGDSDAAAAAPREatvvtvrptsvpmtvelpgrldayRQAE-VRARVAGIVTARTY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 231 RPNQPVEAGTPLFALDETTLRSRADVLGKEVAVADAELVAASQR-------AFDNPQSKGELTLLQGRAQQRRAELAAVQ 303
Cdd:PRK09578  80 EEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKrrryddlVRDRAVSERDYTEAVADERQAKAAVASAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 304 AQLKRTQ-------VLAPRAGVA----------VFSDPndwlGKPVSTGERI----MQVADPAQPAMQIQLAV----ADA 358
Cdd:PRK09578 160 AELARAQlqldyatVTAPIDGRArralvtegalVGQDQ----ATPLTTVEQLdpiyVNFSQPAADVEALRRAVksgrATG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 501229677 359 IAlEPGAEVTLFLTAYPLSPLKGKVLETSYQARPADDgVVAYRLL 403
Cdd:PRK09578 236 IA-QQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTD-TVAMRAL 278
PRK10476 PRK10476
multidrug transporter subunit MdtN;
184-318 1.57e-03

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.40  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677 184 VLLVALLFGALLLVpVRQTALAPAqivSRQAQI------VTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLRSRADVL 257
Cdd:PRK10476  16 LAIVALAIVALVFV-IWRTDSAPS---TDDAYIdadvvhVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQA 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501229677 258 GKEVAVADAELvAASQRAFDNPQSKGELTllqgRAQQRRAELAAVQA--QLKRTQVLAPRAGV 318
Cdd:PRK10476  92 QADLALADAQI-MTTQRSVDAERSNAASA----NEQVERARANAKLAtrTLERLEPLLAKGYV 149
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 168-375 1.58e-03

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: 40.48  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  168 LTRRQRLGRWRPSRRQVL--LVALLFGALLLVPVRQTALAPAQIVSRQAQiVTSPIDGVINQvqvrpnQPVEAGTpLFAL 245
Cdd:pfam00529  81 LDRLQALESELAISRQDYdgATAQLRAAQAAVKAAQAQLAQAQIDLARRR-VLAPIGGISRE------SLVTAGA-LVAQ 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  246 DETTLRSRadvlgkeVAVADAELVAASQRAFDNPQS-KGELTLLQGRAQQRRAELAAVQAQLKRTQVLAPRAGVAVFSDP 324
Cdd:pfam00529 153 AQANLLAT-------VAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSV 225

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501229677  325 NDwLGKPVSTGERIMQVADPAQPAMQIQLAVADAIALEPGAEVTLFLTAYP 375
Cdd:pfam00529 226 TV-DGGTVSAGLRLMFVVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFP 275
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
215-251 1.91e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 36.27  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 501229677  215 QIVTSPIDGVINQVQVRPNQPVEAGTPLFALDETTLR 251
Cdd:pfam13533   3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQ 39
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 217-246 5.43e-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: 37.18  E-value: 5.43e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 501229677 217 VTSPIDGVINQVQVRPNQPVEAGTPLFALD 246
Cdd:COG0511  107 IEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 197-271 7.59e-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: 38.91  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501229677  197 VPVRQTALAPAQIVSRQAQI-----VTSPIDGVINQVQVRPNQPVEAGTPLFALD----ETTLRSRADVLGKEVAVADAE 267
Cdd:COG1038  1054 VRVRDRSVKVTVASREKADPgnpghIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEamkmETTITAPRDGTVKEVLVKEGD 1133


                  ....
gi 501229677  268 LVAA 271
Cdd:COG1038  1134 QVEA 1137
 
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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