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Conserved domains on  [gi|1198427303|gb|OUN15544|]
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hypothetical protein B5G38_09725 [Gemmiger sp. An87]

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

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 ...
51-378 3.59e-45

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: 158.18  E-value: 3.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  51 TLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQeavaAEKQQNELSI 130
Cdd:COG0845     2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQ----AQLAAAQAQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 131 SQAQRRLEdaRNQKAIDEGVTADWEQTEKDAKLRQDSLAIEDAQdvlvnavaaadapsaaaQQLKTLQSAKAQCTITAPC 210
Cdd:COG0845    78 ELAKAELE--RYKALLKKGAVSQQELDQAKAALDQAQAALAAAQ-----------------AALEQARANLAYTTIRAPF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 211 SGTVTQVKAVVG---GAAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGAKD--VFHGSITWIAPKAtvnENGE 285
Cdd:COG0845   139 DGVVGERNVEPGqlvSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAV---DPAT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 286 ASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVGTDENGeAVVYRKDTDAegnvTFTPIPVTTGMETELSV 365
Cdd:COG0845   216 RTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGG-AYVFVVDADG----KVERRPVTLGRRDGDQV 290
                         330
                  ....*....|...
gi 1198427303 366 EVSgEGLTEGMEL 378
Cdd:COG0845   291 EVL-SGLKAGDRV 302
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
51-378 3.59e-45

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: 158.18  E-value: 3.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  51 TLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQeavaAEKQQNELSI 130
Cdd:COG0845     2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQ----AQLAAAQAQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 131 SQAQRRLEdaRNQKAIDEGVTADWEQTEKDAKLRQDSLAIEDAQdvlvnavaaadapsaaaQQLKTLQSAKAQCTITAPC 210
Cdd:COG0845    78 ELAKAELE--RYKALLKKGAVSQQELDQAKAALDQAQAALAAAQ-----------------AALEQARANLAYTTIRAPF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 211 SGTVTQVKAVVG---GAAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGAKD--VFHGSITWIAPKAtvnENGE 285
Cdd:COG0845   139 DGVVGERNVEPGqlvSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAV---DPAT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 286 ASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVGTDENGeAVVYRKDTDAegnvTFTPIPVTTGMETELSV 365
Cdd:COG0845   216 RTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGG-AYVFVVDADG----KVERRPVTLGRRDGDQV 290
                         330
                  ....*....|...
gi 1198427303 366 EVSgEGLTEGMEL 378
Cdd:COG0845   291 EVL-SGLKAGDRV 302
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
49-376 1.72e-30

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: 118.96  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  49 TFTLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVAAEKQQNEL 128
Cdd:TIGR01730   3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 129 SISQAQRRledarnqkaidegvtadweqtekdAKLRQDSLAIE-DAQDVLVNAVAAADAPSAAAQQLKTLQSAKAQCTIT 207
Cdd:TIGR01730  83 AQRSFERA------------------------ERLVKRNAVSQaDLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 208 APCSGTVTQVKAVVG---GAAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGAKD--VFHGSITWIAPKAtvnE 282
Cdd:TIGR01730 139 APFDGTIGRRLVEVGayvTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPgeEFKGKLRFIDPRV---D 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 283 NGEASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVGTDENGEAV-VYRKDTDAEgnvtftPIPVTTGMET 361
Cdd:TIGR01730 216 SGTGTVRVRATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVyVVKNDGKVS------KRPVEVGLRN 289
                         330
                  ....*....|....*
gi 1198427303 362 ELSVEVSGeGLTEGM 376
Cdd:TIGR01730 290 GGYVEIES-GLKAGD 303
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
56-307 2.85e-10

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: 59.44  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  56 DLSRTLSVSGSIQ--SAQVTEVAAAQTYPVAEVLV-SEGDVVAEGDVIATLDTTDLdaqIQVQQEAVAAEKQQNELSISQ 132
Cdd:pfam16576   1 PLSRTIRAVGRVAydERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPEL---VAAQQEYLLALRSGDALSKSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 133 aqrRLEDARNqkaidegvtadweqtekdaKLRQdsLAIEDAQdvlvnavaaadapsaaAQQLKTLQSAKAQCTITAPCSG 212
Cdd:pfam16576  78 ---LLRAARQ-------------------RLRL--LGMPEAQ----------------IAELERTGKVQPTVTVYAPISG 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 213 TVTQVKAVVGG---AAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGA--KDVFHGSITWIAPkaTVNengEAS 287
Cdd:pfam16576 118 VVTELNVREGMyvqPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPAlpGKTFEGKVDYIYP--TLD---PKT 192
                         250       260
                  ....*....|....*....|..
gi 1198427303 288 YAVKV--SVDDATEALRLGMTA 307
Cdd:pfam16576 193 RTVRVriELPNPDGRLKPGMFA 214
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
49-328 6.99e-09

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 57.09  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  49 TFTLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVA---AEKQQ 125
Cdd:PRK11578   38 TLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMelrAQRQQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 126 NELSISQAQRRLedARNQKAIDEGVTA--DWEQTEKDAKLRQDSLAIEDAQdvlvnavaaadaPSAAAQQLKTLQSAKAQ 203
Cdd:PRK11578  118 AEAELKLARVTL--SRQQRLAKTQAVSqqDLDTAATELAVKQAQIGTIDAQ------------IKRNQASLDTAKTNLDY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 204 CTITAPCSGTVTQVKAVVGGA------AGAIATIENQSALEALLSVREYDINQLAVGQSVTLTS-GAKDV-FHGSITWIA 275
Cdd:PRK11578  184 TRIVAPMAGEVTQITTLQGQTviaaqqAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVlGDPLTrYEGVLKDIL 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1198427303 276 PKATvNENGEASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVG 328
Cdd:PRK11578  264 PTPE-KVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALG 315
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
51-378 3.59e-45

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: 158.18  E-value: 3.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  51 TLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQeavaAEKQQNELSI 130
Cdd:COG0845     2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQ----AQLAAAQAQL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 131 SQAQRRLEdaRNQKAIDEGVTADWEQTEKDAKLRQDSLAIEDAQdvlvnavaaadapsaaaQQLKTLQSAKAQCTITAPC 210
Cdd:COG0845    78 ELAKAELE--RYKALLKKGAVSQQELDQAKAALDQAQAALAAAQ-----------------AALEQARANLAYTTIRAPF 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 211 SGTVTQVKAVVG---GAAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGAKD--VFHGSITWIAPKAtvnENGE 285
Cdd:COG0845   139 DGVVGERNVEPGqlvSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPgkTFEGKVTFIDPAV---DPAT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 286 ASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVGTDENGeAVVYRKDTDAegnvTFTPIPVTTGMETELSV 365
Cdd:COG0845   216 RTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGG-AYVFVVDADG----KVERRPVTLGRRDGDQV 290
                         330
                  ....*....|...
gi 1198427303 366 EVSgEGLTEGMEL 378
Cdd:COG0845   291 EVL-SGLKAGDRV 302
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
49-376 1.72e-30

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: 118.96  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  49 TFTLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVAAEKQQNEL 128
Cdd:TIGR01730   3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 129 SISQAQRRledarnqkaidegvtadweqtekdAKLRQDSLAIE-DAQDVLVNAVAAADAPSAAAQQLKTLQSAKAQCTIT 207
Cdd:TIGR01730  83 AQRSFERA------------------------ERLVKRNAVSQaDLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 208 APCSGTVTQVKAVVG---GAAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGAKD--VFHGSITWIAPKAtvnE 282
Cdd:TIGR01730 139 APFDGTIGRRLVEVGayvTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPgeEFKGKLRFIDPRV---D 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 283 NGEASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVGTDENGEAV-VYRKDTDAEgnvtftPIPVTTGMET 361
Cdd:TIGR01730 216 SGTGTVRVRATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVyVVKNDGKVS------KRPVEVGLRN 289
                         330
                  ....*....|....*
gi 1198427303 362 ELSVEVSGeGLTEGM 376
Cdd:TIGR01730 290 GGYVEIES-GLKAGD 303
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
58-314 1.89e-30

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 119.00  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  58 SRTLSVSGSIQsAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVAA---------------- 121
Cdd:COG1566    32 DEPVTADGRVE-ARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAaeaqlarleaelgaea 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 122 EKQQNELSISQAQRRLEDA-----RNQKAIDEGVTADWEQTEKDAKLRQDSLAIEDAQDVLVNAVAAADAPSAAAQQLKT 196
Cdd:COG1566   111 EIAAAEAQLAAAQAQLDLAqreleRYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 197 LQSAKAQ----------CTITAPCSGTVTQVKAVVGGAAGA---IATIENQSALEALLSVREYDINQLAVGQSVTLTSGA 263
Cdd:COG1566   191 VAQAEAAlaqaelnlarTTIRAPVDGVVTNLNVEPGEVVSAgqpLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDA 270
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1198427303 264 KD--VFHGSITWIAPKA-------TVNENGEASYAVKVSVDDAT-EALRLGMTAKAKVLLE 314
Cdd:COG1566   271 YPdrVFEGKVTSISPGAgftsppkNATGNVVQRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
56-307 2.85e-10

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: 59.44  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  56 DLSRTLSVSGSIQ--SAQVTEVAAAQTYPVAEVLV-SEGDVVAEGDVIATLDTTDLdaqIQVQQEAVAAEKQQNELSISQ 132
Cdd:pfam16576   1 PLSRTIRAVGRVAydERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPEL---VAAQQEYLLALRSGDALSKSE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 133 aqrRLEDARNqkaidegvtadweqtekdaKLRQdsLAIEDAQdvlvnavaaadapsaaAQQLKTLQSAKAQCTITAPCSG 212
Cdd:pfam16576  78 ---LLRAARQ-------------------RLRL--LGMPEAQ----------------IAELERTGKVQPTVTVYAPISG 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 213 TVTQVKAVVGG---AAGAIATIENQSALEALLSVREYDINQLAVGQSVTLTSGA--KDVFHGSITWIAPkaTVNengEAS 287
Cdd:pfam16576 118 VVTELNVREGMyvqPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPAlpGKTFEGKVDYIYP--TLD---PKT 192
                         250       260
                  ....*....|....*....|..
gi 1198427303 288 YAVKV--SVDDATEALRLGMTA 307
Cdd:pfam16576 193 RTVRVriELPNPDGRLKPGMFA 214
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
49-328 6.99e-09

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 57.09  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  49 TFTLEKGDLSRTLSVSGSIQSAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVA---AEKQQ 125
Cdd:PRK11578   38 TLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMelrAQRQQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 126 NELSISQAQRRLedARNQKAIDEGVTA--DWEQTEKDAKLRQDSLAIEDAQdvlvnavaaadaPSAAAQQLKTLQSAKAQ 203
Cdd:PRK11578  118 AEAELKLARVTL--SRQQRLAKTQAVSqqDLDTAATELAVKQAQIGTIDAQ------------IKRNQASLDTAKTNLDY 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 204 CTITAPCSGTVTQVKAVVGGA------AGAIATIENQSALEALLSVREYDINQLAVGQSVTLTS-GAKDV-FHGSITWIA 275
Cdd:PRK11578  184 TRIVAPMAGEVTQITTLQGQTviaaqqAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVlGDPLTrYEGVLKDIL 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1198427303 276 PKATvNENGEASYAVKVSVDDATEALRLGMTAKAKVLLEEKKGVFSVPLDAVG 328
Cdd:PRK11578  264 PTPE-KVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALG 315
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
205-304 4.23e-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: 50.82  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 205 TITAPCSGTVTQVKAVVGG---AAGAIATIENQSALEALLSVREYDINQLAVGQSVTLT--SGAKDVFHGSITWIAPKAT 279
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQvvqAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKldPGSDYTLEGKVVRISPTVD 80
                          90       100
                  ....*....|....*....|....*
gi 1198427303 280 vNENGEASYAVKVSVDDATEALRLG 304
Cdd:pfam13437  81 -PDTGVIPVRVSIENPKTPIPLLPG 104
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
60-311 9.26e-08

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


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 53.47  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  60 TLSVSGSIQSAQVTEVAAaqtypVAEVLVSEGDVVAEGDVIATLDTTDLDAQI--------------------------- 112
Cdd:TIGR01843  36 KVVPSGNVKVVQHLEGGI-----VREILVREGDRVKAGQVLVELDATDVEADAaelesqvlrleaevarlraeadsqaai 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 113 --------------------------------QVQQEAVAAEKQQNELSISQAQRRLEDARNQ-KAIDEGVTADWEQTEK 159
Cdd:TIGR01843 111 efpddllsaedpavpelikgqqslfesrkstlRAQLELILAQIKQLEAELAGLQAQLQALRQQlEVISEELEARRKLKEK 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 160 DAKLRQDSLAIEDA-------------------------------------QDVLVNAVAAADAPSAAAQQLKTLQSAKA 202
Cdd:TIGR01843 191 GLVSRLELLELEREraeaqgelgrleaelevlkrqidelqlerqqieqtfrEEVLEELTEAQARLAELRERLNKARDRLQ 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 203 QCTITAPCSGTVTQVKAV-VGG---AAGAIATI--ENQSAL-EALLSVReyDINQLAVGQSVTLTSGAKD-----VFHGS 270
Cdd:TIGR01843 271 RLIIRSPVDGTVQSLKVHtVGGvvqPGETLMEIvpEDDPLEiEAKLSPK--DIGFVHVGQPAEIKFSAFPyrrygILNGK 348
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1198427303 271 ITWIAPKATVNENGEAS-YAVKVSVDD-------ATEALRLGMTAKAKV 311
Cdd:TIGR01843 349 VKSISPDTFTDERGGGPyYRVRISIDQntlgigpKGLELSPGMPVTADI 397
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
83-120 3.93e-07

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 46.28  E-value: 3.93e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1198427303  83 VAEVLVSEGDVVAEGDVIATLDTTDLDAQIQVQQEAVA 120
Cdd:pfam13533  13 VVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
55-311 1.52e-05

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: 46.26  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  55 GDLSRTLSVSGSIQ-SAQVTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDLDAQIQV------------------- 114
Cdd:pfam00529   2 APLTKGVEAPGRVVvSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSaeaqlakaqaqvarlqael 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 115 -QQEAVAAEKQQNELSISQAQRRLEDAR----NQKAIDEGVTADWEQTE---------KDAKLRQDSLAIEDAQDVLVNA 180
Cdd:pfam00529  82 dRLQALESELAISRQDYDGATAQLRAAQaavkAAQAQLAQAQIDLARRRvlapiggisRESLVTAGALVAQAQANLLATV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 181 VAAADAPSAAAQQLKTLQSA-------------------------KAQCTITAPCSGTVTQVKAVVGGAAGAIAT----I 231
Cdd:pfam00529 162 AQLDQIYVQITQSAAENQAEvrselsgaqlqiaeaeaelklakldLERTEIRAPVDGTVAFLSVTVDGGTVSAGLrlmfV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 232 ENQSALEALLSVREYDINQLAVGQSVTLTSGA-----KDVFHGSITWIAPKatvnengeaSYAVKVSVDDATEA---LRL 303
Cdd:pfam00529 242 VPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAfpqtkTGRFTGVVVGISPD---------TGPVRVVVDKAQGPyypLRI 312

                  ....*...
gi 1198427303 304 GMTAKAKV 311
Cdd:pfam00529 313 GLSAGALV 320
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
83-305 7.69e-05

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 44.18  E-value: 7.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  83 VAEVLVSEGDVVAEGDVIATLDTTDL-DAQIQVQQEAVAAekqQNELSISQAQRRLED-ARNQKAIDEGvTADWEQTEKD 160
Cdd:PRK03598   54 LASLAVDEGDAVKAGQVLGELDAAPYeNALMQAKANVSVA---QAQLDLMLAGYRDEEiAQARAAVKQA-QAAYDYAQNF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 161 AKlRQDSL-----------------------AIEDAQDVLVNAVA--AADAPSAAAQQLKTLQSAKAQC-------TITA 208
Cdd:PRK03598  130 YN-RQQGLwksrtisandlenarssrdqaqaTLKSAQDKLSQYREgnRPQDIAQAKASLAQAQAALAQAelnlqdtELIA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 209 PCSGTVTQVKAVVGGAAGAIATIENQSaLEALLSVREY----DINQLAVGQSVTLTS-GAKD-VFHGSITWIAPKA---- 278
Cdd:PRK03598  209 PSDGTILTRAVEPGTMLNAGSTVFTLS-LTRPVWVRAYvderNLGQAQPGRKVLLYTdGRPDkPYHGQIGFVSPTAeftp 287
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1198427303 279 -TVnENGEAS----YAVKVSVDDATEALRLGM 305
Cdd:PRK03598  288 kTV-ETPDLRtdlvYRLRIVVTDADDALRQGM 318
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
69-263 7.30e-04

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


Pssm-ID: 213754 [Multi-domain]  Cd Length: 327  Bit Score: 41.35  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  69 SAQVTEVAAAQTYP---VAEVLVSEGDVVAEGDVIATLDTTDldaqiQVQQEAVAAEKQQNELSISQAQRRLE----DAR 141
Cdd:TIGR02971  10 EGEVVAVAAPSSGGtdrIKKLLVAEGDRVQAGQVLAELDSRP-----ERTAELDVARTQLDEAKARLAQVRAGakkgEIA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 142 NQKAIDEGVTADWEQTEKDAKLRQDSLAIEDAQ----------------------------------------------- 174
Cdd:TIGR02971  85 AQRAARAAAKLFKDVAAQQATLNRLEAELETAQrevdryrslfrdgavsasdldskalklrtaeeeleealasrseqidg 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 175 --------DVLVNAVAAADAPSAAAQQLKTLQSAKA---QCTITAPCSGTVTQVKAVVGGAAG--AIATIENQSALEALL 241
Cdd:TIGR02971 165 araalaslAEEVRETDVDLAQAEVKSALEAVQQAEAlleLTYVKAPIDGRVLKIHAREGEVIGseGILEMGDTSQMYAVA 244
                         250       260
                  ....*....|....*....|..
gi 1198427303 242 SVREYDINQLAVGQSVTLTSGA 263
Cdd:TIGR02971 245 EVYETDINRVRVGQRATITSTA 266
PDHac_trf_long TIGR01348
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ...
72-239 1.32e-03

pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]


Pssm-ID: 273566 [Multi-domain]  Cd Length: 546  Bit Score: 40.63  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303  72 VTEVAAAQTYPVAEVLVSEGDVVAEGDVIATLDTTDlDAQIQVQQEAVAAEKQQNELSISQAQrrledarNQKAIDEGVT 151
Cdd:TIGR01348  42 SMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLEVGA-GAQAQAEAKKEAAPAPTAGAPAPAAQ-------AQAAPAAGQS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1198427303 152 ADWEQ-TEKDAKLRQDSLAIEdaqdVLVNavaaADAPSAAAQQLKTLQSAKAQCTITAPCSGTVTQVKAVVG---GAAGA 227
Cdd:TIGR01348 114 SGVQEvTVPDIGDIEKVTVIE----VLVK----VGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGdsvPTGDL 185
                         170
                  ....*....|..
gi 1198427303 228 IATIENQSALEA 239
Cdd:TIGR01348 186 ILTLSVAGSTPA 197
 
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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