|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
27-356 |
1.47e-77 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 241.49 E-value: 1.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 27 AIGIVGVLVILYAWQLPPFTRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEA 106
Cdd:COG1566 11 ALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 107 QLAMKIAALnNNLQQRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQGSADIDQAKA 186
Cdd:COG1566 91 QLAAAEAQL-ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 187 ALEMSRQDLQTvIVNRGALEADVENAKAALELAQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIA 265
Cdd:COG1566 170 QLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDlWVEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 266 NIKETQLAELRVGQPVKFTVDALNNKAYQGRVESISPATGvefSAITPDNATGNfvkIAQRIPVRIEVlgKPEDAALLRP 345
Cdd:COG1566 249 YVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAG---FTSPPKNATGN---VVQRYPVRIRL--DNPDPEPLRP 320
|
330
....*....|.
gi 556299675 346 GMSVQVTIDTR 356
Cdd:COG1566 321 GMSATVEIDTE 331
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
3-356 |
4.30e-51 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 174.88 E-value: 4.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 3 QQDAAKEQanTRKNVRI----VSVFTAAAIGIVGVLVIlyawqlppftRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQ 78
Cdd:PRK15136 11 QQPVKKKG--KRKRALLlltlLFIIIGVAYGIYWFLVL----------RHHQETDDAYVAGNQVQIMSQVSGSVTKVWAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 79 DFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNAraqslksQADLKRVKELTA 158
Cdd:PRK15136 79 NTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQA-------QSDLNRRVPLGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 159 DGSLSIRE----RDAalasaaqgsadIDQAKAALEMSRQDL---QTVIVNRgALEAD--VENAKAALELAQIDLQNTRIV 229
Cdd:PRK15136 152 ANLIGREElqhaRDA-----------VASAQAQLDVAIQQYnanQAMILNT-PLEDQpaVQQAATEVRNAWLALQRTKIV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 230 APRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALN-NKAYQGRVESISPATGVE 307
Cdd:PRK15136 220 SPMTGYVSRRSVQVGAQISPTTPLMAVVPATNlWVDANFKETQLANMRIGQPATITSDIYGdDVVYTGKVVGLDMGTGSA 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 556299675 308 FSAITPDNATGNFVKIAQRIPVRIEVLGKPEDAALLRPGMSVQVTIDTR 356
Cdd:PRK15136 300 FSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTA 348
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
44-355 |
7.68e-33 |
|
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: 124.84 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 44 PFTRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRK 123
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 124 SAEATIAKND-----------------AALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQGSADIDQAKA 186
Cdd:pfam00529 83 RLQALESELAisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 187 ALEMSRQD--------LQTVIVNRGALEADVENAKAALELAQIDLQNTRIVAPRDGQLGQIAVRL-GAYVTAGTHLTTLV 257
Cdd:pfam00529 163 QLDQIYVQitqsaaenQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 258 PPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKA---YQGRVESISPATGvefsaitpdnatgnfvkiaqriPVRIEV 333
Cdd:pfam00529 243 PEDNlLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTG----------------------PVRVVV 300
|
330 340
....*....|....*....|..
gi 556299675 334 LGKPEDAALLRPGMSVQVTIDT 355
Cdd:pfam00529 301 DKAQGPYYPLRIGLSAGALVRL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
59-357 |
2.57e-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: 117.80 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 59 GQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMkiaalnnnlqqrksaeatiakndaalkn 138
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAA---------------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 139 ARAQSLKSQADLKRVKELTADGSLSirerdaalasaaqgSADIDQAKAALEmsrqdlqtvivnrgALEADVENAKAALEL 218
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVS--------------QADLDDAKAAVE--------------AAQADLEAAKASLAS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 219 AQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRV 297
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPlEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 298 ESISPAtgvefsaitPDNATGNFvkiaqriPVRIEVlgkPEDAALLRPGMSVQVTIDTRE 357
Cdd:TIGR01730 208 RFIDPR---------VDSGTGTV-------RVRATF---PNPDGRLLPGMFGRVTISLKV 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
27-356 |
1.47e-77 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 241.49 E-value: 1.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 27 AIGIVGVLVILYAWQLPPFTRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEA 106
Cdd:COG1566 11 ALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 107 QLAMKIAALnNNLQQRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQGSADIDQAKA 186
Cdd:COG1566 91 QLAAAEAQL-ARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 187 ALEMSRQDLQTvIVNRGALEADVENAKAALELAQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIA 265
Cdd:COG1566 170 QLAQAQAGLRE-EEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDlWVEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 266 NIKETQLAELRVGQPVKFTVDALNNKAYQGRVESISPATGvefSAITPDNATGNfvkIAQRIPVRIEVlgKPEDAALLRP 345
Cdd:COG1566 249 YVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAG---FTSPPKNATGN---VVQRYPVRIRL--DNPDPEPLRP 320
|
330
....*....|.
gi 556299675 346 GMSVQVTIDTR 356
Cdd:COG1566 321 GMSATVEIDTE 331
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
3-356 |
4.30e-51 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 174.88 E-value: 4.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 3 QQDAAKEQanTRKNVRI----VSVFTAAAIGIVGVLVIlyawqlppftRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQ 78
Cdd:PRK15136 11 QQPVKKKG--KRKRALLlltlLFIIIGVAYGIYWFLVL----------RHHQETDDAYVAGNQVQIMSQVSGSVTKVWAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 79 DFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNAraqslksQADLKRVKELTA 158
Cdd:PRK15136 79 NTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQA-------QSDLNRRVPLGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 159 DGSLSIRE----RDAalasaaqgsadIDQAKAALEMSRQDL---QTVIVNRgALEAD--VENAKAALELAQIDLQNTRIV 229
Cdd:PRK15136 152 ANLIGREElqhaRDA-----------VASAQAQLDVAIQQYnanQAMILNT-PLEDQpaVQQAATEVRNAWLALQRTKIV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 230 APRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALN-NKAYQGRVESISPATGVE 307
Cdd:PRK15136 220 SPMTGYVSRRSVQVGAQISPTTPLMAVVPATNlWVDANFKETQLANMRIGQPATITSDIYGdDVVYTGKVVGLDMGTGSA 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 556299675 308 FSAITPDNATGNFVKIAQRIPVRIEVLGKPEDAALLRPGMSVQVTIDTR 356
Cdd:PRK15136 300 FSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTA 348
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
60-360 |
1.72e-46 |
|
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: 160.88 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 60 QTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAmkiaalnnnlqqrksaeatiakndaalkNA 139
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLA----------------------------AA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 140 RAQSLKSQADLKRVKELTADGSLSirerdaalasaaqgSADIDQAKAALEmsrqdlqtvivnrgALEADVENAKAALELA 219
Cdd:COG0845 74 QAQLELAKAELERYKALLKKGAVS--------------QQELDQAKAALD--------------QAQAALAAAQAALEQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 220 QIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRVE 298
Cdd:COG0845 126 RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPlEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVT 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556299675 299 SISPatgvefsaiTPDNATGNFvkiaqriPVRIEVlgkPEDAALLRPGMSVQVTIDTREAKQ 360
Cdd:COG0845 206 FIDP---------AVDPATRTV-------RVRAEL---PNPDGLLRPGMFVRVRIVLGEREN 248
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
25-358 |
4.26e-42 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 149.79 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 25 AAAIGIVGVLVILYA-WQlppfTRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQ 103
Cdd:PRK10476 15 ALAIVALAIVALVFViWR----TDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 104 AEAQLAMKIAALNNnlQQR----KSAEATIAKndAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAalASAAQGSA 179
Cdd:PRK10476 91 AQADLALADAQIMT--TQRsvdaERSNAASAN--EQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQ--ARTAQRDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 180 DIDqAKAALEMSRQDLQTViVNRGALEADVENAKAALELAQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPP 259
Cdd:PRK10476 165 EVS-LNQALLQAQAAAAAV-GGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 260 QHW-VIANIKETQLAELRVGQPVKFTVDALNNKAYQGRVESISpatgvefSAITPDNATG------------NFVKIAQR 326
Cdd:PRK10476 243 DHWyAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIG-------WGVLPDDGGNvprglpyvprsiNWVRVAQR 315
|
330 340 350
....*....|....*....|....*....|..
gi 556299675 327 IPVRIEvLGKPeDAALLRPGMSVQVTIDTREA 358
Cdd:PRK10476 316 FPVRIM-LDKP-DPELFRIGASAVVELRPGAA 345
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
44-355 |
7.68e-33 |
|
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: 124.84 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 44 PFTRHAQFTDNAYVRGQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRK 123
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 124 SAEATIAKND-----------------AALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQGSADIDQAKA 186
Cdd:pfam00529 83 RLQALESELAisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 187 ALEMSRQD--------LQTVIVNRGALEADVENAKAALELAQIDLQNTRIVAPRDGQLGQIAVRL-GAYVTAGTHLTTLV 257
Cdd:pfam00529 163 QLDQIYVQitqsaaenQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 258 PPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKA---YQGRVESISPATGvefsaitpdnatgnfvkiaqriPVRIEV 333
Cdd:pfam00529 243 PEDNlLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTG----------------------PVRVVV 300
|
330 340
....*....|....*....|..
gi 556299675 334 LGKPEDAALLRPGMSVQVTIDT 355
Cdd:pfam00529 301 DKAQGPYYPLRIGLSAGALVRL 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
59-357 |
2.57e-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: 117.80 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 59 GQTTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMkiaalnnnlqqrksaeatiakndaalkn 138
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAA---------------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 139 ARAQSLKSQADLKRVKELTADGSLSirerdaalasaaqgSADIDQAKAALEmsrqdlqtvivnrgALEADVENAKAALEL 218
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVS--------------QADLDDAKAAVE--------------AAQADLEAAKASLAS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 219 AQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRV 297
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPlEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 298 ESISPAtgvefsaitPDNATGNFvkiaqriPVRIEVlgkPEDAALLRPGMSVQVTIDTRE 357
Cdd:TIGR01730 208 RFIDPR---------VDSGTGTV-------RVRATF---PNPDGRLLPGMFGRVTISLKV 248
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
68-358 |
9.33e-25 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 102.73 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 68 VNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAMKIAALNnnLQQRKSAEATIAKNDAALKNARAQSLKSQ 147
Cdd:PRK03598 50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLD--LMLAGYRDEEIAQARAAVKQAQAAYDYAQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 148 ADLKRVKELTADGSLSIRERDAALASAAQGSADIDQAKAAL----EMSR-QDLqtvivnrGALEADVENAKAALELAQID 222
Cdd:PRK03598 128 NFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLsqyrEGNRpQDI-------AQAKASLAQAQAALAQAELN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 223 LQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRVESIS 301
Cdd:PRK03598 201 LQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPvWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVS 280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 302 PATgvEF---SAITPDNATgnfvKIAQRIpvRIeVLGKPEDAalLRPGMSVQVTIDTREA 358
Cdd:PRK03598 281 PTA--EFtpkTVETPDLRT----DLVYRL--RI-VVTDADDA--LRQGMPVTVRFADEAG 329
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
27-339 |
1.75e-24 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 101.74 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 27 AIGIVGVLVILYAWQL---PPFTRHAQFTDNAYVrgqttfISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQ 103
Cdd:PRK10559 16 VLVILAFIAIFRAWVFyteSPWTRDARFSADVVA------IAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 104 AEAQLAMKIAalnnnLQQRKSAEATiakndaalknaraqslksqadlkrvkeltadgslsireRDAALASAAQGSADIDQ 183
Cdd:PRK10559 90 AEADVAYYQV-----LAQEKRREAG--------------------------------------RRNRLGVQAMSREEIDQ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 184 AKAALEMSRQDLQtvivnrgaleadveNAKAALELAQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVpPQH-- 261
Cdd:PRK10559 127 ANNVLQTVLHQLA--------------KAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALV-KQNsf 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 262 WVIANIKETQLAELRVGQPVKFTVDAlNNKAYQGRVESIspATGVEFSAITPDN---ATGN----FVKIAQRIPVRIEVL 334
Cdd:PRK10559 192 YVLAYMEETKLEGVRPGYRAEITPLG-SNKVLKGTVDSV--AAGVTNSSSTRDSkgmATIDsnleWVRLAQRVPVRIRLD 268
|
....*
gi 556299675 335 GKPED 339
Cdd:PRK10559 269 NQQGN 273
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
86-357 |
7.63e-16 |
|
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: 78.13 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 86 GDLLLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQ----QRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGS 161
Cdd:TIGR01843 113 PDDLLSAEDPAVPELIKGQQSLFESRKSTLRAQLElilaQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 162 LS-------IRERDAALASAAQGSADIDQAKAALEMSRQDLQTVI------VNRGALEADVENAKAALELAQIDLQNTR- 227
Cdd:TIGR01843 193 VSrlellelERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEqtfreeVLEELTEAQARLAELRERLNKARDRLQRl 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 228 -IVAPRDGQLGQIAVR-LGAYVTAGTHLTTLVP--PQHWVIANIKETQLAELRVGQPVKFTVDALNNKAY---QGRVESI 300
Cdd:TIGR01843 273 iIRSPVDGTVQSLKVHtVGGVVQPGETLMEIVPedDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYgilNGKVKSI 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 556299675 301 SPatgvefSAITPDNATGNFVKIaqRIPVRIEVLGKPEDAALLRPGMSVQVTIDTRE 357
Cdd:TIGR01843 353 SP------DTFTDERGGGPYYRV--RISIDQNTLGIGPKGLELSPGMPVTADIKTGE 401
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
201-349 |
3.55e-14 |
|
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: 70.61 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 201 NRGALEADVENAKAALEL-----AQID-LQNTR-------IVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIAN 266
Cdd:pfam16576 71 DALSKSELLRAARQRLRLlgmpeAQIAeLERTGkvqptvtVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTvWVEAD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 267 IKETQLAELRVGQPVKFTVDALNNKAYQGRVESISPatgvefsAITPDNATgnfvkiaqrIPVRIEVlgkPEDAALLRPG 346
Cdd:pfam16576 151 VPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYP-------TLDPKTRT---------VRVRIEL---PNPDGRLKPG 211
|
...
gi 556299675 347 MSV 349
Cdd:pfam16576 212 MFA 214
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
67-360 |
3.01e-12 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 67.11 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 67 QVNGYITEVKVQDFVQVKKGDLLLQIDDRiyrqrvhQAEAQLamkiaalnnnlqqrKSAEATIAKNDAALKNARAQSLKS 146
Cdd:PRK11578 67 QVSGQLKTLSVAIGDKVKKDQLLGVIDPE-------QAENQI--------------KEVEATLMELRAQRQQAEAELKLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 147 QADLKRVKELTADGSLSIRerdaalasaaqgsaDIDQAKAALEMSRQDLQTvivnrgaLEADVENAKAALELAQIDLQNT 226
Cdd:PRK11578 126 RVTLSRQQRLAKTQAVSQQ--------------DLDTAATELAVKQAQIGT-------IDAQIKRNQASLDTAKTNLDYT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 227 RIVAPRDGQLGQIAVRLGAYVTAG----THLTTLVPPQHWVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRVESISP 302
Cdd:PRK11578 185 RIVAPMAGEVTQITTLQGQTVIAAqqapNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILP 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 556299675 303 atgvefsaiTPDNatgnfVKIAQRIPVRIEVlgkPEDAALLRPGMSVQVTIDTREAKQ 360
Cdd:PRK11578 265 ---------TPEK-----VNDAIFYYARFEV---PNPNGLLRLDMTAQVHIQLTDVKN 305
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
227-346 |
2.69e-11 |
|
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: 59.68 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 227 RIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQH-WVIANIKETQLAELRVGQPVKFTVDALNNKAYQGRVESISPatg 305
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRlLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISP--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 556299675 306 vefsaiTPDNATGNFvkiaqriPVRIEVLGkPEDAALLRPG 346
Cdd:pfam13437 78 ------TVDPDTGVI-------PVRVSIEN-PKTPIPLLPG 104
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
61-260 |
7.90e-10 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 59.80 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 61 TTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLamkiaalnnnlqqrksaeatiAKNDAALKNAR 140
Cdd:PRK11556 87 TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQL---------------------AKDQATLANAR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 141 aqslksqADLKRVKELTADGSLSIRERDA--ALASAAQGSADIDQakaalemsrqdlqtvivnrgaleadvenakAALEL 218
Cdd:PRK11556 146 -------RDLARYQQLAKTNLVSRQELDAqqALVSETEGTIKADE------------------------------ASVAS 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556299675 219 AQIDLQNTRIVAPRDGQLGQIAVRLGAYVTAGTHLTTLVPPQ 260
Cdd:PRK11556 189 AQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQ 230
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
61-109 |
1.37e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 47.44 E-value: 1.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 556299675 61 TTFISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLA 109
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
64-319 |
5.59e-07 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 50.87 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 64 ISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRIYRQRVHQAEAQLAmkiaalnnnlqqRKSAEATIAkndaalknaraqs 143
Cdd:PRK15030 68 VRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLA------------KAQAAANIA------------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 144 lksQADLKRVKELTADGSLSIRERDAALASAAQGSADidqakaalemsrqdlqtvivnrgaleadVENAKAALELAQIDL 223
Cdd:PRK15030 123 ---QLTVNRYQKLLGTQYISKQEYDQALADAQQANAA----------------------------VTAAKAAVETARINL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 224 QNTRIVAPRDGQLGQIAVRLGAYVTAGtHLTTLVPPQHWVIANIKETQLAE--LRVGQPV-KFTVDALNNKAYQGRVESI 300
Cdd:PRK15030 172 AYTKVTSPISGRIGKSNVTEGALVQNG-QATALATVQQLDPIYVDVTQSSNdfLRLKQELaNGTLKQENGKAKVSLITSD 250
|
250 260
....*....|....*....|...
gi 556299675 301 S---PATG-VEFSAITPDNATGN 319
Cdd:PRK15030 251 GikfPQDGtLEFSDVTVDQTTGS 273
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
64-249 |
1.84e-05 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 46.25 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 64 ISPQVNGYITEVKVQDFVQVKKGDLLLQIDDriyrqrvhqaeaqlAMKIAALNnnlqqrkSAEATIAKNDAALKNARAqS 143
Cdd:PRK09859 64 IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDP--------------APLQAELN-------SAKGSLAKALSTASNARI-T 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 144 LKSQADLKRVKELtadgslsirerdaalasaaqgsadidqakaalemSRQDLQTVIVNRGALEADVENAKAALELAQIDL 223
Cdd:PRK09859 122 FNRQASLLKTNYV----------------------------------SRQDYDTARTQLNEAEANVTVAKAAVEQATINL 167
|
170 180
....*....|....*....|....*.
gi 556299675 224 QNTRIVAPRDGQLGQIAVRLGAYVTA 249
Cdd:PRK09859 168 QYANVTSPITGVSGKSSVTVGALVTA 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
82-225 |
2.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 82 QVKKGDLLLQIDDRIYRQRVH----QAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNARAQSLKSQA------DLK 151
Cdd:COG4913 582 QVKGNGTRHEKDDRRRIRSRYvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswDEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 152 RVKELTADgslsIRERDAALASAAQGSAD-------IDQAKAALEMSRQDLQTVIVNRGALEADVENAKAALELAQIDLQ 224
Cdd:COG4913 662 DVASAERE----IAELEAELERLDASSDDlaaleeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
.
gi 556299675 225 N 225
Cdd:COG4913 738 A 738
|
|
| NHLM_micro_HlyD |
TIGR03794 |
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the ... |
19-355 |
9.85e-05 |
|
NHLM bacteriocin system secretion protein; Members of this protein family are homologs of the HlyD membrane fusion protein of type I secretion systems. Their occurrence in prokaryotic genomes is associated with the occurrence of a novel class of microcin (small bacteriocins) with a leader peptide region related to nitrile hydratase. We designate the class of bacteriocin as Nitrile Hydratase Leader Microcin, or NHLM. This family, therefore, is designated as NHLM bacteriocin system secretion protein. Some but not all NHLM-class putative microcins belong to the TOMM (thiazole/oxazole modified microcin) class as assessed by the presence of the scaffolding protein and/or cyclodehydratase in the same gene clusters. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274787 [Multi-domain] Cd Length: 421 Bit Score: 44.06 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 19 IVSVFTAAAIGIVGVLVILYAwqlppftrhaqftDNAYVRGQTTF--ISPQVNGYITEVKVQDFVQVKKGDLLLQIDDRI 96
Cdd:TIGR03794 27 GVIVVAALAWGIFGSIPITVS-------------GNGILILSSGVdtIQSPGSGVVIDLDVEVGDQVKKGQVVARLFQPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 97 YRQRVHQAEAQLAMkiaalnnnLQQRKSAeatIAKNDAALKNARAQSLKSQadlkrvKELTADGSLSIRERDAALasaaq 176
Cdd:TIGR03794 94 LRERLQESYQKLTQ--------LQEQLEE---VRNYTGRLKEGRERHFQKS------KEALEETIGRLREELAAL----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 177 gSADIDQAKAALemSRQDLQTVIVNRGALEADVENAK--AALELAQIDLQNTR--------IVAPRDGQLGQIAVRLGAY 246
Cdd:TIGR03794 152 -SREVGKQRGLL--SRGLATFKRDRILQQQWREEQAKydAADKARAIYALQTKadernletVLQSLSQADFQLAGVAQQE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 247 VTAgthlttlvppqhwVIANIKET--QLAELRVgqpvKFTVDALNNKAYQGRVESISPATGVEFSAITP------DNATG 318
Cdd:TIGR03794 229 LET-------------VEARIKEAryEIEELEN----KLNLNTRIVSQHSGRVIELNYTPGQLVAAGAPlaslevEDQTD 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 556299675 319 NFVKIAQRIPvrievlgkPEDAALLRPGMSVQVTIDT 355
Cdd:TIGR03794 292 EGLEGVAYFP--------VAEGKKIRPGMSVQITPST 320
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-230 |
5.54e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 91 QIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAA 170
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 171 LASAAQGSADIDQAKAALEMSRQDLQTVIVNRGALEADVENAKAALELAQIDLQNTRIVA 230
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
68-256 |
7.79e-04 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 40.93 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 68 VNGYITEVKVQDFVQVKKGDLLLQIDdriyrqrvhqaeaqlamkiaalnnnlqqrkSAEATIAKNDA--ALKNARAQSLK 145
Cdd:PRK09578 70 VAGIVTARTYEEGQEVKQGAVLFRID------------------------------PAPLKAARDAAagALAKAEAAHLA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 146 SQADLKRVKELTADGSLSIRERDAALASAAQGsadidqakaalemsrqdlqtvivnrgalEADVENAKAALELAQIDLQN 225
Cdd:PRK09578 120 ALDKRRRYDDLVRDRAVSERDYTEAVADERQA----------------------------KAAVASAKAELARAQLQLDY 171
|
170 180 190
....*....|....*....|....*....|...
gi 556299675 226 TRIVAPRDGQLGQIAVRLGAYV--TAGTHLTTL 256
Cdd:PRK09578 172 ATVTAPIDGRARRALVTEGALVgqDQATPLTTV 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-228 |
9.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 98 RQRVHQAEAQLAMKIAALNnnlQQRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQG 177
Cdd:COG1196 311 RRELEERLEELEEELAELE---EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 556299675 178 SADIDQAKAALEMSRQDLQTVIVNRGALEADVENAKAALELAQIDLQNTRI 228
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-227 |
1.39e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 98 RQRVHQAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNARAQSLKSQADLKRVKELTADGSLSIRERDAALASAAQG 177
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 556299675 178 SADIDQAKAALEMSRQDLQTVIVNRGALEADVENAKAALELAQIDLQNTR 227
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-220 |
1.52e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556299675 89 LLQIDDRIYRQRVHQAEAQLAMKIAALNNNLQQRKSAEATIAKNDAALKNARAQSLKSQADL----KRVKELTADGSLSI 164
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLE 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556299675 165 RERDAALASAAQGSADIDQAKAALEMSRQDLQTVIVNRGALEADVENAKAALELAQ 220
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
|
| |
