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Conserved domains on  [gi|648489891|ref|WP_026181642|]
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MULTISPECIES: efflux RND transporter periplasmic adaptor subunit [unclassified Thioalkalivibrio]

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 ...
 45-388 1.16e-63

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: 206.72  E-value: 1.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  45 TRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREAQMQYGREVVS 124
Cdd:COG0845   11 TVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 125 PQSRSIGQmpgmgipSMFDQMFTQpagqmmgmgdpaldrrtdlysryigVDQAQARWEQARARVAELDAAIRDTRSEAPF 204
Cdd:COG0845   91 LKKGAVSQ-------QELDQAKAA-------------------------LDQAQAALAAAQAALEQARANLAYTTIRAPF 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 205 DGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGD--EVEARVAQIFPLADPQRHTV 282
Cdd:COG0845  139 DGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAVDPATRTV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 283 TVKFDLPQGVRG-GPGMHAAVHLPQGEASgNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLE 361
Cdd:COG0845  219 RVRAELPNPDGLlRPGMFVRVRIVLGERE-NALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLK 297

                        330       340
                 ....*....|....*....|....*..
gi 648489891 362 PGMQILARPGAGVRSGQPVGSRAPDSG 388
Cdd:COG0845  298 AGDRVVVSGLQRLRDGAKVRVVEAAAP 324
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 45-388 1.16e-63

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: 206.72  E-value: 1.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  45 TRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREAQMQYGREVVS 124
Cdd:COG0845   11 TVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 125 PQSRSIGQmpgmgipSMFDQMFTQpagqmmgmgdpaldrrtdlysryigVDQAQARWEQARARVAELDAAIRDTRSEAPF 204
Cdd:COG0845   91 LKKGAVSQ-------QELDQAKAA-------------------------LDQAQAALAAAQAALEQARANLAYTTIRAPF 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 205 DGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGD--EVEARVAQIFPLADPQRHTV 282
Cdd:COG0845  139 DGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAVDPATRTV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 283 TVKFDLPQGVRG-GPGMHAAVHLPQGEASgNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLE 361
Cdd:COG0845  219 RVRAELPNPDGLlRPGMFVRVRIVLGERE-NALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLK 297

                        330       340
                 ....*....|....*....|....*..
gi 648489891 362 PGMQILARPGAGVRSGQPVGSRAPDSG 388
Cdd:COG0845  298 AGDRVVVSGLQRLRDGAKVRVVEAAAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 34-380 1.49e-44

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: 156.71  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891   34 PVLTVEP-DKAATRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIR 112
Cdd:TIGR01730   2 TVATVESeTLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  113 EAQMQYGRevvspqsrsigqmpgmgipsmFDQMFTQPAGQmmgmgdpaldrRTDLYSRYIGVDQAQARWEQARARVAELD 192
Cdd:TIGR01730  82 LAQRSFER---------------------AERLVKRNAVS-----------QADLDDAKAAVEAAQADLEAAKASLASAQ 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  193 AAIRDTRSEAPFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDT--GDEVEARVAQ 270
Cdd:TIGR01730 130 LNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDAlpGEEFKGKLRF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  271 IFPLADPQRHTVTVKFDLP---QGVRGGPGMHAAVHLPqgeASGNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLG 347
Cdd:TIGR01730 210 IDPRVDSGTGTVRVRATFPnpdGRLLPGMFGRVTISLK---VRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVG 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 648489891  348 GSRGDQVVVTSGLEPGMQILARPGAGVRSGQPV 380
Cdd:TIGR01730 287 LRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 202-300 1.57e-11

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: 63.29  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  202 APFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDT--GDEVEARVAQIFPLADPQR 279
Cdd:pfam16576 113 APISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPAlpGKTFEGKVDYIYPTLDPKT 192

                          90       100
                  ....*....|....*....|..
gi 648489891  280 HTVTVKFDLP-QGVRGGPGMHA 300
Cdd:pfam16576 193 RTVRVRIELPnPDGRLKPGMFA 214
PRK09859 PRK09859
multidrug transporter subunit MdtE;
35-376 5.62e-10

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 60.50  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  35 VLTVEPDKAA-TRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIRE 113
Cdd:PRK09859  38 VVTLSPGSVNvLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 114 AQMQYGREVVSPQSRSIGQMPgmgipsmFDqmftqpagqmmgmgdpalDRRTDLYSRYIGVDQAQARWEQA--RARVAEL 191
Cdd:PRK09859 118 ARITFNRQASLLKTNYVSRQD-------YD------------------TARTQLNEAEANVTVAKAAVEQAtiNLQYANV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 192 DAAIRDT--RSEAPFDGLVMHKHVEEGDTVQPGQPL---LTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGDEVEA 266
Cdd:PRK09859 173 TSPITGVsgKSSVTVGALVTANQADSLVTVQRLDPIyvdLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQ 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 267 RVAQIF--PLADPQRHTVTVK--FDLPQGvRGGPGMHAAVHLPQGeASGNRVVIPRSALIPGGALPRVA-VLDGEGHVRV 341
Cdd:PRK09859 253 TGTLKFsdPTVDETTGSVTLRaiFPNPNG-DLLPGMYVTALVDEG-SRQNVLLVPQEGVTHNAQGKATAlILDKDDVVQL 330

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648489891 342 RMVRLGGSRGDQVVVTSGLEPGMQILA------RPGAGVRS 376
Cdd:PRK09859 331 REIEASKAIGDQWVVTSGLQAGDRVIVsglqriRPGIKARA 371
RND-peri-MexC NF033138
MexC family multidrug efflux RND transporter periplasmic adaptor subunit;
27-385 1.73e-05

MexC family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 411094  Cd Length: 375  Bit Score: 46.66  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  27 GMAHASGPVLTV----EPdKAATRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQA 102
Cdd:NF033138  30 AAAEVARPVEVVavatEP-LALTSELPGRVEPMRVAEVRARVAGIVLQKRFEEGADVKAGDLLFQIDPAPLKAALSRAEG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 103 EMRTTEAAIREAQMQYGRevvspqsrsigQMPGMGIPSMFDQMFtqpagqmmgmgDPALdrrTDLYSRYIGVDQAQARWE 182
Cdd:NF033138 109 ELARAQAVLLEAQARVKR-----------YEPLVKIEAVSQQDF-----------DTAT---ADLRSAQAATRSAQADLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 183 QARARVAEldaairdTRSEAPFDGLVMHKHVEEGDTVQPGQPLL--------------TFGHVEYLRV-EAQVPVRLVAG 247
Cdd:NF033138 164 TARLNLGY-------ASVTAPISGRIGRALVTEGALVGQGDATLmariqqldpiyvdfTQSAADALRLrEALKDGALAAG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 248 lqEDDYVHVRLDtGDEVEARVAQIFPLADPQRHTVTV----KFDLPQGVRGgPGMHAAVHLPQGEASGNRVVIPRSALIP 323
Cdd:NF033138 237 --DSQALSIRVE-GTDYERQGALMFTDVAVDRGTGQVslrgKFDNADGVLL-PGMYVRVRTPQGTDNQAILVPQRAVQRG 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489891 324 GGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLEPGMQILARPGAGVRSGQPVGSRAP 385
Cdd:NF033138 313 SDGSAQVMVVGADGRAEARSVRTGAMQGSRWQISEGLKAGDQVIVGGLAGLQPGAKVVPKQA 374
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 201-228 1.50e-03

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 37.00  E-value: 1.50e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489891 201 EAPFDGLVMHKHVEEGDTVQPGQPLLTF 228
Cdd:cd06849   47 EAPAAGVLAKILVEEGDTVPVGQVIAVI 74
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 45-388 1.16e-63

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: 206.72  E-value: 1.16e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  45 TRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREAQMQYGREVVS 124
Cdd:COG0845   11 TVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 125 PQSRSIGQmpgmgipSMFDQMFTQpagqmmgmgdpaldrrtdlysryigVDQAQARWEQARARVAELDAAIRDTRSEAPF 204
Cdd:COG0845   91 LKKGAVSQ-------QELDQAKAA-------------------------LDQAQAALAAAQAALEQARANLAYTTIRAPF 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 205 DGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGD--EVEARVAQIFPLADPQRHTV 282
Cdd:COG0845  139 DGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAVDPATRTV 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 283 TVKFDLPQGVRG-GPGMHAAVHLPQGEASgNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLE 361
Cdd:COG0845  219 RVRAELPNPDGLlRPGMFVRVRIVLGERE-NALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLK 297

                        330       340
                 ....*....|....*....|....*..
gi 648489891 362 PGMQILARPGAGVRSGQPVGSRAPDSG 388
Cdd:COG0845  298 AGDRVVVSGLQRLRDGAKVRVVEAAAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 34-380 1.49e-44

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: 156.71  E-value: 1.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891   34 PVLTVEP-DKAATRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIR 112
Cdd:TIGR01730   2 TVATVESeTLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  113 EAQMQYGRevvspqsrsigqmpgmgipsmFDQMFTQPAGQmmgmgdpaldrRTDLYSRYIGVDQAQARWEQARARVAELD 192
Cdd:TIGR01730  82 LAQRSFER---------------------AERLVKRNAVS-----------QADLDDAKAAVEAAQADLEAAKASLASAQ 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  193 AAIRDTRSEAPFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDT--GDEVEARVAQ 270
Cdd:TIGR01730 130 LNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDAlpGEEFKGKLRF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  271 IFPLADPQRHTVTVKFDLP---QGVRGGPGMHAAVHLPqgeASGNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLG 347
Cdd:TIGR01730 210 IDPRVDSGTGTVRVRATFPnpdGRLLPGMFGRVTISLK---VRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVG 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 648489891  348 GSRGDQVVVTSGLEPGMQILARPGAGVRSGQPV 380
Cdd:TIGR01730 287 LRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
47-304 2.01e-25

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 105.13  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  47 TVSGTVvPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREAQMQYGREVVSPQ 126
Cdd:COG1566   36 TADGRV-EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 127 SRSIGQM--------------------PGMGIPSMFDQMFTQ--PAGQMMGMGDPALDRRTDLYSRYIGVDQAQARWEQA 184
Cdd:COG1566  115 AEAQLAAaqaqldlaqreleryqalykKGAVSQQELDEARAAldAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQA 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 185 RARVAELDAAIRDTRSEAPFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGD-- 262
Cdd:COG1566  195 EAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPdr 274

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648489891 263 EVEARVAQIFPLADP------------QRHTVTVKFDLPQGVRGGPGMHAAVHL 304
Cdd:COG1566  275 VFEGKVTSISPGAGFtsppknatgnvvQRYPVRIRLDNPDPEPLRPGMSATVEI 328
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 202-300 1.57e-11

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: 63.29  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  202 APFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDT--GDEVEARVAQIFPLADPQR 279
Cdd:pfam16576 113 APISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPAlpGKTFEGKVDYIYPTLDPKT 192

                          90       100
                  ....*....|....*....|..
gi 648489891  280 HTVTVKFDLP-QGVRGGPGMHA 300
Cdd:pfam16576 193 RTVRVRIELPnPDGRLKPGMFA 214
PRK09859 PRK09859
multidrug transporter subunit MdtE;
35-376 5.62e-10

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 60.50  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  35 VLTVEPDKAA-TRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIRE 113
Cdd:PRK09859  38 VVTLSPGSVNvLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASN 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 114 AQMQYGREVVSPQSRSIGQMPgmgipsmFDqmftqpagqmmgmgdpalDRRTDLYSRYIGVDQAQARWEQA--RARVAEL 191
Cdd:PRK09859 118 ARITFNRQASLLKTNYVSRQD-------YD------------------TARTQLNEAEANVTVAKAAVEQAtiNLQYANV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 192 DAAIRDT--RSEAPFDGLVMHKHVEEGDTVQPGQPL---LTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGDEVEA 266
Cdd:PRK09859 173 TSPITGVsgKSSVTVGALVTANQADSLVTVQRLDPIyvdLTQSVQDFLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQ 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 267 RVAQIF--PLADPQRHTVTVK--FDLPQGvRGGPGMHAAVHLPQGeASGNRVVIPRSALIPGGALPRVA-VLDGEGHVRV 341
Cdd:PRK09859 253 TGTLKFsdPTVDETTGSVTLRaiFPNPNG-DLLPGMYVTALVDEG-SRQNVLLVPQEGVTHNAQGKATAlILDKDDVVQL 330

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 648489891 342 RMVRLGGSRGDQVVVTSGLEPGMQILA------RPGAGVRS 376
Cdd:PRK09859 331 REIEASKAIGDQWVVTSGLQAGDRVIVsglqriRPGIKARA 371
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 48-279 2.43e-09

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: 58.20  E-value: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891   48 VSGTVVPYREV-TLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREAQMQYGREVVSPQ 126
Cdd:pfam00529  10 APGRVVVSGNAkAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALES 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  127 SRSIGQMPGMGIPSMFDQMFTQ---------------------------PAGQMMGMG----------DPALDRRTDLYS 169
Cdd:pfam00529  90 ELAISRQDYDGATAQLRAAQAAvkaaqaqlaqaqidlarrrvlapiggiSRESLVTAGalvaqaqanlLATVAQLDQIYV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  170 RYIGVDQAQARW-----EQARARVAELDAAIRDTRSE-------APFDGLVMHKHVE-EGDTVQPGQPLLTFGHVEYLRV 236
Cdd:pfam00529 170 QITQSAAENQAEvrselSGAQLQIAEAEAELKLAKLDlerteirAPVDGTVAFLSVTvDGGTVSAGLRLMFVVPEDNLLV 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 648489891  237 EAQVPVRLVAGLQEDDYVHVRLD-----TGDEVEARVAQIFPLADPQR 279
Cdd:pfam00529 250 PGMFVETQLDQVRVGQPVLIPFDafpqtKTGRFTGVVVGISPDTGPVR 297
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 202-290 8.01e-08

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: 50.05  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  202 APFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGDE--VEARVAQIFPLADPQR 279
Cdd:pfam13437   4 APVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDytLEGKVVRISPTVDPDT 83

                          90
                  ....*....|.
gi 648489891  280 HTVTVKFDLPQ 290
Cdd:pfam13437  84 GVIPVRVSIEN 94
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
3-393 2.25e-06

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 49.41  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891   3 KRFSRLFLSALLTLPLISLGSGGVGMAHASGP------VLTVEPdKAATRTVS--GTVVPYREVTLTAQSAGRVVQVAGA 74
Cdd:PRK09578   2 EWARRRRLLLAALVALFVLAGCGKGDSDAAAAapreatVVTVRP-TSVPMTVElpGRLDAYRQAEVRARVAGIVTARTYE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  75 EGDRFEQDSVLVSISDDRLRAQRQAAQAEMRTTEAAIREA--QMQYGREVVSPQSRSigqmpgmgipsmfdqmftqpagq 152
Cdd:PRK09578  81 EGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAAldKRRRYDDLVRDRAVS----------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 153 mmgmgdpaldrRTDLYSRYIGVDQAQARWEQARARVAELDAAIRDTRSEAPFDGLVMHKHVEEGDTVQPGQ--PLLTFGH 230
Cdd:PRK09578 138 -----------ERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALVGQDQatPLTTVEQ 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 231 VEYLRVEAQVPVRLVAGL-------------QEDDYVHVRLDTGDEVEARVAQIFP-LA-DPQRHTVTVKFDLPQGVRG- 294
Cdd:PRK09578 207 LDPIYVNFSQPAADVEALrravksgratgiaQQDVAVTLVRADGSEYPLKGKLLFSdLAvDPTTDTVAMRALFPNPEREl 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 295 GPGMHAAVHLPQGEASgNRVVIPRSALIPGGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLEPGMQILARPGAGV 374
Cdd:PRK09578 287 LPGAYVRIALDRAVNP-RAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQF 365

                        410
                 ....*....|....*....
gi 648489891 375 RSGQPVGSRAPDSGGSADP 393
Cdd:PRK09578 366 APGTAVKAVERAPAAKPAP 384
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 14-373 2.73e-06

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 49.00  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  14 LTLPLISLGSGGVGMAHASGPV-----LTVEP-DKAATRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVS 87
Cdd:PRK11578  12 LIALVIVLAGGITLWRILNAPVptyqtLIVRPgDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  88 ISDDR--------------LRAQRQAAQAEMRTTEAAIREAQMQYGREVVSPQSrsigqmpgmgipsmFDQMFTQPAgqm 153
Cdd:PRK11578  92 IDPEQaenqikeveatlmeLRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQD--------------LDTAATELA--- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 154 mgmgdpaldrrtdLYSRYIGVDQAQARWEQARARVAELDaaIRDTRSEAPFDGLVMHKHVEEGDTV---QPGQPLLTFGH 230
Cdd:PRK11578 155 -------------VKQAQIGTIDAQIKRNQASLDTAKTN--LDYTRIVAPMAGEVTQITTLQGQTViaaQQAPNILTLAD 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 231 VEYLRVEAQVpvrlvaglQEDDYVHVRL----------DTGDEVEARVAQIFPLADPQRHTV--TVKFDLP--QGVRgGP 296
Cdd:PRK11578 220 MSTMLVKAQV--------SEADVIHLKPgqkawftvlgDPLTRYEGVLKDILPTPEKVNDAIfyYARFEVPnpNGLL-RL 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 297 GMHAAVHLpQGEASGNRVVIPRSALIP--GGALPRVAVLDGeGHVRVRMVRLGGSRGDQVVVTSGLEPGMQ-ILARPGAG 373
Cdd:PRK11578 291 DMTAQVHI-QLTDVKNVLTIPLSALGDpvGDNRYKVKLLRN-GETREREVTIGARNDTDVEIVKGLEAGDEvIIGEAKPG 368
RND-peri-MexC NF033138
MexC family multidrug efflux RND transporter periplasmic adaptor subunit;
27-385 1.73e-05

MexC family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 411094  Cd Length: 375  Bit Score: 46.66  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  27 GMAHASGPVLTV----EPdKAATRTVSGTVVPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQA 102
Cdd:NF033138  30 AAAEVARPVEVVavatEP-LALTSELPGRVEPMRVAEVRARVAGIVLQKRFEEGADVKAGDLLFQIDPAPLKAALSRAEG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 103 EMRTTEAAIREAQMQYGRevvspqsrsigQMPGMGIPSMFDQMFtqpagqmmgmgDPALdrrTDLYSRYIGVDQAQARWE 182
Cdd:NF033138 109 ELARAQAVLLEAQARVKR-----------YEPLVKIEAVSQQDF-----------DTAT---ADLRSAQAATRSAQADLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 183 QARARVAEldaairdTRSEAPFDGLVMHKHVEEGDTVQPGQPLL--------------TFGHVEYLRV-EAQVPVRLVAG 247
Cdd:NF033138 164 TARLNLGY-------ASVTAPISGRIGRALVTEGALVGQGDATLmariqqldpiyvdfTQSAADALRLrEALKDGALAAG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 248 lqEDDYVHVRLDtGDEVEARVAQIFPLADPQRHTVTV----KFDLPQGVRGgPGMHAAVHLPQGEASGNRVVIPRSALIP 323
Cdd:NF033138 237 --DSQALSIRVE-GTDYERQGALMFTDVAVDRGTGQVslrgKFDNADGVLL-PGMYVRVRTPQGTDNQAILVPQRAVQRG 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489891 324 GGALPRVAVLDGEGHVRVRMVRLGGSRGDQVVVTSGLEPGMQILARPGAGVRSGQPVGSRAP 385
Cdd:NF033138 313 SDGSAQVMVVGADGRAEARSVRTGAMQGSRWQISEGLKAGDQVIVGGLAGLQPGAKVVPKQA 374
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 53-227 2.44e-05

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 45.72  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891  53 VPYREVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLR-------AQRQAAQAEM-------RTTE---------- 108
Cdd:PRK03598  39 VDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYEnalmqakANVSVAQAQLdlmlagyRDEEiaqaraavkq 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489891 109 --AAIREAQMQYGREVVSPQSRSIGQmpgmgipSMFDQMFTQPAgqmmgMGDPALDRRTDLYSRYIG------VDQAQAR 180
Cdd:PRK03598 119 aqAAYDYAQNFYNRQQGLWKSRTISA-------NDLENARSSRD-----QAQATLKSAQDKLSQYREgnrpqdIAQAKAS 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 648489891 181 WEQARARVAELDAAIRDTRSEAPFDGLVMHKHVEEGDTVQPGQPLLT 227
Cdd:PRK03598 187 LAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFT 233
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
202-240 1.34e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 36.27  E-value: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 648489891  202 APFDGLVMHKHVEEGDTVQPGQPLLTFGHVEYL----RVEAQV 240
Cdd:pfam13533   7 SPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQlqlqQAEAQL 49
NagE COG2190
Phosphotransferase system IIA component [Carbohydrate transport and metabolism];
212-266 1.37e-03

Phosphotransferase system IIA component [Carbohydrate transport and metabolism];


Pssm-ID: 441793 [Multi-domain]  Cd Length: 154  Bit Score: 38.95  E-value: 1.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 648489891 212 HVEEGDTVQPGQPLLTFgHVEYLRVEAQVPVRLVAGLQEDDYVHVRLDTGDEVEA 266
Cdd:COG2190   92 LVKEGDKVKAGDPLIEF-DLDAIKAAGYSLITPVVVTNSDEYKSVELTKSGQVKA 145
lipoyl_domain cd06849
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ...
 201-228 1.50e-03

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


Pssm-ID: 133458 [Multi-domain]  Cd Length: 74  Bit Score: 37.00  E-value: 1.50e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489891 201 EAPFDGLVMHKHVEEGDTVQPGQPLLTF 228
Cdd:cd06849   47 EAPAAGVLAKILVEEGDTVPVGQVIAVI 74
AceF COG0508
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ...
 201-228 2.39e-03

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


Pssm-ID: 440274 [Multi-domain]  Cd Length: 77  Bit Score: 36.58  E-value: 2.39e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489891 201 EAPFDGLVMHKHVEEGDTVQPGQPLLTF 228
Cdd:COG0508   49 PAPAAGVLLEILVKEGDTVPVGAVIAVI 76
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
56-102 2.66e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 35.50  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 648489891   56 REVTLTAQSAGRVVQVAGAEGDRFEQDSVLVSISDDRLRAQRQAAQA 102
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 201-228 2.77e-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: 35.85  E-value: 2.77e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489891 201 EAPFDGLVMHKHVEEGDTVQPGQPLLTF 228
Cdd:cd06850   40 TAPVAGVVKEILVKEGDQVEAGQLLVVI 67
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 201-227 5.38e-03

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


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 36.80  E-value: 5.38e-03
                         10        20
                 ....*....|....*....|....*..
gi 648489891 201 EAPFDGLVMHKHVEEGDTVQPGQPLLT 227
Cdd:COG0511  108 EAPVSGTVVEILVENGQPVEYGQPLFV 134
 
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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