|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
36-373 |
1.47e-82 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 254.97 E-value: 1.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 36 KRSTLLWMLGVLIIGILVILWAWRIGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:COG1566 2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQkQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1566 82 QAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 196 LAALKQAEANVLVAKEALKT-AQVAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYL 274
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREeEELAAA--QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 275 IP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAGSEFSvlkPDNATGNftkVVQRIAVRITIDP 353
Cdd:COG1566 239 VPlDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSP---PKNATGN---VVQRYPVRIRLDN 312
|
330 340
....*....|....*....|
gi 447201370 354 NQEgmEHLRPGMSVITSVDT 373
Cdd:COG1566 313 PDP--EPLRPGMSATVEIDT 330
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
36-375 |
2.52e-49 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 170.65 E-value: 2.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 36 KRSTLLWMLGVLIIGILVILWaWRIgpFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:PRK15136 21 KRALLLLTLLFIIIGVAYGIY-WFL--VLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQkvaqaasGVEQAKNTLANQTQSIAQKQADIVAAQAKVEqVRaQYELSLAQ--LRRYQQLGNSGAASKsEQDKAAADAe 193
Cdd:PRK15136 98 EQ-------AFEKAKTALANSVRQTHQLMINSKQYQANIE-LQ-KTALAQAQsdLNRRVPLGNANLIGR-EELQHARDA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 194 nnlAALKQAEANVLVAKEALKTAQVAEAGLEAQ--VSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQL 271
Cdd:PRK15136 167 ---VASAQAQLDVAIQQYNANQAMILNTPLEDQpaVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 272 LYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM-KHKKFTGHVEQISPAAGSEFSVLKPDNATGNFTKVVQRIAVRI 349
Cdd:PRK15136 244 MAVVPaTNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRI 323
|
330 340
....*....|....*....|....*.
gi 447201370 350 TIDPNQEGMEHLRPGMSVITSVDTSS 375
Cdd:PRK15136 324 ELDAKQLAQHPLRIGLSTLVTVDTAN 349
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
78-375 |
1.84e-43 |
|
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: 153.18 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 78 KTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYdqkvaqaasgveqakntlanqtqsiaqkQADIVAAQAKVEQV 157
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDL----------------------------QAALAQAQAQLAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 158 RAQYELSLAQLRRYQQLGNSGAASKSEqdkaaadaennlaaLKQAEANVLVAkealktaqvaeaglEAQVSSAKAQLDQA 237
Cdd:COG0845 74 QAQLELAKAELERYKALLKKGAVSQQE--------------LDQAKAALDQA--------------QAALAAAQAALEQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 238 QTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLI-PQQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVE 316
Cdd:COG0845 126 RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIAdLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447201370 317 QISPAAgsefsvlkpDNATGNFTkvvqriaVRITIdPNQEGMehLRPGMSVITSVDTSS 375
Cdd:COG0845 206 FIDPAV---------DPATRTVR-------VRAEL-PNPDGL--LRPGMFVRVRIVLGE 245
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
34-358 |
6.21e-38 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 139.39 E-value: 6.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 34 PTKRSTLLWMLGVLIIGILVILwAWRIGPFATsvqqTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDAT 113
Cdd:PRK10476 8 SPRKKLPALAIVALAIVALVFV-IWRTDSAPS----TDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 114 TYDQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAA--- 190
Cdd:PRK10476 83 PYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTaqr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 191 DAENNL-AALKQAEANVlvakealkTAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGS 269
Cdd:PRK10476 163 DAEVSLnQALLQAQAAA--------AAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 270 QLLYLIPQQTW-VIANFKETQIANMRIGQKAwfTVDAM--KHKKFTGHVEQISPAAGSEFSVLKPDN-----ATGNFTKV 341
Cdd:PRK10476 235 PIFTLIDTDHWyAIANFRETDLKNIRVGDCA--TVYSMidRGRPFEGKVDSIGWGVLPDDGGNVPRGlpyvpRSINWVRV 312
|
330
....*....|....*...
gi 447201370 342 VQRIAVRITID-PNQEGM 358
Cdd:PRK10476 313 AQRFPVRIMLDkPDPELF 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
60-366 |
6.46e-35 |
|
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: 130.62 E-value: 6.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 60 IGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQA----------------- 122
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAeaqlakaqaqvarlqae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 123 ASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS---EQDKAAADAENNLAAL 199
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISREslvTAGALVAQAQANLLAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 200 KQAEANVLVAKEALKTAQVAEA-----GLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRV-GQYVAAGSQLLY 273
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVrselsGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 274 LIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM---KHKKFTGHVEQISPAAGSefsvlkpdnatgnftkvvqriaVRI 349
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFpqtKTGRFTGVVVGISPDTGP----------------------VRV 298
|
330
....*....|....*..
gi 447201370 350 TIDPNQEGMEHLRPGMS 366
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLS 315
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
36-374 |
2.66e-24 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 101.96 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 36 KRSTLLWMLGVLIIGILVILWAWRIgpfatsvQQTDNSY-----VKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHI 110
Cdd:PRK03598 2 KKKVVIGLAVVVLAAAVAGGWWWYQ-------SRQDNGLtlygnVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 111 DATTYDQKVAQAASGVEQAKNTLA-----NQTQSIAQkqadivaAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASkseq 185
Cdd:PRK03598 75 DAAPYENALMQAKANVSVAQAQLDlmlagYRDEEIAQ-------ARAAVKQAQAAYDYAQNFYNRQQGLWKSRTIS---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 186 dkaAADAENNLAALKQAEANVLVAKEALKTAQ-------VAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVN 258
Cdd:PRK03598 144 ---ANDLENARSSRDQAQATLKSAQDKLSQYRegnrpqdIAQA--KASLAQAQAALAQAELNLQDTELIAPSDGTILTRA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 259 PRVGQYVAAGSQLLYL-IPQQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAgsEF---SVLKPDNA 334
Cdd:PRK03598 219 VEPGTMLNAGSTVFTLsLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTA--EFtpkTVETPDLR 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 447201370 335 tgnfTKVVQRIavRITIDPNQEGmehLRPGMSVITSVDTS 374
Cdd:PRK03598 297 ----TDLVYRL--RIVVTDADDA---LRQGMPVTVRFADE 327
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
77-367 |
3.51e-24 |
|
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: 101.24 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 77 GKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYdqkvaqaasgveqakntlanqtqsiaqkQADIVAAQAKVEQ 156
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY----------------------------QLALQAALAQLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 157 VRAQYELSLAQLRRYQQLGNSGAASKSEQDKaaadaennlaalkqaeanvlvakealktAQVAEAGLEAQVSSAKAQLDQ 236
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVSQADLDD----------------------------AKAAVEAAQADLEAAKASLAS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 237 AQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHV 315
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDlDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447201370 316 EQISPAAgsefsvlkpDNATGNFtkvvqriAVRITIDPNQEGmehLRPGMSV 367
Cdd:TIGR01730 208 RFIDPRV---------DSGTGTV-------RVRATFPNPDGR---LLPGMFG 240
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
36-320 |
2.09e-21 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 94.07 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 36 KRSTLLWMLGVLIIGILVILWAWRIGPFAT----SVQQTD---NSYVKGKTTIL-----SSQINGYVKDVLVKDFDHVKK 103
Cdd:PRK11578 6 KVKKRYLIALVIVLAGGITLWRILNAPVPTyqtlIVRPGDlqqSVLATGKLDALrkvdvGAQVSGQLKTLSVAIGDKVKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 104 GQVLMHIDAttydqkvaqaasgvEQAKNtlanqtqSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS 183
Cdd:PRK11578 86 DQLLGVIDP--------------EQAEN-------QIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 184 EQDKAAADAennlaalkqaeanvlvakeALKTAQVAEagLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQ 263
Cdd:PRK11578 145 DLDTAATEL-------------------AVKQAQIGT--IDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQ 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447201370 264 YVAAGSQ---LLYLIPQQTW-VIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISP 320
Cdd:PRK11578 204 TVIAAQQapnILTLADMSTMlVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILP 264
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
78-367 |
2.93e-15 |
|
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: 74.08 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 78 KTTILSSQINGYVKDVLVKDF-DHVKKGQVLMHIDATtydqkvaqaasgveqakntlanqtqsiaqkqaDIVAAQAkveq 156
Cdd:pfam16576 18 RLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSP--------------------------------ELVAAQQ---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 157 vraqyELSLAQlrryqqlgNSGAASKSEQDKAAAdaennlaalkqaeanvlvaKEALKTAQVAEAGLeaqvssakAQLDQ 236
Cdd:pfam16576 62 -----EYLLAL--------RSGDALSKSELLRAA-------------------RQRLRLLGMPEAQI--------AELER 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 237 AQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGsQLLYLIPQ--QTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGH 314
Cdd:pfam16576 102 TGKVQPTVTVYAPISGVVTELNVREGMYVQPG-DTLFTIADlsTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGK 180
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447201370 315 VEQISPaagsefsVLKPDNATgnftkvvqrIAVRITIdPNQEGMehLRPGMSV 367
Cdd:pfam16576 181 VDYIYP-------TLDPKTRT---------VRVRIEL-PNPDGR--LKPGMFA 214
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
31-373 |
4.20e-13 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 69.38 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 31 KLIPTKRSTLLWMLGVLIIGILVILWAWrigPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHI 110
Cdd:PRK10559 2 KTLIRKISRTAITLVLVILAFIAIFRAW---VFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 111 DATTYDQKVAQAasgveqakntlanqtqsiaqkQADIVAAQAKVEQVRAQYElslaqlrRYQQLGNSgAASKSEQDKAaa 190
Cdd:PRK10559 79 DQPRYQKALAEA---------------------EADVAYYQVLAQEKRREAG-------RRNRLGVQ-AMSREEIDQA-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 191 daeNNlaalkqaeanvlvakeALKTAqvaeaglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQ 270
Cdd:PRK10559 128 ---NN----------------VLQTV-------LHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGST 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 271 LLYLIPQQT-WVIANFKETQIANMRIGQKAWFTvDAMKHKKFTGHVEQIspAAGSEFSVLKPDN---ATGN----FTKVV 342
Cdd:PRK10559 182 AVALVKQNSfYVLAYMEETKLEGVRPGYRAEIT-PLGSNKVLKGTVDSV--AAGVTNSSSTRDSkgmATIDsnleWVRLA 258
|
330 340 350
....*....|....*....|....*....|.
gi 447201370 343 QRIAVRITIDPNQegmEHLRPGMSVITSVDT 373
Cdd:PRK10559 259 QRVPVRIRLDNQQ---GNLYPAGTTATVVIT 286
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
46-375 |
6.08e-13 |
|
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: 69.65 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 46 VLIIGILVILWAWRI-GPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATT---------- 114
Cdd:TIGR01843 9 WLIAGLVVIFFLWAYfAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDveadaaeles 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 115 -----------------------------------YDQKVAQAASGVEQAKNTLANQTQSI----AQKQADIVAAQAKVE 155
Cdd:TIGR01843 89 qvlrleaevarlraeadsqaaiefpddllsaedpaVPELIKGQQSLFESRKSTLRAQLELIlaqiKQLEAELAGLQAQLQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 156 QVRAQYELSLAQLRRYQQLGNSGAASKS---EQDKAAADAENNLAALKqAEANVLVAK--------------------EA 212
Cdd:TIGR01843 169 ALRQQLEVISEELEARRKLKEKGLVSRLellELERERAEAQGELGRLE-AELEVLKRQidelqlerqqieqtfreevlEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 213 LKTAQVAEAGLEAQVSSAKAQLDQaqttkdySVIVAPMDGQLGEV-NPRVGQYVAAGSQLLYLIP--QQTWVIANFKETQ 289
Cdd:TIGR01843 248 LTEAQARLAELRERLNKARDRLQR-------LIIRSPVDGTVQSLkVHTVGGVVQPGETLMEIVPedDPLEIEAKLSPKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 290 IANMRIGQKAWFTVDAMKHKKF---TGHVEQISPAAGSEfsvlkpDNATGNFTKVvqriavRITIDPNQEGME----HLR 362
Cdd:TIGR01843 321 IGFVHVGQPAEIKFSAFPYRRYgilNGKVKSISPDTFTD------ERGGGPYYRV------RISIDQNTLGIGpkglELS 388
|
410
....*....|...
gi 447201370 363 PGMSVITSVDTSS 375
Cdd:TIGR01843 389 PGMPVTADIKTGE 401
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
245-364 |
8.70e-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: 58.53 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 245 VIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQT-WVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPaag 323
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRlLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISP--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 447201370 324 sefsvlKPDNATGNFTkvvqriaVRITIDPNQEGmEHLRPG 364
Cdd:pfam13437 78 ------TVDPDTGVIP-------VRVSIENPKTP-IPLLPG 104
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
64-299 |
2.79e-09 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 58.26 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 64 ATSVQQTDNSYVKGKTTI-------LSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQAASGVEQAKNTLANQ 136
Cdd:PRK11556 65 ATATEQAVPRYLTGLGTVtaantvtVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 137 TQSIAqkqadivaaqakveqvraqyelslaqlrRYQQLGNSGAASKSEQDkaaadaeNNLAALKQAEANVLVAkealkta 216
Cdd:PRK11556 145 RRDLA----------------------------RYQQLAKTNLVSRQELD-------AQQALVSETEGTIKAD------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 217 qvaeaglEAQVSSAKAQLDqaqttkdYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQTW---VIANFKETQIANM 293
Cdd:PRK11556 183 -------EASVASAQLQLD-------YSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHpidLVFTLPESDIATV 248
|
....*.
gi 447201370 294 RIGQKA 299
Cdd:PRK11556 249 VQAQKA 254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-242 |
1.54e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyeLSLAQLRRyQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--IARLEERR-RELEERLEELEEELAELEEELEEL 335
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447201370 196 LAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
119-215 |
2.63e-06 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 48.88 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 119 VAQAASGVEQAKNTLANQTQSIAQ--KQA--DIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAEN 194
Cdd:COG1538 53 IEAAKAQAEAAEADLRAARLDLAAevAQAyfDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQ 132
|
90 100
....*....|....*....|.
gi 447201370 195 NLAALKQAEANVLVAKEALKT 215
Cdd:COG1538 133 ARAQLAQAEAQLAQARNALAL 153
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
116-233 |
8.40e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIvAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAELAKKKAEE-RREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE 300
|
90 100 110
....*....|....*....|....*....|....*...
gi 447201370 196 LAaLKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQ 233
Cdd:COG2268 301 RE-EAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
133-242 |
1.54e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 133 LANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS-----------EQDKAAADAENN-LAALK 200
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaelEAELERLDASSDdLAALE 691
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 447201370 201 Q----AEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG4913 692 EqleeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
79-122 |
2.08e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 41.27 E-value: 2.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 447201370 79 TTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQA 122
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQA 45
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
187-252 |
2.26e-05 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 45.94 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 187 KAAADAENnlAALKQAEANVLVAKEALK-----------------TAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVAP 249
Cdd:PRK09578 100 KAARDAAA--GALAKAEAAHLAALDKRRryddlvrdravserdytEAVADERQAKAAVASAKAELARAQLQLDYATVTAP 177
|
...
gi 447201370 250 MDG 252
Cdd:PRK09578 178 IDG 180
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
111-235 |
3.07e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 45.49 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 111 DATTYDQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyelsLAQLrryqqlgnsgaaskseQDKAAA 190
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKE----LANA----------------QAQALQ 314
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 447201370 191 DAENNLAALKQAEANvlvAKEALKTAQVAEAGLEAQVSSAKAQLD 235
Cdd:TIGR04320 315 TAQNNLATAQAALAN---AEARLAKAKEALANLNADLAKKQAALD 356
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
152-339 |
3.21e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 45.48 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 152 AKVEQVRAQYELSLAQL--RRYQQLGNSGAASKSEQDKAAADAEnnlaalkQAEANVLVAKEALKTAQVAEAgleaqvss 229
Cdd:PRK15030 108 AKGDLAKAQAAANIAQLtvNRYQKLLGTQYISKQEYDQALADAQ-------QANAAVTAAKAAVETARINLA-------- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 230 akaqldqaqttkdYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQTWVIAnFKETQIANMRIGQKAWFTVDAMKHK 309
Cdd:PRK15030 173 -------------YTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIY-VDVTQSSNDFLRLKQELANGTLKQE 238
|
170 180 190
....*....|....*....|....*....|....*..
gi 447201370 310 KFTGHVEQIS------PAAGS-EFSVLKPDNATGNFT 339
Cdd:PRK15030 239 NGKAKVSLITsdgikfPQDGTlEFSDVTVDQTTGSIT 275
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
129-242 |
8.61e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.95 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 129 AKNTLANQTQSIAQKQADIVAAQAKVEQvrAQYELSLAQlrryQQLGNSGAASKSEQdKAAADAENNLA-----ALKQAE 203
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAA--AQTALNTAQ----AALTSAQTAYAAAQ-AALATAQKELAnaqaqALQTAQ 317
|
90 100 110
....*....|....*....|....*....|....*....
gi 447201370 204 ANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:TIGR04320 318 NNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
112-274 |
5.33e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.78 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 112 ATTYDQKVAQAASGVEQAKNTLAnqtqSIAQKQADIVAAQAKVEQVRAQYElslAQLRRYQQlgnSGAASKSEQDKAAAD 191
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAAA----AAAREAAPLKASLRKLERAKARAD---AELKRADK---ALAAAKTDEAKARAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 192 AENNLAALKQAEANvlvakEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVApMDGQLGeVNPrVGQYVAAGSQL 271
Cdd:PRK12472 262 ERQQKAAQQAAEAA-----TQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAA-TDAKLA-LEP-VSIYISRATQK 333
|
...
gi 447201370 272 LYL 274
Cdd:PRK12472 334 LYV 336
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-254 |
8.48e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyeLSLAQ-LRRYQQLGNSGAASKSEQDKAAADAEN 194
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--LGNVRnNKEYEALQKEIESLKRRISDLEDEILE 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447201370 195 NLAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQ--AQTTKDYSVIVAPMDGQL 254
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAelEELEAEREELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-241 |
2.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYElslAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG4942 61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 447201370 196 LAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTK 241
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-242 |
2.48e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 117 QKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRaqyelslAQLRRYQQLGNSGAASKsEQDKAAADAENNL 196
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQLGNVRNNK-EYEALQKEIESLK 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 447201370 197 AALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
145-242 |
2.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 145 ADIVAAQAKVEQVRAQYELsLAQLRRYQQlgnsgAASKSEQDKAAADAENNLAALKQAEANVLVAKEALKTAQVAEAGLE 224
Cdd:COG4913 235 DDLERAHEALEDAREQIEL-LEPIRELAE-----RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90
....*....|....*...
gi 447201370 225 AQVSSAKAQLDQAQTTKD 242
Cdd:COG4913 309 AELERLEARLDALREELD 326
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
121-238 |
4.33e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 121 QAASGVEQAKNTLANQTQSIAQ----KQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENNL 196
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADllslERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 447201370 197 AALKQAEANVLvAKEALKTAQVAEagLEAQVSSAKAQLDQAQ 238
Cdd:PRK09039 126 DSEKQVSARAL-AQVELLNQQIAA--LRRQLAALEAALDASE 164
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
126-238 |
6.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 126 VEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLgnsgaASKSEQDKAAADAENNLAALKQAEAN 205
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110
....*....|....*....|....*....|...
gi 447201370 206 VLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQ 238
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELL 183
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
140-236 |
7.01e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 36.52 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 140 IAQKQADIVAAQAKVEQVRAQYELSLAQLRRyqqlgnsgaasKSEQDKAAADAE-NNLAALKQAEANvlvaKEALKTAQV 218
Cdd:PRK07353 41 IRTNRAEAKERLAEAEKLEAQYEQQLASARK-----------QAQAVIAEAEAEaDKLAAEALAEAQ----AEAQASKEK 105
|
90
....*....|....*...
gi 447201370 219 AEAGLEAQVSSAKAQLDQ 236
Cdd:PRK07353 106 ARREIEQQKQAALAQLEQ 123
|
|
|