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Conserved domains on  [gi|769946247|ref|WP_045079542|]
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efflux RND transporter periplasmic adaptor subunit [Aequorivita vladivostokensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
113-321 1.05e-92

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: 284.01  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  113 NTIQLSGKIMANEEANAVQASYFEGRIEKLNVNFTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPA--LYKAVR 190
Cdd:pfam16576   4 RTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKseLLRAAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  191 NKLKLWKLSETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQISQLKEGQ 270
Cdd:pfam16576  84 QRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQ 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 769946247  271 KITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFV 321
Cdd:pfam16576 164 PAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
466-559 1.44e-32

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


:

Pssm-ID: 432106  Cd Length: 93  Bit Score: 120.57  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  466 VFDDYILLKDALVNDDAKNAQEAGNQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANAIENSSDIATQRGHFKHLSA 545
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79
                          90
                  ....*....|....
gi 769946247  546 HMISSVQLFGVNEN 559
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
49-75 3.79e-11

Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins.


:

Pssm-ID: 437167 [Multi-domain]  Cd Length: 28  Bit Score: 57.61  E-value: 3.79e-11
                          10        20
                  ....*....|....*....|....*..
gi 769946247   49 WTCSMHPQIMQPEPGDCPICGMDLIPA 75
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
PRK09859 super family cl31380
multidrug transporter subunit MdtE;
262-396 1.70e-04

multidrug transporter subunit MdtE;


The actual alignment was detected with superfamily member PRK09859:

Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 44.32  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 262 QISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAKVamTKGSdnMETQITVP 341
Cdd:PRK09859 230 QIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALV--DEGS--RQNVLLVP 305
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 769946247 342 ATAVMWTGERSLVYVKTNPNEpVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNG 396
Cdd:PRK09859 306 QEGVTHNAQGKATALILDKDD-VVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
 
Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
113-321 1.05e-92

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: 284.01  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  113 NTIQLSGKIMANEEANAVQASYFEGRIEKLNVNFTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPA--LYKAVR 190
Cdd:pfam16576   4 RTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKseLLRAAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  191 NKLKLWKLSETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQISQLKEGQ 270
Cdd:pfam16576  84 QRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQ 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 769946247  271 KITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFV 321
Cdd:pfam16576 164 PAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
107-412 2.55e-75

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: 242.93  E-value: 2.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 107 VSGTDENTIQLSGKIMANEEANavQASYFEGRIEKLNVNfTGEEVRRGQLLATIYAPT----LVAAQQELLTA-ASMKES 181
Cdd:COG0845    4 ERGDVPETVEATGTVEARREVE--VRARVSGRVEEVLVD-EGDRVKKGQVLARLDPPDlqaaLAQAQAQLAAAqAQLELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 182 QP------ALYK-------AVRNKLKLWKLSETQIN----QIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIV 244
Cdd:COG0845   81 KAelerykALLKkgavsqqELDQAKAALDQAQAALAaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 245 KVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAK 324
Cdd:COG0845  161 TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 325 VAMTKGSDnmetQITVPATAVMWTGERSLVYVKTNPNepVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTVDAAA 404
Cdd:COG0845  241 IVLGEREN----ALLVPASAVVRDGGGAYVFVVDADG--KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGA 314

                 ....*...
gi 769946247 405 QLQGKKSM 412
Cdd:COG0845  315 KVRVVEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
108-400 2.17e-47

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: 168.65  E-value: 2.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  108 SGTDENTIQLSGKIMANEEAN-AVQASyfeGRIEKLNVNfTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPALY 186
Cdd:TIGR01730   8 SETLANTLTFPGSLEAVDEADlAAEVA---GKITKISVR-EGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  187 KAVRNKL-KLWKLS-----------------ETQINQIESS-GKVRENFP---IYATVSGTVSQKIAEEGDYVKQGQPIV 244
Cdd:TIGR01730  84 QRSFERAeRLVKRNavsqadlddakaaveaaQADLEAAKASlASAQLNLRyteIRAPFDGTIGRRLVEVGAYVTAGQTLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  245 KVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAK 324
Cdd:TIGR01730 164 TIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRVT 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769946247  325 VaMTKGSDNMetqITVPATAVMWTGERSLVYVKTNPNepVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTV 400
Cdd:TIGR01730 244 I-SLKVRSSA---IVVPTQAVIEDLNGKYVYVVKNDG--KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
466-559 1.44e-32

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


Pssm-ID: 432106  Cd Length: 93  Bit Score: 120.57  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  466 VFDDYILLKDALVNDDAKNAQEAGNQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANAIENSSDIATQRGHFKHLSA 545
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79
                          90
                  ....*....|....
gi 769946247  546 HMISSVQLFGVNEN 559
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
30-417 3.40e-28

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 117.28  E-value: 3.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  30 ANTKNVSDMTENSTMEKQMWTCSMHPQIMQPEPGDCPICGMDLIP------AETGAEGLAMNEIKMSDnamalANIQTTI 103
Cdd:PRK09783  26 AKAEPPAEKTSTAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPkyadeeSSASSGGVRIDPTQTQN-----LGVKTAT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 104 VGNVSGTDENTIqlSGKIMANEEANAVQASYFEGRIEKLNVNFTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKeSQP 183
Cdd:PRK09783 101 VTRGPLTFAQTF--PANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDWVEAQSEYLLLRETG-GTA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 184 ALYKAVRNKLKLWKLSETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQI 263
Cdd:PRK09783 178 TQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 264 SQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMfvTAKVAMTKGSDNMetqITVPAT 343
Cdd:PRK09783 258 WLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGM--NAWLQLNTASEPM---LLIPSQ 332
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 769946247 344 AVMWTGERSlvYVKTNPNEPVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTVDAAAQLQGKKSMMNATG 417
Cdd:PRK09783 333 ALIDTGSEQ--RVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERMRSES 404
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
49-75 3.79e-11

Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins.


Pssm-ID: 437167 [Multi-domain]  Cd Length: 28  Bit Score: 57.61  E-value: 3.79e-11
                          10        20
                  ....*....|....*....|....*..
gi 769946247   49 WTCSMHPQIMQPEPGDCPICGMDLIPA 75
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
PRK09859 PRK09859
multidrug transporter subunit MdtE;
262-396 1.70e-04

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 44.32  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 262 QISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAKVamTKGSdnMETQITVP 341
Cdd:PRK09859 230 QIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALV--DEGS--RQNVLLVP 305
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 769946247 342 ATAVMWTGERSLVYVKTNPNEpVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNG 396
Cdd:PRK09859 306 QEGVTHNAQGKATALILDKDD-VVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
217-246 3.63e-03

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: 36.24  E-value: 3.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 769946247 217 PIYATVSGTVSQKIAEEGDYVKQGQPIVKV 246
Cdd:cd06850   38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
113-321 1.05e-92

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: 284.01  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  113 NTIQLSGKIMANEEANAVQASYFEGRIEKLNVNFTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPA--LYKAVR 190
Cdd:pfam16576   4 RTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKseLLRAAR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  191 NKLKLWKLSETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQISQLKEGQ 270
Cdd:pfam16576  84 QRLRLLGMPEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQ 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 769946247  271 KITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFV 321
Cdd:pfam16576 164 PAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
107-412 2.55e-75

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: 242.93  E-value: 2.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 107 VSGTDENTIQLSGKIMANEEANavQASYFEGRIEKLNVNfTGEEVRRGQLLATIYAPT----LVAAQQELLTA-ASMKES 181
Cdd:COG0845    4 ERGDVPETVEATGTVEARREVE--VRARVSGRVEEVLVD-EGDRVKKGQVLARLDPPDlqaaLAQAQAQLAAAqAQLELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 182 QP------ALYK-------AVRNKLKLWKLSETQIN----QIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIV 244
Cdd:COG0845   81 KAelerykALLKkgavsqqELDQAKAALDQAQAALAaaqaALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 245 KVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAK 324
Cdd:COG0845  161 TIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 325 VAMTKGSDnmetQITVPATAVMWTGERSLVYVKTNPNepVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTVDAAA 404
Cdd:COG0845  241 IVLGEREN----ALLVPASAVVRDGGGAYVFVVDADG--KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGA 314

                 ....*...
gi 769946247 405 QLQGKKSM 412
Cdd:COG0845  315 KVRVVEAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
108-400 2.17e-47

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: 168.65  E-value: 2.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  108 SGTDENTIQLSGKIMANEEAN-AVQASyfeGRIEKLNVNfTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPALY 186
Cdd:TIGR01730   8 SETLANTLTFPGSLEAVDEADlAAEVA---GKITKISVR-EGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  187 KAVRNKL-KLWKLS-----------------ETQINQIESS-GKVRENFP---IYATVSGTVSQKIAEEGDYVKQGQPIV 244
Cdd:TIGR01730  84 QRSFERAeRLVKRNavsqadlddakaaveaaQADLEAAKASlASAQLNLRyteIRAPFDGTIGRRLVEVGAYVTAGQTLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  245 KVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAK 324
Cdd:TIGR01730 164 TIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRVT 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 769946247  325 VaMTKGSDNMetqITVPATAVMWTGERSLVYVKTNPNepVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTV 400
Cdd:TIGR01730 244 I-SLKVRSSA---IVVPTQAVIEDLNGKYVYVVKNDG--KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKL 313
DUF3347 pfam11827
Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized ...
466-559 1.44e-32

Protein of unknown function (DUF3347); This entry represents a functionally uncharacterized domain found in bacterial proteins.


Pssm-ID: 432106  Cd Length: 93  Bit Score: 120.57  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  466 VFDDYILLKDALVNDDAKNAQEAGNQINQSLKKVDMKLLSdEKAHNHWMTIQKELKTSANAIENSSDIATQRGHFKHLSA 545
Cdd:pfam11827   1 VYQSYLNLKDALVADDAKEAKSAAAKLLASLKAVDMSLLT-EKAHNEWMDILEDLKEHAEHIAEATDIEHQREHFSDLSE 79
                          90
                  ....*....|....
gi 769946247  546 HMISSVQLFGVNEN 559
Cdd:pfam11827  80 DMIDLVKAFGLSSG 93
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
30-417 3.40e-28

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 117.28  E-value: 3.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  30 ANTKNVSDMTENSTMEKQMWTCSMHPQIMQPEPGDCPICGMDLIP------AETGAEGLAMNEIKMSDnamalANIQTTI 103
Cdd:PRK09783  26 AKAEPPAEKTSTAERKVLFWYDPMYPNTRFDKPGKSPFMDMDLVPkyadeeSSASSGGVRIDPTQTQN-----LGVKTAT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 104 VGNVSGTDENTIqlSGKIMANEEANAVQASYFEGRIEKLNVNFTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKeSQP 183
Cdd:PRK09783 101 VTRGPLTFAQTF--PANVSYNEYQYAIVQARAAGFIDKVYPLTVGDKVQKGTPLLDLTIPDWVEAQSEYLLLRETG-GTA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 184 ALYKAVRNKLKLWKLSETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQI 263
Cdd:PRK09783 178 TQTEGILERLRLAGMPEADIRRLIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 264 SQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMfvTAKVAMTKGSDNMetqITVPAT 343
Cdd:PRK09783 258 WLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGM--NAWLQLNTASEPM---LLIPSQ 332
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 769946247 344 AVMWTGERSlvYVKTNPNEPVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTVDAAAQLQGKKSMMNATG 417
Cdd:PRK09783 333 ALIDTGSEQ--RVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGLFLIDSEANISGALERMRSES 404
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
93-325 1.85e-25

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 107.44  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  93 AMALANIQTTIVGNVSGTDENTIQLSGKIMANEeaNAVQASYfEGRIEKLNVNfTGEEVRRGQLLATIYAPTLVA----- 167
Cdd:COG1566   13 VLLLLALGLALWAAGRNGPDEPVTADGRVEARV--VTVAAKV-SGRVTEVLVK-EGDRVKKGQVLARLDPTDLQAalaqa 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 168 --------AQQELLTAASMKESQPALYKAVRNKLK---------------LWK----------------------LSETQ 202
Cdd:COG1566   89 eaqlaaaeAQLARLEAELGAEAEIAAAEAQLAAAQaqldlaqreleryqaLYKkgavsqqeldearaaldaaqaqLEAAQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 203 ------INQIESSGKVRENFP--------------------IYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMF 256
Cdd:COG1566  169 aqlaqaQAGLREEEELAAAQAqvaqaeaalaqaelnlarttIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEA 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 257 DAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKS----------RTVSVRTTLNNKEDI-LKPGMFVTAKV 325
Cdd:COG1566  249 YVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSppknatgnvvQRYPVRIRLDNPDPEpLRPGMSATVEI 328
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
218-318 3.50e-18

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: 80.10  E-value: 3.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  218 IYATVSGTVSQKIAEEGDYVKQGQPIVKVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNT 297
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVDP 81
                          90       100
                  ....*....|....*....|...
gi 769946247  298 KSRTVSVRTTL--NNKEDILKPG 318
Cdd:pfam13437  82 DTGVIPVRVSIenPKTPIPLLPG 104
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
114-394 8.59e-15

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: 75.54  E-value: 8.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  114 TIQLSGKIMANEEANAVQASyFEGRIEKLNVNfTGEEVRRGQLLATIYAPTLVAAQQELLTAASMKESQPALYKAVRNKL 193
Cdd:pfam00529   7 GVEAPGRVVVSGNAKAVQPQ-VSGIVTRVLVK-EGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  194 KLWKLS----------------------ETQINQIESSGKVRENFPIYATVSGTVSQKIAEEGDYVKQGQPIVK--VSDL 249
Cdd:pfam00529  85 QALESElaisrqdydgataqlraaqaavKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLatVAQL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  250 GTVWAMFDAYERQISQLKEGQKITVT----------TNAYPNKE-------FEATVSFIDPvlNTKSRTVSVRTTL---N 309
Cdd:pfam00529 165 DQIYVQITQSAAENQAEVRSELSGAQlqiaeaeaelKLAKLDLErteirapVDGTVAFLSV--TVDGGTVSAGLRLmfvV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247  310 NKEDILKPGMFVTAKVamTKGSDNMEtqITVPATAVMwTGERSLVYVKTNPNEPVFEMRAVTLGNKNGDVYTITEGLSNG 389
Cdd:pfam00529 243 PEDNLLVPGMFVETQL--DQVRVGQP--VLIPFDAFP-QTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAG 317

                  ....*
gi 769946247  390 EEVVT 394
Cdd:pfam00529 318 ALVRL 322
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
148-396 1.62e-13

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 72.90  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 148 GEEVRRGQLLATI----YAPTLVAAQQELltaasmKESQPALYKAVRNKLKLWKLSETQ-------------INQIESSG 210
Cdd:PRK11556 106 GQQVKAGDLLAEIdprpFKVALAQAQGQL------AKDQATLANARRDLARYQQLAKTNlvsrqeldaqqalVSETEGTI 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 211 KVRENF-----------PIYATVSGTVSQKIAEEGDYVKQGQ--PIVKVSDLGTVWAMFDAYERQISQL----KEGQKIT 273
Cdd:PRK11556 180 KADEASvasaqlqldysRITAPISGRVGLKQVDVGNQISSGDttGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLV 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 274 VTTNAYPNKEF--EATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAKVAMtkgsDNMETQITVPATAVMWTGER 351
Cdd:PRK11556 260 VEAWDRTNSKKlsEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLV----DTLQNAVVIPTAALQMGNEG 335
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 769946247 352 SLVYVKTNPNEpvFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNG 396
Cdd:PRK11556 336 HFVWVLNDENK--VSKHLVTPGIQDSQKVVISAGLSAGDRVVTDG 378
HMBD pfam19335
Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple ...
49-75 3.79e-11

Heavy metal binding domain; This domain is a copper-binding domain found in single or multiple copies at the N-terminus of a wide variety of copper or other heavy metal binding transporters and other proteins.


Pssm-ID: 437167 [Multi-domain]  Cd Length: 28  Bit Score: 57.61  E-value: 3.79e-11
                          10        20
                  ....*....|....*....|....*..
gi 769946247   49 WTCSMHPQIMQPEPGDCPICGMDLIPA 75
Cdd:pfam19335   2 YICPMHPDITSDKPGKCPICGMALVPV 28
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
148-406 1.84e-10

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 62.89  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 148 GEEVRRGQLLATIYAPTLVAAQQElltAASMKESQPALYKAVRNKLKLWK-----------------LSETQINQIESSG 210
Cdd:PRK09578  82 GQEVKQGAVLFRIDPAPLKAARDA---AAGALAKAEAAHLAALDKRRRYDdlvrdravserdyteavADERQAKAAVASA 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 211 KV---RENFPI-YATV----SGTVSQKIAEEGDYVKQGQ--PIVKVSDLGTVWAMF-------DAYERQIsqlKEGQ--- 270
Cdd:PRK09578 159 KAelaRAQLQLdYATVtapiDGRARRALVTEGALVGQDQatPLTTVEQLDPIYVNFsqpaadvEALRRAV---KSGRatg 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 271 ----KITVTT-----NAYPNKefeATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVtaKVAMTKGSDNmeTQITVP 341
Cdd:PRK09578 236 iaqqDVAVTLvradgSEYPLK---GKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYV--RIALDRAVNP--RAILVP 308
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 769946247 342 ATAVMWTGERSLVYVkTNPNEPVFEMRAVTLGNKNGDvYTITEGLSNGEEVVtngtftVDAAAQL 406
Cdd:PRK09578 309 RDALLRTADSASVKV-VGQNGKVRDVEVEADQMSGRD-WIVTRGLAGGERVI------VDNAAQF 365
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
218-410 2.54e-06

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 50.10  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 218 IYATVSGTVSQKIAEEGDYVKQGQP--IVKVSDLGTVWAMFDAYERQISQLKE------------GQKITVTTN---AYP 280
Cdd:PRK15030 176 VTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPIYVDVTQSSNDFLRLKQelangtlkqengKAKVSLITSdgiKFP 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 281 NkefEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAKvaMTKGSDnmETQITVPATAVMWT--GERSLVYVKT 358
Cdd:PRK15030 256 Q---DGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRAR--LEEGLN--PNAILVPQQGVTRTprGDATVLVVGA 328
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 769946247 359 NPNepvFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNGTFTVDAAAQLQGKK 410
Cdd:PRK15030 329 DDK---VETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQE 377
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
162-394 3.66e-05

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 46.31  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 162 APTLVAAQQELLTAAS---MKESQPALYKAVRNKLKLwKLSETQINQiessgkvrENFPIYATVSGTVSQKIAEEGDYV- 237
Cdd:PRK11578 136 AKTQAVSQQDLDTAATelaVKQAQIGTIDAQIKRNQA-SLDTAKTNL--------DYTRIVAPMAGEVTQITTLQGQTVi 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 238 --KQGQPIVKVSDLGTVWAMFDAYERQISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTV--SVRTTLNNKED 313
Cdd:PRK11578 207 aaQQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIfyYARFEVPNPNG 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 314 ILKPGMfvTAKVAMTkgSDNMETQITVPATAV--MWTGERSLVYVKTNPNEpvfEMRAVTLGNKNGDVYTITEGLSNGEE 391
Cdd:PRK11578 287 LLRLDM--TAQVHIQ--LTDVKNVLTIPLSALgdPVGDNRYKVKLLRNGET---REREVTIGARNDTDVEIVKGLEAGDE 359

                 ...
gi 769946247 392 VVT 394
Cdd:PRK11578 360 VII 362
PRK09859 PRK09859
multidrug transporter subunit MdtE;
262-396 1.70e-04

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 44.32  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769946247 262 QISQLKEGQKITVTTNAYPNKEFEATVSFIDPVLNTKSRTVSVRTTLNNKEDILKPGMFVTAKVamTKGSdnMETQITVP 341
Cdd:PRK09859 230 QIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALV--DEGS--RQNVLLVP 305
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 769946247 342 ATAVMWTGERSLVYVKTNPNEpVFEMRAVTLGNKNGDVYTITEGLSNGEEVVTNG 396
Cdd:PRK09859 306 QEGVTHNAQGKATALILDKDD-VVQLREIEASKAIGDQWVVTSGLQAGDRVIVSG 359
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
217-246 3.63e-03

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: 36.24  E-value: 3.63e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 769946247 217 PIYATVSGTVSQKIAEEGDYVKQGQPIVKV 246
Cdd:cd06850   38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
 
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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