|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-531 |
0e+00 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 722.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 2 SNWIKPYIEQNKGRMTVTIFLGLLGVSSGAMLLFISGYLISKSALRPEnVMAVYVPIVATRAFSIGQAVFHYVERLVGHD 81
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPP-VLYLSVAAVAVRAFGIGRAVFRYLERLVGHD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 82 VVLRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIA 161
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 162 ACMLATIVFLLPFISLLLMKKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHI 241
Cdd:TIGR02868 160 AAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 242 RDSIIQLVVGIVVVSMiIWTGNEA-ASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVEGNGVLQD 320
Cdd:TIGR02868 240 GAALTLLAAGLAVLGA-LWAGGPAvADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 EKELPRDKDYVaPKHIDIELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS 400
Cdd:TIGR02868 319 EGSAPAAGAVG-LGKPTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 401 EHAHT---NLLSKYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGE 477
Cdd:TIGR02868 397 VPVSSldqDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 478 RQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHL 531
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-570 |
0e+00 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 660.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 4 WIKPYIEQNKGRMTVTIFLGLLGVSSGAMLLFISGYLISKSALRPEnVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVV 83
Cdd:COG4987 5 RLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPP-ILNLFVPIVGVRAFAIGRTVFRYLERLVSHDAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 84 LRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAAC 163
Cdd:COG4987 84 LRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 164 MLATIVFLLPFISLLLMKKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRD 243
Cdd:COG4987 164 GLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 244 SIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVEGngvlQDEKE 323
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLD----APPAV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 324 LPRDKDYVAPKHIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHA 403
Cdd:COG4987 320 TEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 404 HT---NLLSKYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQR 480
Cdd:COG4987 400 RDldeDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
570
....*....|
gi 2662793383 561 NEKYRKLYEL 570
Cdd:COG4987 560 NGRYRQLYQR 569
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-570 |
4.67e-125 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 379.51 E-value: 4.67e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 4 WIKPYIEQNKGRMTVTIFLGLLGVSSGAMLLFISGYLISkSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVV 83
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIID-ALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 84 LRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLY---LRTIFPSILALVVYSIFVLVIgtfDVVFALI 160
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLahgLPQLVRSVVTLIGALVVLFVI---DWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 161 AACMLATIVFLLPFISLLLMKKHHVTLKQgRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNH 240
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEA-LAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 241 IRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNqvegnGVLQD 320
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF-----ELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 EKELPRDKDYVAPKHI--DIELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL 398
Cdd:COG1132 321 PPEIPDPPGAVPLPPVrgEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 399 N----SEHAHTNLLSKyISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFS 474
Cdd:COG1132 400 DgvdiRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 475 GGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSH 554
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....*.
gi 2662793383 555 EQLLKENEKYRKLYEL 570
Cdd:COG1132 559 EELLARGGLYARLYRL 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-569 |
1.34e-109 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 339.49 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 5 IKPYI---EQNKGRMTVTIFLGLLGVSSGAMLLFISGYLISKSALRPENVMAVY---VPIVATRAFSIGQAVFHYVERLV 78
Cdd:PRK11160 4 LLPFLklyKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFnymLPAAGVRGAAIGRTAGRYGERLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 79 GHDVVLRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVysIFVLVIGT--FDVV 156
Cdd:PRK11160 84 SHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVV--ILVLTIGLsfFDLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 157 FALIAACMLATIVFLLPFISLLLMKKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMK 236
Cdd:PRK11160 162 LALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 237 RWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVegng 316
Cdd:PRK11160 242 NLTGLSQALMILANGLTVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEI---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 317 VLQD-EKELPRDKDyVAPKHIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE 395
Cdd:PRK11160 318 TEQKpEVTFPTTST-AAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 396 VLLN-------SEHAhtnlLSKYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATlPDGLQTKMHE 468
Cdd:PRK11160 397 ILLNgqpiadySEAA----LRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 469 MGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKI 548
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
570 580
....*....|....*....|.
gi 2662793383 549 VMQGSHEQLLKENEKYRKLYE 569
Cdd:PRK11160 552 IEQGTHQELLAQQGRYYQLKQ 572
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
104-569 |
1.86e-99 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 317.16 E-value: 1.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 104 FFRSRfQTGDMLGVLSeDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAacMLATIVFLLpfISLLLMKKH 183
Cdd:COG2274 246 FFESR-SVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV--LLLIPLYVL--LGLLFQPRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 184 HVTLKQGRNRLYQQ---LTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIW 260
Cdd:COG2274 320 RRLSREESEASAKRqslLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 261 TGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVegngvLQDEKELPRDKDYVAPKHI--DI 338
Cdd:COG2274 400 GAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDI-----LDLPPEREEGRSKLSLPRLkgDI 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNLLSKYISVL 415
Cdd:COG2274 475 ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlRQIDPASLRRQIGVV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIV 495
Cdd:COG2274 555 LQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 496 LDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYE 569
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
338-552 |
1.96e-92 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 281.12 E-value: 1.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT--NLLSKYISVL 415
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDleKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDTTIGNNVrigkpeatdeeiwkalekaqlashiatlpdglqtkmhemGKRFSGGERQRVAFARTLMQEAPIIV 495
Cdd:cd03247 81 NQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 496 LDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQG 552
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-561 |
6.93e-88 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 282.42 E-value: 6.93e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 1 MSNWIKPYIEQNKGRMTVTIFLGLLgvsSGAMLLFISGYL---ISKSALRPENVMAVYVPIVATRAFSIGQAVFHYVERL 77
Cdd:COG4988 4 LDKRLKRLARGARRWLALAVLLGLL---SGLLIIAQAWLLaslLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 78 VGHDVVLRILEKMRTKLYgivepQALF-----FRSRFQTGDMLGVLSEDIEHLQNlYLRTIFP-SILALVVYSIFVLVIG 151
Cdd:COG4988 81 AAFRAAARVKRRLRRRLL-----EKLLalgpaWLRGKSTGELATLLTEGVEALDG-YFARYLPqLFLAALVPLLILVAVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 152 TFDVVFALIaacMLATiVFLLP-FISLL------LMKKHHVTLkqgrNRLYQQLTDAVFGLSDWQASGRKDEFIDKyVEQ 224
Cdd:COG4988 155 PLDWLSGLI---LLVT-APLIPlFMILVgkgaakASRRQWRAL----ARLSGHFLDRLRGLTTLKLFGRAKAEAER-IAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 225 NAQLL--KTEKRMKrwnhirdsiIQLVVGIV-----VVSMIIwtgneaaseqIAptVIAAFVLM--TLSVTNAL------ 289
Cdd:COG4988 226 ASEDFrkRTMKVLR---------VAFLSSAVleffaSLSIAL----------VA--VYIGFRLLggSLTLFAALfvllla 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 290 ----IPLSD-------------AIDRIPSYVESahrlnqvEGNGVLQDEKELPrdkdyvAPKHIDIELNHVSYSYPhSNE 352
Cdd:COG4988 285 peffLPLRDlgsfyharangiaAAEKIFALLDA-------PEPAAPAGTAPLP------AAGPPSIELEDVSFSYP-GGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 353 FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsEHAHTNL----LSKYISVLNQKPHLFDTTIGN 428
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLdpasWRRQIAWVPQNPYLFAGTIRE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 NVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTE 508
Cdd:COG4988 430 NLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 509 LSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
338-569 |
9.87e-68 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 219.41 E-value: 9.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYpHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISV 414
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtlDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYE 569
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
338-568 |
2.67e-63 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 207.47 E-value: 2.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISV 414
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLY 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-568 |
1.36e-61 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 213.04 E-value: 1.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 7 PYIEQNKGRMTVTIFLGLLGVSSGAMLLFISGYLISK-SALRPENVmAVYVP-----IVATRAfsIGQAVFHYVERLVGH 80
Cdd:TIGR02203 7 SYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDgFGGRDRSV-LWWVPlvvigLAVLRG--ICSFVSTYLLSWVSN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 81 DVVLRILEKMRTKLYGIvePQALFfrSRFQTGDMLGVLSEDIEHlqnlylrtifpsILALVVYSIFVLVIGTFDVVFALI 160
Cdd:TIGR02203 84 KVVRDIRVRMFEKLLGL--PVSFF--DRQPTGTLLSRITFDSEQ------------VASAATDAFIVLVRETLTVIGLFI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 161 AacMLAT-------IVFLLPFISLLL---------MKKHHVTLKQGRNRLYQQLTDA--VFGLSDWQASGRKdefidKYV 222
Cdd:TIGR02203 148 V--LLYYswqltliVVVMLPVLSILMrrvskrlrrISKEIQNSMGQVTTVAEETLQGyrVVKLFGGQAYETR-----RFD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 223 EQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSY 302
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 303 VESAHRLNqvegnGVLQDEKELprDKDYVAPKHI--DIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKST 380
Cdd:TIGR02203 301 LAAAESLF-----TLLDSPPEK--DTGTRAIERArgDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKST 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 381 LLKLLTGALSPLHGEVLLNS-EHAHTNL--LSKYISVLNQKPHLFDTTIGNNVRIGKP-EATDEEIWKALEKAQLASHIA 456
Cdd:TIGR02203 374 LVNLIPRFYEPDSGQILLDGhDLADYTLasLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 457 TLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEH 536
Cdd:TIGR02203 454 KLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK 533
|
570 580 590
....*....|....*....|....*....|..
gi 2662793383 537 VDEVIFLDRGKIVMQGSHEQLLKENEKYRKLY 568
Cdd:TIGR02203 534 ADRIVVMDDGRIVERGTHNELLARNGLYAQLH 565
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
337-561 |
3.74e-61 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 201.69 E-value: 3.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYIS 413
Cdd:cd03254 2 EIEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
338-570 |
4.84e-61 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 202.00 E-value: 4.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYIS 413
Cdd:cd03249 1 IEFKNVSFRYPSRPDVpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYEL 570
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-543 |
1.07e-60 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 209.84 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 20 IFLGLLGVSSGAMLL---FISGYLISKSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYG 96
Cdd:TIGR02857 6 ALLALLGVLGALLIIaqaWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 97 IVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAACMLATIVFllpFIS 176
Cdd:TIGR02857 86 AVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPI---FMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 177 LLLMKKHHVTLKQGR--NRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLV--VGI 252
Cdd:TIGR02857 163 LIGWAAQAAARKQWAalSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFatLSV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 253 VVVSMIIwtGNEAASEQIaPTVIAAFVLmtLSVTNALIPLSD--AidripSYVESAHRLNQVEGNGVLQDEKELPR--DK 328
Cdd:TIGR02857 243 ALVAVYI--GFRLLAGDL-DLATGLFVL--LLAPEFYLPLRQlgA-----QYHARADGVAAAEALFAVLDAAPRPLagKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 329 DYVAPKHIDIELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHT 405
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVplaDADA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 406 NLLSKYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFAR 485
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFL 543
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
338-547 |
6.80e-59 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 193.75 E-value: 6.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAH---TNLLSKYISV 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVrigkpeatdeeiwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGK 547
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
337-552 |
1.09e-57 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 192.42 E-value: 1.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL---NSEHAHTNLLSKYIS 413
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQG 552
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
338-570 |
2.87e-57 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 202.36 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYpHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAhtnlLSK 410
Cdd:COG5265 358 VRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgqdirdvTQAS----LRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 YISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQE 490
Cdd:COG5265 433 AIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 491 APIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYEL 570
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
104-568 |
2.46e-55 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 198.81 E-value: 2.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 104 FFRSRfQTGDMLGVLSED---IEHLQNLYLrTIFPSILALVVYSIFVLVIGT--FDVVFALIAACMLATIVFLLPFisll 178
Cdd:TIGR01193 246 FFSTR-RTGEIVSRFTDAssiIDALASTIL-SLFLDMWILVIVGLFLVRQNMllFLLSLLSIPVYAVIIILFKRTF---- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 179 lmKKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSI---IQLVVGIVvv 255
Cdd:TIGR01193 320 --NKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIkavTKLILNVV-- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 256 smIIWTGneaaseqiaptviaAFVLMTLSVT-------NALI-----PLSDAIDRIPSYVESA---HRLNQVEgngVLQD 320
Cdd:TIGR01193 396 --ILWTG--------------AYLVMRGKLTlgqlitfNALLsyfltPLENIINLQPKLQAARvanNRLNEVY---LVDS 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 EKELPRDKDYVAPKHIDIELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNs 400
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN- 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 401 ehaHTNL-------LSKYISVLNQKPHLFDTTIGNNVRIG-KPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKR 472
Cdd:TIGR01193 535 ---GFSLkdidrhtLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 473 FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATeEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQG 552
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
490
....*....|....*.
gi 2662793383 553 SHEQLLKENEKYRKLY 568
Cdd:TIGR01193 691 SHDELLDRNGFYASLI 706
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-567 |
1.02e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 186.71 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHSNEFVlKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYIS 413
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtrASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKL 567
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-553 |
2.46e-51 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 175.37 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKYIS 413
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdisKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFDTTIGNNVRIGKpEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGS 553
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
23-310 |
3.63e-51 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 177.29 E-value: 3.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 23 GLLGVSSGAMLLFISGYLISKSALRP--ENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYGIVEP 100
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGlaAPTFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 101 QALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAACMLATIVFLLPFISLLLM 180
Cdd:cd18585 81 LAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 181 KKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIW 260
Cdd:cd18585 161 KKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 261 TGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAidriPSYVE----SAHRLN 310
Cdd:cd18585 241 GAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLA----FQYLGetraAARRLF 290
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
316-570 |
2.17e-49 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 180.21 E-value: 2.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 316 GVLQDEKELPRDKDYVAPKHIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE 395
Cdd:PRK11176 320 AILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 396 VLLNS----EHAHTNLlSKYISVLNQKPHLFDTTIGNNVRIGKPEA-TDEEIWKALEKAQLASHIATLPDGLQTKMHEMG 470
Cdd:PRK11176 400 ILLDGhdlrDYTLASL-RNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 471 KRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVM 550
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
250 260
....*....|....*....|
gi 2662793383 551 QGSHEQLLKENEKYRKLYEL 570
Cdd:PRK11176 559 RGTHAELLAQNGVYAQLHKM 578
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
304-568 |
1.49e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 175.03 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 304 ESAHRLNQVEGNGVLQDEKELPRDKDyvapkhIDIELNHVSYsYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLK 383
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGEKELASNDP------VTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 384 LLTGALsPLHGEVLLNS-EHAHTNLLS--KYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPD 460
Cdd:PRK11174 395 ALLGFL-PYQGSLKINGiELRELDPESwrKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 461 GLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEV 540
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260
....*....|....*....|....*...
gi 2662793383 541 IFLDRGKIVMQGSHEQLLKENEKYRKLY 568
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
338-570 |
1.62e-47 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 166.12 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH---AHTNLLSKYISV 414
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYEL 570
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
92-567 |
2.14e-46 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 172.00 E-value: 2.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 92 TKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYL---RTIFPSILALvvysiFVLVIGTFDVVFALIAACMLATI 168
Cdd:TIGR01192 93 TEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLefmRQHLATFVAL-----FLLIPTAFAMDWRLSIVLMVLGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 169 VFLlpFISLLLM---KKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRW------- 238
Cdd:TIGR01192 168 LYI--LIAKLVMqrtKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWwalasgl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 239 NHIRdSIIQLVVGIVVVSMIIWTGNEAASEQIAptviaaFVlmtlSVTNALIPLSDAIDRIPSYVESAHRlnQVEGNGVL 318
Cdd:TIGR01192 246 NRMA-STISMMCILVIGTVLVIKGELSVGEVIA------FI----GFANLLIGRLDQMSGFITQIFEARA--KLEDFFDL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 319 QD---EKELPRDKDYVAPKHIDIELNHVSYSYPHSNEFVlKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE 395
Cdd:TIGR01192 313 EDsvfQREEPADAPELPNVKGAVEFRHITFEFANSSQGV-FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 396 VLLNSEHAHT---NLLSKYISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKR 472
Cdd:TIGR01192 392 ILIDGIDINTvtrESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 473 FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQG 552
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
490
....*....|....*
gi 2662793383 553 SHEQLLKENEKYRKL 567
Cdd:TIGR01192 552 SFQELIQKDGRFYKL 566
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
338-563 |
7.80e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 160.96 E-value: 7.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKYISV 414
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPH--LFDTTIGNNV-----RIGKPEAT-DEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFART 486
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVafgpeNLGLPREEiRERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHL--VgIEHVDEVIFLDRGKIVMQGSHEQLLKENEK 563
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLdlV-AELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
145-560 |
8.82e-46 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 169.54 E-value: 8.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 145 IFVLVIGTFDVVFALIAACmLATIVFLLPFISLLLMKKHHVTLKQGRNRLYQQLT------DAVfglsdwQASGRKDEFI 218
Cdd:COG4618 145 IFLAVLFLFHPLLGLLALV-GALVLVALALLNERLTRKPLKEANEAAIRANAFAEaalrnaEVI------EAMGMLPALR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 219 DKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAP-TVIAAFVLMTLsvtnALIPLSDAID 297
Cdd:COG4618 218 RRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPgAMIAASILMGR----ALAPIEQAIG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 298 RIPSYV---ESAHRLNQVEGNGVLQDEK-ELPRdkdyvaPKHiDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGR 373
Cdd:COG4618 294 GWKQFVsarQAYRRLNELLAAVPAEPERmPLPR------PKG-RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 374 SGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISVLNQKPHLFDTTIGNNvrIGK-PEATDEEIWKAlekA 449
Cdd:COG4618 367 SGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdrEELGRHIGYLPQDVELFDGTIAEN--IARfGDADPEKVVAA---A 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 450 QLAS-H--IATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK-TVI 525
Cdd:COG4618 442 KLAGvHemILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGaTVV 521
|
410 420 430
....*....|....*....|....*....|....*
gi 2662793383 526 WITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-548 |
1.84e-44 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 157.25 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 331 VAPKHID--IELNHVSYSYP-HSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHA 403
Cdd:cd03248 3 LAPDHLKgiVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpiSQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 404 HTNLLSKyISVLNQKPHLFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAF 483
Cdd:cd03248 83 HKYLHSK-VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKI 548
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
338-571 |
4.08e-44 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 157.13 E-value: 4.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAH---TNLLSKYISV 414
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHL-FDTTIGNNVRIG---------KPEATDEEI-WKALEKAQLAsHIATLPdglqtkMHEMgkrfSGGERQRVAF 483
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAvEEALERTGLE-HLADRP------VDEL----SGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
250
....*....|.
gi 2662793383 561 nEKYRKLYELD 571
Cdd:COG1120 229 -ELLEEVYGVE 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
337-570 |
4.74e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 165.28 E-value: 4.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYpHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHAHTnLLSKYI 412
Cdd:PRK10790 340 RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplSSLSHS-VLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLFDTTIGNNVRIGKpEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAP 492
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYEL 570
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQL 574
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
339-547 |
2.79e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.78 E-value: 2.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKYISVL 415
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPH--LFDTTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFARTL 487
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGI-EHVDEVIFLDRGK 547
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
338-548 |
9.39e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 149.56 E-value: 9.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNE--FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLL 408
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDT-TIGNNVRI-----GKPEATDEE-IWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRV 481
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRErAEELLERVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHVDEVIFLDRGKI 548
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
338-560 |
1.53e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.83 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYISVL 415
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT-TIGNNVRI-----GKPEATDEE-IWKALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfarlyGLPRKEARErIDELLELF-----------GLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
338-547 |
3.57e-41 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 147.62 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYP---HSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhtnllskYISv 414
Cdd:cd03250 1 ISVEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA-------YVS- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 lnQKPHLFDTTIGNNVRIGKPEatDEE-IWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:cd03250 73 --QEPWIQNGTIRENILFGKPF--DEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHHLVGIEHVDEVIFLDRGK 547
Cdd:cd03250 149 YLLDDPLSAVDAHVGRHIFENCILglLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
277-567 |
3.78e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 158.35 E-value: 3.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 277 AFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVegngvLQDEKELPRDKDYvAPKHID--IELNHVSYSYP-HSNEF 353
Cdd:TIGR00958 422 SFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY-----LDRKPNIPLTGTL-APLNLEglIEFQDVSFSYPnRPDVP 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHAHTNLLSKYISVlNQKPHLFDTTIGNN 429
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgvplVQYDHHYLHRQVALV-GQEPVLFSGSVREN 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTEL 509
Cdd:TIGR00958 575 IAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 510 SLIETMFSAteEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKL 567
Cdd:TIGR00958 655 LLQESRSRA--SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
339-552 |
1.24e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 145.27 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehahtnllskyisvlnqk 418
Cdd:cd03214 1 EVENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 phlfdttignnvriGKPEATdeeiwkaLEKAQLASHIATLPDGL-QTKMHEMGKRF----SGGERQRVAFARTLMQEAPI 493
Cdd:cd03214 60 --------------GKDLAS-------LSPKELARKIAYVPQALeLLGLAHLADRPfnelSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETM--FSATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQG 552
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
338-560 |
4.49e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.16 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYISVL 415
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT-TIGNNVRIGKP--EATDEEIWKALEKaqlASHIATLPDGLQTKMHEmgkrFSGGERQRVAFARTLMQEAP 492
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREE 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
344-568 |
1.44e-39 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 152.17 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 344 SYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKY---ISVLNQKPH 420
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWrsrLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 421 LFDTTIGNNVRIGKPEATDEEIWKAlekAQLAS-H--IATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLD 497
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHV---ARLASvHddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 498 EPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLY 568
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY 547
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
338-559 |
3.55e-39 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 143.41 E-value: 3.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTN------LLSKY 411
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFDT-TIGNNV------RIGKPEATDEEIwkALEKAQLAshiatlpdGLQTKMHEMGKRFSGGERQRVAFA 484
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplreHTRLSEEEIREI--VLEKLEAV--------GLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHL---VGIehVDEVIFLDRGKIVMQGSHEQLLK 559
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLdtaFAI--ADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
338-567 |
5.31e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.72 E-value: 5.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHAHTNLLSKYIS 413
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKP--HLFDTTIGNNVRIGkPE---ATDEEIWK----ALEKAQLASHIATLPdglqtkmhemgKRFSGGERQRVAFA 484
Cdd:TIGR04520 81 MVFQNPdnQFVGATVEDDVAFG-LEnlgVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
....*
gi 2662793383 563 KYRKL 567
Cdd:TIGR04520 229 LLKEI 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
338-548 |
6.01e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.88 E-value: 6.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-----HAHTnlLSKYI 412
Cdd:COG4619 1 LELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsamPPPE--WRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLFDTTIGNNV----RIGKPEATDEEIWKALEKAQLASHIatlpdgLQTKMHEMgkrfSGGERQRVAFARTLM 488
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDI------LDKPVERL----SGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTElSLIETMFS---ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKI 548
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENT-RRVEELLReylAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
338-549 |
1.04e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNE--FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLL 408
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDT-TIGNNVRI-----GKPEATDEE-IWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRV 481
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRErARELLERVGLGDRLDHRPSQL-----------SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHVDEVIFLDRGKIV 549
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-568 |
1.07e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNllSKYISVLNQ 417
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--RRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KpHLFDTTI----------GNNVRIG---KPEATD-EEIWKALEKAQLAS----HIATLpdglqtkmhemgkrfSGGERQ 479
Cdd:COG1121 83 R-AEVDWDFpitvrdvvlmGRYGRRGlfrRPSRADrEAVDEALERVGLEDladrPIGEL---------------SGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTE---LSLIETMfsATEEKTVIWITHHLVGI-EHVDEVIFLDRGkIVMQGSHE 555
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEealYELLREL--RREGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGPPE 223
|
250
....*....|...
gi 2662793383 556 QLLKEnEKYRKLY 568
Cdd:COG1121 224 EVLTP-ENLSRAY 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
338-561 |
2.74e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHsnefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-HAHTNLLSKYISVLN 416
Cdd:COG3840 2 LRLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTALPPAERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QK----PHLfdtTIGNNVRIG-----KPEATD-EEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFART 486
Cdd:COG3840 78 QEnnlfPHL---TVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 487 LMQEAPIIVLDEPTIGLDP--KTE-LSLIETMfsATEEK-TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalRQEmLDLVDEL--CRERGlTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
339-552 |
4.41e-38 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 139.59 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHtnLLSKYISVLNQK 418
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 pHLFDTTIGNNVR-------------IGKPEATD-EEIWKALEKAQLA----SHIATLpdglqtkmhemgkrfSGGERQR 480
Cdd:cd03235 77 -RSIDRDFPISVRdvvlmglyghkglFRRLSKADkAKVDEALERVGLSeladRQIGEL---------------SGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTE---LSLIETMfsATEEKTVIWITH--HLVgIEHVDEVIFLDRgKIVMQG 552
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQediYELLREL--RREGMTILVVTHdlGLV-LEYFDRVLLLNR-TVVASG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
94-560 |
2.78e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 148.17 E-value: 2.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 94 LYGIVE-PQALFFRSrfQTGDMLGVLSEDIEHLQnlylrTIFPSILALVVYSIFVlVIGTfdVVFALIAACMLATIVFLL 172
Cdd:TIGR00957 1045 LHNKLRsPMSFFERT--PSGNLVNRFSKELDTVD-----SMIPPVIKMFMGSLFN-VIGA--LIVILLATPIAAVIIPPL 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 173 PFISLLLMKKHHVTLKQ-------GRNRLYQQLTDAVFGLSDWQASGRKDEFI---DKYVEQNAQLLKTEKRMKRWNHIR 242
Cdd:TIGR00957 1115 GLLYFFVQRFYVASSRQlkrlesvSRSPVYSHFNETLLGVSVIRAFEEQERFIhqsDLKVDENQKAYYPSIVANRWLAVR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 243 dsiIQLVVGIVVVSMIIWTGNEAASeqIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRLNQVEgngvlQDEK 322
Cdd:TIGR00957 1195 ---LECVGNCIVLFAALFAVISRHS--LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYS-----ETEK 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 323 ELPRDKDYVAPKHI-----DIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVL 397
Cdd:TIGR00957 1265 EAPWQIQETAPPSGwpprgRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 398 LN----SEHAHTNLLSKyISVLNQKPHLFDTTIGNNVrigKP--EATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGK 471
Cdd:TIGR00957 1345 IDglniAKIGLHDLRFK-ITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 472 RFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQ 551
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
....*....
gi 2662793383 552 GSHEQLLKE 560
Cdd:TIGR00957 1501 GAPSNLLQQ 1509
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
274-560 |
5.12e-37 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 144.41 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 274 VIAAFVLMTlsvtNALIPLSDAIDRIPSYVESA---HRLNQVEGNGVLQDEK-ELPRDKdyvapKHIDIElnHVSYSYPH 349
Cdd:TIGR01842 260 MIAGSILVG----RALAPIDGAIGGWKQFSGARqayKRLNELLANYPSRDPAmPLPEPE-----GHLSVE--NVTIVPPG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 350 SNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNLLSKYISVLNQKPHLFDTTI 426
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlKQWDRETFGKHIGYLPQDVELFPGTV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 427 GNNV-RIGKpEATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP 505
Cdd:TIGR01842 409 AENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 506 KTELSLIETMFSATEEK-TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:TIGR01842 488 EGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
338-559 |
3.36e-36 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 135.11 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphsNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLLS 409
Cdd:COG1127 6 IEVRNLTKSF---GDRvVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqditglSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 KyISVLNQKPHLFDT-TIGNNV------RIGKPEATDEEIwkALEKAQ---LASHIATLPDGLqtkmhemgkrfSGGERQ 479
Cdd:COG1127 83 R-IGMLFQGGALFDSlTVFENVafplreHTDLSEAEIREL--VLEKLElvgLPGAADKMPSEL-----------SGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQ 556
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEE 228
|
...
gi 2662793383 557 LLK 559
Cdd:COG1127 229 LLA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
355-500 |
3.70e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTN---LLSKYISVLNQKPHLF-DTTIGNNV 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerkSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 431 RIG------KPEATDEEIWKALEKAQlashiatLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLG-------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
338-557 |
1.59e-35 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 133.07 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphsNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG-----ALSPLHGEVLLNSEhahtNLLSKY 411
Cdd:cd03260 1 IELRDLNVYY---GDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK----DIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLN---------QKPHLFDTTIGNNVRIGKP-------EATDEEIWKALEKAQLashiatlPDGLQTKMHemGKRFSG 475
Cdd:cd03260 74 VDVLElrrrvgmvfQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAAL-------WDEVKDRLH--ALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSH 554
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPT 224
|
...
gi 2662793383 555 EQL 557
Cdd:cd03260 225 EQI 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-552 |
2.71e-35 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 131.85 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefvlKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS-EHAHTNLLSKYISVLN 416
Cdd:cd03298 1 VRLDKIRFSYGEQP----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKPHLF-DTTIGNNVRIGKPEATdeeiwKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIV 495
Cdd:cd03298 77 QENNLFaHLTVEQNVGLGLSPGL-----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 496 LDEPTIGLDP--KTELSLIETMFSATEEKTVIWITHHLVGIEHVDE-VIFLDRGKIVMQG 552
Cdd:cd03298 152 LDEPFAALDPalRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
338-568 |
3.19e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE------HAHTNLLSKY 411
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFD-TTIGNNVRIG----KPeatdeeIWKAL-------EKAQLASHIATLpdGLQTKMHEMGKRFSGGERQ 479
Cdd:COG3638 82 IGMIFQQFNLVPrLSVLTNVLAGrlgrTS------TWRSLlglfppeDRERALEALERV--GLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIwITHHLVGI--EHVDEVIFLDRGKIVMQGSHE 555
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVV-VNLHQVDLarRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|...
gi 2662793383 556 QLlkENEKYRKLY 568
Cdd:COG3638 233 EL--TDAVLREIY 243
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
338-567 |
3.75e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 133.35 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT------NLL 408
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKP--HLFDTTIGNNV-----RIGKPEAtdeeiwKALEKAQLASHIATLPDGLQTKM-HEMgkrfSGGERQR 480
Cdd:TIGR04521 81 RKKVGLVFQFPehQLFEETVYKDIafgpkNLGLSEE------EAEERVKEALELVGLDEEYLERSpFEL----SGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTE---LSLIETMFSaTEEKTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQ 556
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRkeiLDLFKRLHK-EKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDGTPRE 229
|
250
....*....|.
gi 2662793383 557 LLKENEKYRKL 567
Cdd:TIGR04521 230 VFSDVDELEKI 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
338-545 |
5.07e-35 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 131.44 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF--VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTnlLSKYISVL 415
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG--PGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFD-TTIGNNVRIG-------KPEAtDEEIWKALEKAQLASHIATLPdglqtkmHEMgkrfSGGERQRVAFARTL 487
Cdd:cd03293 79 FQQDALLPwLTVLDNVALGlelqgvpKAEA-RERAEELLELVGLSGFENAYP-------HQL----SGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHhlvgieHVDEVIFL-DR 545
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH------DIDEAVFLaDR 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-558 |
5.33e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.11 E-value: 5.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSP---LHGEVLLNSE---HAHTNLLSKY 411
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRdllELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKP--HLFDTTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPdglqtkmHEmgkrFSGGERQRVAF 483
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYP-------HQ----LSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
338-568 |
1.12e-34 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 131.15 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsEHAHTNL-------LSK 410
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID-GTDINKLkgkalrqLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 YISVLNQKPHLFD-TTIGNNVRIGK--------------PEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSG 475
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQL-----------SG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIwITHHLVGI--EHVDEVIFLDRGKIVMQ 551
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVI-VSLHQVDLarEYADRIVGLKDGRIVFD 226
|
250
....*....|....*..
gi 2662793383 552 GSHEQLlkENEKYRKLY 568
Cdd:cd03256 227 GPPAEL--TDEVLDEIY 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-569 |
1.26e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 131.08 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNE--FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKY---I 412
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKP-------HLFDTTIGNNVRIGKPEATDEEIWKALEKAQLAshiatlPDGLQTKMHEMgkrfSGGERQRVAFAR 485
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLP------PSFLDRYPHQL----SGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTE---LSLIETMfSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLK-- 559
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQaeiLNLLKDL-REERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAgp 230
|
250
....*....|
gi 2662793383 560 ENEKYRKLYE 569
Cdd:COG1124 231 KHPYTRELLA 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
338-548 |
1.26e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 128.67 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSneFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYISVL 415
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT-TIGNNVRigkpeatdeeiwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKI 548
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
338-550 |
1.81e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 130.98 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNE--FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTnlLSKYISVL 415
Cdd:COG1116 8 LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--PGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFD-TTIGNNVRIG-------KPEAtDEEIWKALEKAQLASHIATLPdglqtkmHEMgkrfSGGERQRVAFARTL 487
Cdd:COG1116 86 FQEPALLPwLTVLDNVALGlelrgvpKAER-RERARELLELVGLAGFEDAYP-------HQL----SGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHhlvgieHVDEVIFL-DRgkIVM 550
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH------DVDEAVFLaDR--VVV 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-558 |
2.24e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.57 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYP--HSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE------HAHTNLL 408
Cdd:COG1123 261 LEVRNLSKRYPvrGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKP-HLFDT--TIGNNV-------RIGKPEATDEEIWKALEKAQL-ASHIATLPdglqtkmHEmgkrFSGGE 477
Cdd:COG1123 341 RRRVQMVFQDPySSLNPrmTVGDIIaeplrlhGLLSRAERRERVAELLERVGLpPDLADRYP-------HE----LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 478 RQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSH 554
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPT 489
|
....
gi 2662793383 555 EQLL 558
Cdd:COG1123 490 EEVF 493
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
338-552 |
7.05e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 128.39 E-value: 7.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV--LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTN------LLS 409
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 KYISVLNQKPHL-FDT--TIGNNV----RIGKPEATDEEIWKALekAQLASHIATLPDGLQTKMHEmgkrFSGGERQRVA 482
Cdd:cd03257 82 KEIQMVFQDPMSsLNPrmTIGEQIaeplRIHGKLSKKEARKEAV--LLLLVGVGLPEEVLNRYPHE----LSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 483 FARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
339-547 |
1.25e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.43 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSneFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnsehahtnllskyisvlnqk 418
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILI-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 phlfdttignnvrigkpeatDEEIWKALEKAQLASHIATLPDglqtkmhemgkrFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:cd00267 59 --------------------DGKDIAKLPLEELRRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 499 PTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGK 547
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
338-566 |
2.68e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-----LLNSEhaHTNLLSKYI 412
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgiTISKE--NLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKP--HLFDTTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFA 484
Cdd:PRK13632 86 GIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
....
gi 2662793383 563 KYRK 566
Cdd:PRK13632 235 ILEK 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
338-548 |
8.00e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 123.87 E-value: 8.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISV 414
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwdpNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVrigkpeatdeeiwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEAPII 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 495 VLDEPTIGLDPKTE---LSLIETMFSATeeKTVIWITHHLVGIEHVDEVIFLDRGKI 548
Cdd:cd03246 119 VLDEPNSHLDVEGEralNQAIAALKAAG--ATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-549 |
8.80e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.68 E-value: 8.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNeFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYISVLNQK 418
Cdd:cd03226 1 RIENISFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 P--HLFDTTIGNNVRIGKPEATD-----EEIWKALEKAQLAS-HIATLpdglqtkmhemgkrfSGGERQRVAFARTLMQE 490
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDAgneqaETVLKDLDLYALKErHPLSL---------------SGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 491 APIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIV 549
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVcDRVLLLANGAIV 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
338-540 |
2.32e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.66 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYISVL 415
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT-TIGNNV----RIGKPEATDEEIWKALEKAQLASHiatlpdglqtkMHEMGKRFSGGERQRVAFARTLMQE 490
Cdd:COG4133 81 GHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVGLAGL-----------ADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 491 APIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEV 540
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
338-549 |
5.97e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.16 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT------NLLSKY 411
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrreiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHL-FDTTIGNNVR-----IGKPEAT-DEEIWKALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFA 484
Cdd:COG2884 81 IGVVFQDFRLlPDRTVYENVAlplrvTGKSRKEiRRRVREVLDLV-----------GLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDE-VIFLDRGKIV 549
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKrVLELEDGRLV 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-560 |
8.31e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 120.65 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNLLSKYISV 414
Cdd:PRK13548 3 LEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrplADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHL-FDTTIGNNVRIG------KPEATDEEIWKALEKAQLAsHIATlpdglqtkmhemgkRF----SGGERQRVAF 483
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGraphglSRAEDDALVAAALAQVDLA-HLAG--------------RDypqlSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQ------EAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSH 554
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLnLAARYADRIVLLHQGRLVADGTP 225
|
....*.
gi 2662793383 555 EQLLKE 560
Cdd:PRK13548 226 AEVLTP 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
338-547 |
2.36e-30 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 116.90 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSneFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-----SEHAHTNLLSKYI 412
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLFDT-TIGNNVRIGkpeatdeeiwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEA 491
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHHLVGIEHV-DEVIFLDRGK 547
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
338-548 |
2.82e-30 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 118.02 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVL-----LNSEHAHTNLLSKYI 412
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLF-DTTIGNNVRI------GKPEATDEEI-WKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFA 484
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLapikvkGMSKAEAEERaLELLEKVGLADKADAYPAQL-----------SGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK-TVIWITHHLVGIEHV-DEVIFLDRGKI 548
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
338-552 |
2.95e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 118.01 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-HAHTNLLSKYISVLN 416
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKPHLFDT-TIGNNVRIG---KPEATDEEIWKALEKAQLAShiatLPDGLQTKMHEMgkrfSGGERQRVAFARTLMQEAP 492
Cdd:cd03259 79 QDYALFPHlTVAENIAFGlklRGVPKAEIRARVRELLELVG----LEGLLNRYPHEL----SGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 493 IIVLDEPTIGLDPKTELSL---IETMFSATeEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03259 151 LLLLDEPLSALDAKLREELreeLKELQREL-GITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-558 |
3.32e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 126.63 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 24 LLGVSSGAMLLFISGYLISKSaLRPENVMAVY-------VPIVATRAFSIGQAVFHYVERLvgHDVVLRilekmrtklyG 96
Cdd:PLN03232 926 VLRVSSSTWLSIWTDQSTPKS-YSPGFYIVVYallgfgqVAVTFTNSFWLISSSLHAAKRL--HDAMLN----------S 992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 97 IVEPQALFFRSRfQTGDMLGVLSEDI-------EHLQNLYLRtifpsiLALVVYSIFVLvIGTFDVVFalIAACMLATIV 169
Cdd:PLN03232 993 ILRAPMLFFHTN-PTGRVINRFSKDIgdidrnvANLMNMFMN------QLWQLLSTFAL-IGTVSTIS--LWAIMPLLIL 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 170 FLLPFI-----SLLLMKKHHVTlkqgRNRLYQQLTDAVFGLSD---WQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHI 241
Cdd:PLN03232 1063 FYAAYLyyqstSREVRRLDSVT----RSPIYAQFGEALNGLSSiraYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTI 1138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 242 R-DSIIQLVVGIVVVSMIIWTGNeaASEQIaptVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAhrLNQVEGNGVLQD 320
Cdd:PLN03232 1139 RlETLGGVMIWLTATFAVLRNGN--AENQA---GFASTMGLLLSYTLNITTLLSGVLRQASKAENS--LNSVERVGNYID 1211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 ekeLPRDKDYVapkhidIELNHVSYSYPHSNEFVLKDVSLQIKAG---------------KKIAILGRSGTGKSTLLKLL 385
Cdd:PLN03232 1212 ---LPSEATAI------IENNRPVSGWPSRGSIKFEDVHLRYRPGlppvlhglsffvspsEKVGVVGRTGAGKSSMLNAL 1282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 386 TGALSPLHGEVLLN----SEHAHTNLlSKYISVLNQKPHLFDTTIGNNVrigKP--EATDEEIWKALEKAQLASHIATLP 459
Cdd:PLN03232 1283 FRIVELEKGRIMIDdcdvAKFGLTDL-RRVLSIIPQSPVLFSGTVRFNI---DPfsEHNDADLWEALERAHIKDVIDRNP 1358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 460 DGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDE 539
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDK 1438
|
570
....*....|....*....
gi 2662793383 540 VIFLDRGKIVMQGSHEQLL 558
Cdd:PLN03232 1439 ILVLSSGQVLEYDSPQELL 1457
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-553 |
3.96e-30 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 117.51 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 333 PKHIDIELNHVSYSY-PHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL-NSEHAHTNL--L 408
Cdd:cd03369 2 PEHGEIEVENLSVRYaPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIdGIDISTIPLedL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDTTIGNNVRIgKPEATDEEIWKALekaqlashiatlpdglqtKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGS 553
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-549 |
5.34e-30 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 124.14 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 11 QNKGRMTVTIFLGLLGVSSGAMLLfisgYLISKSALRPENVMAVYVPI--------VATRAFSigQAVFHYVerlvGHDV 82
Cdd:COG4615 10 ESRWLLLLALLLGLLSGLANAGLI----ALINQALNATGAALARLLLLfagllvllLLSRLAS--QLLLTRL----GQHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 83 V----LRILEKMRTKLYGIVEpqalffrsRFQTGDMLGVLSEDIEHLqnlylrTIFPSILALVVYSIfVLVIGTF----- 153
Cdd:COG4615 80 VarlrLRLSRRILAAPLERLE--------RIGAARLLAALTEDVRTI------SQAFVRLPELLQSV-ALVLGCLaylaw 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 154 --DVVFALIAACMLATIVFLlpFISLLLMKKHHVTLKQGRNRLYQQLTDAVFG-----LSdwqaSGRKDEFIDKYVEQNA 226
Cdd:COG4615 145 lsPPLFLLTLVLLGLGVAGY--RLLVRRARRHLRRAREAEDRLFKHFRALLEGfkelkLN----RRRRRAFFDEDLQPTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 227 QLLKTEK-RMKRWNHIRDSIIQLVVgIVVVSMIIWTGNEAASeqIAPTVIAAFVLMTLSVTNaliPLSDAIDRIPSYVE- 304
Cdd:COG4615 219 ERYRDLRiRADTIFALANNWGNLLF-FALIGLILFLLPALGW--ADPAVLSGFVLVLLFLRG---PLSQLVGALPTLSRa 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 305 --SAHRLNQVEGNGVlQDEKELPRDKDYVAPKHID-IELNHVSYSYPHSNE---FVLKDVSLQIKAGKKIAILGRSGTGK 378
Cdd:COG4615 293 nvALRKIEELELALA-AAEPAAADAAAPPAPADFQtLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 379 STLLKLLTGALSPLHGEVLLNSEHAHTNLLSKY---ISVLNQKPHLFDTTIGnnvriGKPEATDEEIWKALEKAQLAsHI 455
Cdd:COG4615 372 STLAKLLTGLYRPESGEILLDGQPVTADNREAYrqlFSAVFSDFHLFDRLLG-----LDGEADPARARELLERLELD-HK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 456 ATLPDGlqtkmhemgkRF-----SGGERQRVAFARTLMQEAPIIVLDEPTIGLDPK------TELsLIEtmFSAtEEKTV 524
Cdd:COG4615 446 VSVEDG----------RFsttdlSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfyTEL-LPE--LKA-RGKTV 511
|
570 580 590
....*....|....*....|....*....|
gi 2662793383 525 IWITH-----HLvgiehVDEVIFLDRGKIV 549
Cdd:COG4615 512 IAISHddryfDL-----ADRVLKMDYGKLV 536
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-567 |
1.46e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.81 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehaHTNL-------LSK 410
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG----GMVLseetvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 YISVLNQKP--HLFDTTIGNNV-----RIGKP-EATDEEIWKALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVA 482
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVafgleNIGVPrEEMVERVDQALRQV-----------GMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 483 FARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
....*..
gi 2662793383 561 NEKYRKL 567
Cdd:PRK13635 231 GHMLQEI 237
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
337-572 |
1.76e-29 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 116.93 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHA-----HTnlLSKY 411
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsklplHT--LRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFDTTIGNNVrigKPE--ATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQ 489
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLL-KENEKYRKLY 568
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
....
gi 2662793383 569 ELDK 572
Cdd:cd03288 254 RTDK 257
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
338-558 |
2.16e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYpHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNllSKYISVLNQ 417
Cdd:COG1126 2 IEIENLHKSF-GDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS--KKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 K-----------PHLfdtTIGNNV--------RIGKPEATDEEIwKALEKAQLASHIATLPDGLqtkmhemgkrfSGGER 478
Cdd:COG1126 78 KvgmvfqqfnlfPHL---TVLENVtlapikvkKMSKAEAEERAM-ELLERVGLADKADAYPAQL-----------SGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 479 QRVAFARTLMQEAPIIVLDEPTIGLDPktELS--LIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSH 554
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP--ELVgeVLDVMRDlAKEGMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPP 220
|
....
gi 2662793383 555 EQLL 558
Cdd:COG1126 221 EEFF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
338-558 |
4.22e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.06 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPH-SNEFvlkdvSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-HAHTNLLSKYISVL 415
Cdd:PRK10771 2 LKLTDITWLYHHlPMRF-----DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFD-TTIGNNVRIG-KP-----EATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFARTLM 488
Cdd:PRK10771 77 FQENNLFShLTVAQNIGLGlNPglklnAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 489 QEAPIIVLDEPTIGLDP--KTE-LSLIETMfSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK10771 146 REQPILLLDEPFSALDPalRQEmLTLVSQV-CQERQLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
338-560 |
6.01e-29 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 115.18 E-value: 6.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV--LLNSEHAHTNL--LSKYIS 413
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLFGERRGGEDVweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLF---DTTIGNNVRIGK-------PEATDEEIWKALEKAQL--ASHIATLPdglqtkMHEMgkrfSGGERQRV 481
Cdd:COG1119 82 LVSPALQLRfprDETVLDVVLSGFfdsiglyREPTDEQRERARELLELlgLAHLADRP------FGTL----SQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVeEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
..
gi 2662793383 559 KE 560
Cdd:COG1119 232 TS 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
338-560 |
7.43e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 114.07 E-value: 7.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNLLSKYISVLN- 416
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPHERARAGi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 ----QKPHLFDT-TIGNNVRIGKPEATDEEIwkaleKAQLASHIATLPDgLQTKMHEMGKRFSGGERQRVAFARTLMQEA 491
Cdd:cd03224 78 gyvpEGRRIFPElTVEENLLLGAYARRRAKR-----KARLERVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 492 PIIVLDEPTIGLDPKtelsLIETMFSA-----TEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:cd03224 152 KLLLLDEPSEGLAPK----IVEEIFEAirelrDEGVTILLVEQNArFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-569 |
2.99e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 118.63 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPHsnEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSehahtnllSKYISVLNQKP 419
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 HLFDT-TIGNNVRIGkpeatDEEIWKALEKAQLASHIATLPDG-------LQTKMHEMG--------------------- 470
Cdd:COG0488 71 PLDDDlTVLDTVLDG-----DAELRALEAELEELEAKLAEPDEdlerlaeLQEEFEALGgweaearaeeilsglgfpeed 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 471 -----KRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDpktelslIETM-----FSATEEKTVIWITH--HLvgIEHV- 537
Cdd:COG0488 146 ldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIewleeFLKNYPGTVLVVSHdrYF--LDRVa 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2662793383 538 DEVIFLDRGKIVM-QGSH-----------EQLLKENEKYRKLYE 569
Cdd:COG0488 217 TRILELDRGKLTLyPGNYsayleqraerlEQEAAAYAKQQKKIA 260
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
338-558 |
3.88e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISV 414
Cdd:COG4559 2 LEAENLSVRLGGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHL-FDTTIGNNVRIG------KPEATDEEIWKALEKAQLAS----HIATLpdglqtkmhemgkrfSGGERQRVAF 483
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALGraphgsSAAQDRQIVREALALVGLAHlagrSYQTL---------------SGGEQQRVQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQ-------EAPIIVLDEPTIGLDPKTELSLIETMFSATEEK-TVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSH 554
Cdd:COG4559 145 ARVLAQlwepvdgGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVAVLHDLnLAAQYADRILLLHQGRLVAQGTP 224
|
....
gi 2662793383 555 EQLL 558
Cdd:COG4559 225 EEVL 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
337-574 |
4.90e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.80 E-value: 4.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKYIS 413
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKpHLfdTTIGNNVR-------------IGKPEATDEEIwkaLEKAQLASHIATLPDGLQTKMhemgkrfSGGERQR 480
Cdd:PRK11231 80 LLPQH-HL--TPEGITVRelvaygrspwlslWGRLSAEDNAR---VNQAMEQTRINHLADRRLTDL-------SGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
250
....*....|....*.
gi 2662793383 559 KEnEKYRKLYELDKGI 574
Cdd:PRK11231 227 TP-GLLRTVFDVEAEI 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
336-563 |
5.45e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 336 IDIELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-----LLNSEHAHTNL 407
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 --LSKYISVLNQKP--HLFDTTIGNNVRIGkPE---ATDEEiwkALEKAQLASHIATLPDGLQTKmhemgKRF--SGGER 478
Cdd:PRK13634 81 kpLRKKVGIVFQFPehQLFEETVEKDICFG-PMnfgVSEED---AKQKAREMIELVGLPEELLAR-----SPFelSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 479 QRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEH-VDEVIFLDRGKIVMQGSHE 555
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*...
gi 2662793383 556 QLLKENEK 563
Cdd:PRK13634 232 EIFADPDE 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
338-549 |
8.93e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 111.37 E-value: 8.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV--LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLL 408
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfalDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDT-TIGNNVRI-----GKPEATDEEIwKALEK---AQLASHiatLPDGLqtkmhemgkrfSGGERQ 479
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLplelaGRRDARARAR-ALLERvglGHRLDH---YPAQL-----------SGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIV 549
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
338-552 |
1.18e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 110.72 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPH-SNEFvlkdvSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-HAHTNLLSKYISVL 415
Cdd:TIGR01277 1 LALDKVRYEYEHlPMEF-----DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQsHTGLAPYQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFD-TTIGNNVRIG-KPEATdeeiWKALEKAQLasHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:TIGR01277 76 FQENNLFAhLTVRQNIGLGlHPGLK----LNAEQQEKV--VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 494 IVLDEPTIGLDPKTE---LSLIETMFSaTEEKTVIWITHHLV-GIEHVDEVIFLDRGKIVMQG 552
Cdd:TIGR01277 150 LLLDEPFSALDPLLReemLALVKQLCS-ERQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
354-552 |
1.47e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 110.82 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGAL---SPLHGEVLLNSEHAHTNLLSKYISVLNQKPHLFDT-----T 425
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGltvreT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGlqtkmHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP 505
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 506 KTELSLIETMFS-ATEEKTVIwITHHLVG---IEHVDEVIFLDRGKIVMQG 552
Cdd:cd03234 177 FTALNLVSTLSQlARRNRIVI-LTIHQPRsdlFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
338-560 |
1.85e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 111.62 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS----EHAHTNLLSKYIS 413
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKP--HLFDTTIGNNVRIGkPE---ATDEEIWKALEKAqLAShiatlpDGLQTKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:PRK13644 81 IVFQNPetQFVGRTVEEDLAFG-PEnlcLPPIEIRKRVDRA-LAE------IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
351-559 |
2.23e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 110.50 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 351 NEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNL--LSKYISVLNQKPHLF-DTTIG 427
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLppEKRDISYVPQNYALFpHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNVRIG-----KPEATDEEiwKALEKAQLAsHIATLpdglqtkMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIG 502
Cdd:cd03299 90 KNIAYGlkkrkVDKKEIER--KVLEIAEML-GIDHL-------LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 503 LDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLK 559
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFK 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
338-547 |
3.59e-27 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 109.26 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE------HAHTNLLSKY 411
Cdd:TIGR02673 2 IEFHNVSKAYPGGVA-ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnrlrGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLF-DTTIGNNVRI-----GKPEAT-DEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFA 484
Cdd:TIGR02673 81 IGVVFQDFRLLpDRTVYENVALplevrGKKEREiQRRVGAALRQVGLEHKADAFPEQL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIEtMFSATEEK--TVIWITHHLVGIEHVD-EVIFLDRGK 547
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILD-LLKRLNKRgtTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
340-543 |
7.38e-27 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 108.09 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT-------NLLSKYI 412
Cdd:TIGR03608 1 LKNISKKF--GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskkasKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLFDT-TIGNNVRIG-----KPEAT-DEEIWKALEKAQLASHiatlpdgLQTKMHEMgkrfSGGERQRVAFAR 485
Cdd:TIGR03608 79 GYLFQNFALIENeTVEENLDLGlkykkLSKKEkREKKKEALEKVGLNLK-------LKQKIYEL----SGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFL 543
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVAKQADRVIEL 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
100-566 |
8.17e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 116.16 E-value: 8.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 100 PQALFfrSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSIlalvvySIFVLVIGTFDVVFALIAACMLATIVFLLPFISL-L 178
Cdd:TIGR01271 972 PMAVL--NTMKAGRILNRFTKDMAIIDDMLPLTLFDFI------QLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLrA 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 179 LMKKHHVTLKQ----GRNRLYQQLTDAVFGLSDWQASGRKDEFidKYVEQNAQLLKTEK-----RMKRWNHIRDSIIQLV 249
Cdd:TIGR01271 1044 YFLRTSQQLKQleseARSPIFSHLITSLKGLWTIRAFGRQSYF--ETLFHKALNLHTANwflylSTLRWFQMRIDIIFVF 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 250 VGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLS-VTNALIP---LSDAIDRIPSYVESAHRLNQVEG-NGVLQDEKEL 324
Cdd:TIGR01271 1122 FFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQwAVNSSIDvdgLMRSVSRVFKFIDLPQEEPRPSGgGGKYQLSTVL 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 325 PRDKDYVA---PKHIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPlHGEVLLNSE 401
Cdd:TIGR01271 1202 VIENPHAQkcwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGV 1280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 402 HAHTNLLSKY---ISVLNQKPHLFDTTIGNNVrigKPEA--TDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGG 476
Cdd:TIGR01271 1281 SWNSVTLQTWrkaFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQ 556
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
|
490
....*....|
gi 2662793383 557 LLKENEKYRK 566
Cdd:TIGR01271 1438 LLNETSLFKQ 1447
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
338-562 |
1.33e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.07 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS---KYISV 414
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEklrKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPH--------LFDTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFART 486
Cdd:PRK13648 88 VFQNPDnqfvgsivKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
338-568 |
1.56e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 108.15 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH------AHTNLLSKY 411
Cdd:TIGR02315 2 LEVENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitklrgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFD-TTIGNNVRIGK--------------PEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGG 476
Cdd:TIGR02315 81 IGMIFQHYNLIErLTVLENVLHGRlgykptwrsllgrfSEEDKERALSALERVGLADKAYQRADQL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHL-VGIEHVDEVIFLDRGKIVMQGS 553
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVdLAKKYADRIVGLKAGEIVFDGA 229
|
250
....*....|....*
gi 2662793383 554 HEQLlkENEKYRKLY 568
Cdd:TIGR02315 230 PSEL--DDEVLRHIY 242
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-552 |
2.34e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 106.10 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 335 HIDIELNHVSYSYPH----SNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLH--GEVLLNSEHAHTNLL 408
Cdd:cd03213 1 GVTLSFRNLTVTVKSspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFdttignnvrigkPEATdeeIWKALekaQLASHIatlpdglqtkmhemgKRFSGGERQRVAFARTLM 488
Cdd:cd03213 81 RKIIGYVPQDDILH------------PTLT---VRETL---MFAAKL---------------RGLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHL--VGIEHVDEVIFLDRGKIVMQG 552
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
191-567 |
2.39e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.84 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 191 RNRLYQQLTDAVFGLSD---WQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRdsiIQLVVGIvvvsMIIWT------ 261
Cdd:PLN03130 1088 RSPVYAQFGEALNGLSTiraYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIR---LETLGGL----MIWLTasfavm 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 262 GNEAASEQIAPTVIAAFVL-MTLSVTNALiplsDAIDRIPSYVESAhrLNQVE--GNGVlqdekELPRDKDYVA------ 332
Cdd:PLN03130 1161 QNGRAENQAAFASTMGLLLsYALNITSLL----TAVLRLASLAENS--LNAVErvGTYI-----DLPSEAPLVIennrpp 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 333 ---PKHIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS-EHAHTNL- 407
Cdd:PLN03130 1230 pgwPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGLm 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 -LSKYISVLNQKPHLFDTTIGNNVrigKP--EATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFA 484
Cdd:PLN03130 1310 dLRKVLGIIPQAPVLFSGTVRFNL---DPfnEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLL-KENEK 563
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSA 1466
|
....
gi 2662793383 564 YRKL 567
Cdd:PLN03130 1467 FSKM 1470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-557 |
3.02e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.49 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS-EHAHTNL--LSKYISVLNQKPHLFDTTIGNNV 430
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGrEIGAYGLreLRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 431 rigKP--EATDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQE-APIIVLDEPTIGLDPKT 507
Cdd:PTZ00243 1405 ---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPAL 1481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2662793383 508 ELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
338-572 |
5.05e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 113.59 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSY-PHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLL------------------------------- 385
Cdd:PTZ00265 1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 386 -----------------------TGALSPLHGEVLLNS-EHAHTNL--LSKYISVLNQKPHLFDTTIGNNVRIGKPEATD 439
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgeDSTVFKNSGKILLDGvDICDYNLkdLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 440 EEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSAT 519
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 520 E--EKTVIWITHHLVGIEHVDEVIFL---DR-GKIVM-QGSHEQLLK-ENEKYRKLYELDK 572
Cdd:PTZ00265 1406 DkaDKTIITIAHRIASIKRSDKIVVFnnpDRtGSFVQaHGTHEELLSvQDGVYKKYVKLAK 1466
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
338-549 |
6.39e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 6.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnllskyisvlnq 417
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------------------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 kphlfdtTIGNNVRIG---------KPEATD-EEIWKALEKAQLASHIATL------PDGLQTKMhemgKRFSGGERQRV 481
Cdd:COG0488 373 -------KLGETVKIGyfdqhqeelDPDKTVlDELRDGAPGGTEQEVRGYLgrflfsGDDAFKPV----GVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKT----ELSLIEtmFsateEKTVIWITH--HLVGiEHVDEVIFLDRGKIV 549
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETlealEEALDD--F----PGTVLLVSHdrYFLD-RVATRILEFEDGGVR 508
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
338-572 |
7.54e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 7.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNE----FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHAHTNLLS 409
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 KYISVLNQKP--HLFDTTIGNNVRIG------KPEATDEEIWKALEKaqlashiatlpdglqTKMHEMgKRF-----SGG 476
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKK---------------VGMYEY-RRHaphllSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSH 554
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
250 260
....*....|....*....|....*....
gi 2662793383 555 EQLLKENEKYRKL-----------YELDK 572
Cdd:PRK13633 229 KEIFKEVEMMKKIgldvpqvtelaYELKK 257
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
338-558 |
1.00e-25 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 105.85 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSnEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNL--LSKYISV 414
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPveLRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQK----PHLfdtTIGNNVRI-----GKPEATDEEiwKALEKAQLAShiatLPDG--LQTKMHEMgkrfSGGERQRVAF 483
Cdd:cd03295 80 VIQQiglfPHM---TVEENIALvpkllKWPKEKIRE--RADELLALVG----LDPAefADRYPHEL----SGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHhlvgieHVDEVIFL-DR------GKIVMQGSH 554
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTH------DIDEAFRLaDRiaimknGEIVQVGTP 220
|
....
gi 2662793383 555 EQLL 558
Cdd:cd03295 221 DEIL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
338-566 |
2.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNL--LSKYI 412
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpiDYSRKGLmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKP--HLFDTTIGNNVRIGK-----PEatdEEIWKALEKAQLASHIATLPDglqTKMHEMgkrfSGGERQRVAFAR 485
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAvnlklPE---DEVRKRVDNALKRTGIEHLKD---KPTHCL----SFGQKKRVAIAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIE-HVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
....
gi 2662793383 563 KYRK 566
Cdd:PRK13636 235 MLRK 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
338-558 |
3.78e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 103.81 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV--LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNlL 408
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllSGKELRK-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDT-TIGNNVrigkpeATDEEIWKaLEKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFAR 485
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENV------ALPLEIAG-VPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
338-562 |
7.59e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.50 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSP-LHGEVLLNSEHahTNLLSKYI---- 412
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPdDNPNSKITVDG--ITLTAKTVwdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 ---SVLNQKP--HLFDTTIGNNVRIG-------KPEATdEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQR 480
Cdd:PRK13640 84 ekvGIVFQNPdnQFVGATVGDDVAFGlenravpRPEMI-KIVRDVLADVGMLDYIDSEPANL-----------SGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
....
gi 2662793383 559 KENE 562
Cdd:PRK13640 232 SKVE 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
338-549 |
9.98e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 100.58 E-value: 9.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehahtnllskyisvlnq 417
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 kphlfdttiGNNVRIGKPeatdeeiwkaleKAQLASHIATLpdglqtkmHEMgkrfSGGERQRVAFARTLMQEAPIIVLD 497
Cdd:cd03216 61 ---------GKEVSFASP------------RDARRAGIAMV--------YQL----SVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 498 EPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIV 549
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
354-531 |
1.03e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsEHAHtnllSKYISVLNQKPHLFDT---TIGNNV 430
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----RRAG----GARVAYVPQRSEVPDSlplTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 431 RIG---------KPEATDE-EIWKALEKAQLAshiatlpdglqtkmhEMGKR----FSGGERQRVAFARTLMQEAPIIVL 496
Cdd:NF040873 79 AMGrwarrglwrRLTRDDRaAVDDALERVGLA---------------DLAGRqlgeLSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 2662793383 497 DEPTIGLDPKTELSLIETMFSATEEK-TVIWITHHL 531
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGaTVVVVTHDL 179
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-568 |
1.14e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 102.75 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEhahtnllskyiSVLNQK 418
Cdd:COG0410 5 EVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE-----------DITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 PH---------------LFDT-TIGNNVRIGKPEATDeeiwKALEKAQLASHIATLPDgLQTKMHEMGKRFSGGERQRVA 482
Cdd:COG0410 72 PHriarlgigyvpegrrIFPSlTVEENLLLGAYARRD----RAEVRADLERVYELFPR-LKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 483 FARTLMQEAPIIVLDEPTIGLDPKtelsLIETMFSA-----TEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQ 556
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPL----IVEEIFEIirrlnREGVTILLVEQNArFALEIADRAYVLERGRIVLEGTAAE 222
|
250
....*....|..
gi 2662793383 557 LLkENEKYRKLY 568
Cdd:COG0410 223 LL-ADPEVREAY 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
269-546 |
2.17e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 269 QIAPTVIAA---F-------VLMTLS-----VTNALIPLSDAIDRIPSYVESAHRLNQVEGNgvLQDEKELPRDKDYVAP 333
Cdd:COG4178 280 VIFPILVAApryFageitlgGLMQAAsafgqVQGALSWFVDNYQSLAEWRATVDRLAGFEEA--LEAADALPEAASRIET 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 334 KHID-IELNHVSYSYPHsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGaLSPL-HGEVLLnseHAHTNLLsky 411
Cdd:COG4178 358 SEDGaLALEDLTLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIAR---PAGARVL--- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 isVLNQKPHLFDTTIGNNVRIGKPEA--TDEEIWKALEKAQLashiatlpDGLQTKMHEM---GKRFSGGERQRVAFART 486
Cdd:COG4178 430 --FLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGL--------GHLAERLDEEadwDQVLSLGEQQRLAFARL 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRG 546
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
338-571 |
3.03e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNLLSKYISV 414
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLfdttignNVRI---------------GKPEATDEEIwkaLEKAqlashIATLpdglqtKMHEMGKRF----SG 475
Cdd:COG4604 80 LRQENHI-------NSRLtvrelvafgrfpyskGRLTAEDREI---IDEA-----IAYL------DLEDLADRYldelSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHlvgIEHV----DEVIFLDRGKIV 549
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHD---INFAscyaDHIVAMKDGRVV 215
|
250 260
....*....|....*....|..
gi 2662793383 550 MQGSHEQLLKEnEKYRKLYELD 571
Cdd:COG4604 216 AQGTPEEIITP-EVLSDIYDTD 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
354-563 |
3.19e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 101.36 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLlskYISVLNQKPHLFDT-T 425
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPHEIARL---GIGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVRIGKPEATDEEIWKAL---EKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLARarrEEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 501 IGLDP--KTELS-LIETMfsATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKeNEK 563
Cdd:cd03219 172 AGLNPeeTEELAeLIREL--RERGITVLLVEHDMdVVMSLADRVTVLDQGRVIAEGTPDEVRN-NPR 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
338-570 |
3.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV---LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL-------NSEHAHTNL 407
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVLNQKP--HLFDTTIGNNVRIGKPE--ATDEEIWK-ALEKAQLAshiatlpdGLQTKMHEMGK-RFSGGERQRV 481
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKiAAEKLEMV--------GLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIEtMFSATEE--KTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQsgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVF 232
|
250
....*....|..
gi 2662793383 559 KENEkYRKLYEL 570
Cdd:PRK13643 233 QEVD-FLKAHEL 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-546 |
4.25e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 100.48 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 350 SNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH------AHTNLLSKY-ISVLNQKPHLF 422
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNesepsfEATRSRNRYsVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 423 DTTIGNNVRIGKPeaTDEEIWKALEKA-QLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:cd03290 92 NATVEENITFGSP--FNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2662793383 502 GLDPKTELSLIET---MFSATEEKTVIWITHHLVGIEHVDEVIFLDRG 546
Cdd:cd03290 170 ALDIHLSDHLMQEgilKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
338-567 |
8.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-----SEHAHTNLLS 409
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 KYISVLNQKP--HLFDTTIGNNVRIGKPE--ATDEEIWKALEKAQlasHIATLP-DGLQTKM-HEMgkrfSGGERQRVAF 483
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINlgLSEEEIENRVKRAM---NIVGLDyEDYKDKSpFEL----SGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
....*..
gi 2662793383 561 NEKYRKL 567
Cdd:PRK13637 236 VETLESI 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
338-553 |
1.27e-23 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 99.12 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN--SEHAHTNLLSKYISVL 415
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgySIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT-TIGNNVRI-----GKPEATdeeiwkalEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQ 489
Cdd:cd03263 81 PQFDALFDElTVREHLRFyarlkGLPKSE--------IKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGS 553
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGS 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
338-557 |
1.42e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.98 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphsNEFV-LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHA--HTNLLSKYISV 414
Cdd:cd03265 1 IEVENLVKKY---GDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGnnvrigkpeaTDEEIWKA----LEKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:cd03265 78 VFQDLSVDDELTG----------WENLYIHArlygVPGAERRERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSL---IETMfSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVweyIEKL-KEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
337-574 |
1.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.85 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNL------ 407
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLkkikev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 --LSKYISVLNQKP--HLFDTTIGNNVRIGkPEATDEEIWKALEKAQLASHIATLPDglqtkmhEMGKR----FSGGERQ 479
Cdd:PRK13645 86 krLRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPE-------DYVKRspfeLSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG---- 552
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGspfe 237
|
250 260 270
....*....|....*....|....*....|
gi 2662793383 553 --SHEQLLKENE-----KYRKLYEL-DKGI 574
Cdd:PRK13645 238 ifSNQELLTKIEidppkLYQLMYKLkNKGI 267
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
334-570 |
1.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 334 KHIDIELNHVS--YSYPHSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV----LLNSEHAHTN 406
Cdd:PRK13631 18 DDIILRVKNLYcvFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 407 L---------------LSKYISVLNQKP--HLFDTTIGNNVRIGkPEATDEEIWKALEKAqlASHIATLpdGLQTKMHEM 469
Cdd:PRK13631 98 ElitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLA--KFYLNKM--GLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 470 GK-RFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLvgiEHV----DEVIFL 543
Cdd:PRK13631 173 SPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTM---EHVlevaDEVIVM 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 544 DRGKIVMQGSHEQ------------------------LLKENEKYRKLYEL 570
Cdd:PRK13631 250 DKGKILKTGTPYEiftdqhiinstsiqvprviqvindLIKKDPKYKKLYQK 300
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
347-529 |
1.63e-23 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 98.26 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 347 YPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLS--KYISVLNQKP-- 419
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEpldYSRKGLLErrQRVGLVFQDPdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 HLFDTTIGNNVRIG------KPEATDEEIWKALEKAQlASHIATLPdglqTKMhemgkrFSGGERQRVAFARTLMQEAPI 493
Cdd:TIGR01166 80 QLFAADVDQDVAFGplnlglSEAEVERRVREALTAVG-ASGLRERP----THC------LSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITH 529
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTH 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
338-568 |
1.74e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYISV 414
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQK---------PHLFDTTIGNNVRIGkPEATDEEIWKALEKA-QLASHIATLPDGLQTKMHEMgkrfSGGERQRVAFA 484
Cdd:PRK13646 83 VRKRigmvfqfpeSQLFEDTVEREIIFG-PKNFKMNLDEVKNYAhRLLMDLGFSRDVMSQSPFQM----SGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
....*..
gi 2662793383 562 EKYRKLY 568
Cdd:PRK13646 238 KKLADWH 244
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-572 |
1.89e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVL-----------LNSEHAHTNLLSKYISVLNQKPHLF 422
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 423 -DTTIGNNVRIG----KPEATDEEIwkALEKAQLASHiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLD 497
Cdd:PRK11264 98 pHRTVLENIIEGpvivKGEPKEEAT--ARARELLAKV------GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 498 EPTIGLDPKTELSLIETMFSATEEK-TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKENEKYRKLYELDK 572
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLEK 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
338-566 |
1.94e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.15 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLS--KYI 412
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikYDKKSLLEvrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKP--HLFDTTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFA 484
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHH---LVGIeHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHdvdLVPV-YADKVYVMSDGKIIKEGTPKEVFSDI 228
|
....*
gi 2662793383 562 EKYRK 566
Cdd:PRK13639 229 ETIRK 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
338-562 |
2.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKYISV 414
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKP--HLFDTTIGNNVRIGKPE-ATDEEIWKalEKAQLASHIATLPDGLQTKMHEMgkrfSGGERQRVAFARTLMQEA 491
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINlGLDEETVA--HRVSSALHMLGLEELRDRVPHHL----SGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
338-547 |
2.49e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 95.98 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnllskyisvlnq 417
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 kphlfdtTIGNNVRIGkpeatdeeiwkalekaqlasHIATLpdglqtkmhemgkrfSGGERQRVAFARTLMQEAPIIVLD 497
Cdd:cd03221 58 -------TWGSTVKIG--------------------YFEQL---------------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 498 EPTIGLDPKTELSLIETMfsATEEKTVIWITHHLVGIEHV-DEVIFLDRGK 547
Cdd:cd03221 96 EPTNHLDLESIEALEEAL--KEYPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
338-568 |
5.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV---LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-----LLNSEHAHTNL-- 407
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyHITPETGNKNLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVLNQKP--HLFDTTIGNNVRIGKPE--ATDEEiwkALEKAQLASHIATLPDGLqtkMHEMGKRFSGGERQRVAF 483
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNfgFSEDE---AKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
....*..
gi 2662793383 562 EKYRKLY 568
Cdd:PRK13641 237 EWLKKHY 243
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
354-549 |
5.46e-23 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.42 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLLSKYISVLNQKPHLF-DTT 425
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNgqslsklSSNERAKLRNKKLGFIYQFHHLLpDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVR----IGKPEATD--EEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFARTLMQEAPIIVLDEP 499
Cdd:TIGR02211 100 ALENVAmpllIGKKSVKEakERAYEMLEKVGLEHRINHRPSEL-----------SGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 500 TIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIV 549
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELntSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
338-560 |
6.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF---VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNL 407
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVLNQKP--HLFDTTIGNNVRIGkPE---ATDEEIWK-ALEKAQLAshiatlpdGLQTKMHEMGK-RFSGGERQR 480
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFG-PQnfgVSQEEAEAlAREKLALV--------GISESLFEKNPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIeTMFSATEEK--TVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELM-TLFKKLHQSgmTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDI 232
|
...
gi 2662793383 558 LKE 560
Cdd:PRK13649 233 FQD 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
338-557 |
6.64e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 6.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphsNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSP---LHGEVLLNSEhahtNLLSKY 411
Cdd:COG1117 12 IEVRNLNVYY---GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPgarVEGEILLDGE----DIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLN---------QKPHLFDTTIGNNVRIG-------KPEATDEEIWKALEKAQLashiatlPDGLQTKMHEMGKRFSG 475
Cdd:COG1117 85 VDVVElrrrvgmvfQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAAL-------WDEVKDRLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHL-----VGiehvDEVIFLDRGKIVM 550
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMqqaarVS----DYTAFFYLGELVE 233
|
....*..
gi 2662793383 551 QGSHEQL 557
Cdd:COG1117 234 FGPTEQI 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
89-561 |
1.03e-22 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 103.10 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 89 KMRTKLYGIVEPQALFF----RSRFQTGDMLGVLSEDIEHLQNL--YLRTIFPSILAlVVYSIFVLVIGTFDVVFALIAa 162
Cdd:TIGR00957 388 RIKTAVMGAVYRKALVItnsaRKSSTVGEIVNLMSVDAQRFMDLatYINMIWSAPLQ-VILALYFLWLNLGPSVLAGVA- 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 163 cmlaTIVFLLPFISLLLMKKH-----HVTLKQGRNRLYQQLTDA--VFGLSDWQASgrkdeFIDKYV---EQNAQLLKTE 232
Cdd:TIGR00957 466 ----VMVLMVPLNAVMAMKTKtyqvaHMKSKDNRIKLMNEILNGikVLKLYAWELA-----FLDKVEgirQEELKVLKKS 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 233 KRMkrwnHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTViAAFVlmTLSVTNAL-IPLSDAIDRIPSYVESAHRLNQ 311
Cdd:TIGR00957 537 AYL----HAVGTFTWVCTPFLVALITFAVYVTVDENNILDAE-KAFV--SLALFNILrFPLNILPMVISSIVQASVSLKR 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 312 VEgngVLQDEKELprDKDYVAPKHID------IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLL 385
Cdd:TIGR00957 610 LR---IFLSHEEL--EPDSIERRTIKpgegnsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 386 TGALSPLHGEVLLNSEHAHtnllskyisvLNQKPHLFDTTIGNNVRIGKPeaTDEEIWKA-LEKAQLASHIATLPDGLQT 464
Cdd:TIGR00957 685 LAEMDKVEGHVHMKGSVAY----------VPQQAWIQNDSLRENILFGKA--LNEKYYQQvLEACALLPDLEILPSGDRT 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 465 KMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSAT---EEKTVIWITHHLVGIEHVDEVI 541
Cdd:TIGR00957 753 EIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQVDVII 832
|
490 500
....*....|....*....|
gi 2662793383 542 FLDRGKIVMQGSHEQLLKEN 561
Cdd:TIGR00957 833 VMSGGKISEMGSYQELLQRD 852
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
338-558 |
1.08e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTgALSPLHGEVLL------NSEHAHTNLLSKY 411
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN-KLEEITSGDLIvdglkvNDPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLF-DTTIGNNVRIG--KPEATDEEIWKALEKAQLASHiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:PRK09493 79 AGMVFQQFYLFpHLTALENVMFGplRVRGASKEEAEKQARELLAKV------GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLI 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-548 |
1.08e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVL-----LNSEHAHTNLLSKYISV 414
Cdd:PRK11247 15 LNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtapLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKphlfdtTIGNNVRIG-----KPEATDeeiwkALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFARTLMQ 489
Cdd:PRK11247 93 LPWK------KVIDNVGLGlkgqwRDAALQ-----ALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 490 EAPIIVLDEPTIGLDPKTEL---SLIETMFSaTEEKTVIWITHHLV-GIEHVDEVIFLDRGKI 548
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIemqDLIESLWQ-QHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
338-548 |
1.22e-22 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 96.32 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTN---LLSKY 411
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRaipYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLF-DTTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFA 484
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGI--EHVDEVIFLDRGKI 548
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
337-553 |
1.29e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.40 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN--------SEHAHTNLL 408
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglpPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SkyisvlnQK----PHLfdtTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGER 478
Cdd:COG3842 83 F-------QDyalfPHL---TVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYPHQL-----------SGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 479 QRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHL-----VGiehvDEVIFLDRGKIVMQ 551
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQeealaLA----DRIAVMNDGRIEQV 217
|
..
gi 2662793383 552 GS 553
Cdd:COG3842 218 GT 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
338-552 |
1.34e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 96.11 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKkIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHA--HTNLLSKYISVL 415
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDT--------TIGNNVRIGKPEAtDEEIWKALEKAQLASHiatlpdglqtkMHEMGKRFSGGERQRVAFARTL 487
Cdd:cd03264 78 PQEFGVYPNftvrefldYIAWLKGIPSKEV-KARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIE-HVDEVIFLDRGKIVMQG 552
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
338-566 |
1.49e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 97.62 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSpLHGEVLLNSEHAHTNLLSKY---ISV 414
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWrkaFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNNVrigKPEA--TDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAP 492
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRK 566
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
338-559 |
2.53e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.30 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsnEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSK--YISV 414
Cdd:COG1118 3 IEVRNISKRFG---SFtLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRerRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLF-DTTIGNNV----RIGKPeaTDEEIwKA-----LEKAQLAshiatlpdglqtkmhEMGKRF----SGGERQR 480
Cdd:COG1118 80 VFQHYALFpHMTVAENIafglRVRPP--SKAEI-RArveelLELVQLE---------------GLADRYpsqlSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPK--TEL-----SLIETMfsateEKTVIWITHHlvgIEHV----DEVIFLDRGKIV 549
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKvrKELrrwlrRLHDEL-----GGTTVFVTHD---QEEAlelaDRVVVMNQGRIE 213
|
250
....*....|
gi 2662793383 550 MQGSHEQLLK 559
Cdd:COG1118 214 QVGTPDEVYD 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-539 |
2.88e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.64 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTgALSPLHGEVLLNSE-----------HAHTN 406
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRveffnqniyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 407 LLSKYISVLNQKPHLFDTTIGNNVRIG------KPEATDEEIWKALEKAqlashiATLPDGLQTKMHEMGKRFSGGERQR 480
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTEL---SLIETMfSATEEKTVIWITHHLVGIEHVDE 539
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMkveSLIQSL-RLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
244-543 |
2.94e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.64 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 244 SIIQLVVGiVVVSMIIWTgneaaseQIAPTVIAafVLMTLSVTNALIPLsdaIDRIPsyvesahrlnQVEGNgvlQDEKE 323
Cdd:PTZ00265 323 SVISILLG-VLISMFMLT-------IILPNITE--YMKSLEATNSLYEI---INRKP----------LVENN---DDGKK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 324 LPRDKDyvapkhidIELNHVSYSYPHSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH 402
Cdd:PTZ00265 377 LKDIKK--------IQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 403 AHTNLLSKY----ISVLNQKPHLFDTTIGNNVR-----IGKPEA------------------------------------ 437
Cdd:PTZ00265 449 NLKDINLKWwrskIGVVSQDPLLFSNSIKNNIKyslysLKDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnt 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 438 ----------------TDEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PTZ00265 529 tdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2662793383 502 GLDPKTELSLIETM--FSATEEKTVIWITHHLVGIEHVDEVIFL 543
Cdd:PTZ00265 609 SLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
338-557 |
3.92e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSY-PHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNL--LSKYIS 413
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlTEENVwdIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKP--HLFDTTIGNNVRIG---KPEATDEEIWKALEKAQLAshiatlpdGLQT-KMHEMGkRFSGGERQRVAFARTL 487
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGlenKGIPHEEMKERVNEALELV--------GMQDfKEREPA-RLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
354-558 |
4.74e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 98.38 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISVLNQKPHL-FDTTIGNN 429
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsaRAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIGK-PEAT-----DEEIWKALEKAQLASHIATLPDGLQTKMhemgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGL 503
Cdd:PRK09536 98 VEMGRtPHRSrfdtwTETDRAAVERAMERTGVAQFADRPVTSL-------SGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 504 DPKTELSLIETMFSATEE-KTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDgKTAVAAIHDLdLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
355-558 |
5.59e-22 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 95.79 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLLSKYISVLNQK----PH--- 420
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamSRKELRELRRKKISMVFQSfallPHrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 421 LFDTTIGNNVRiGKPEATDEEiwKALEKAQLAshiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:cd03294 120 LENVAFGLEVQ-GVPRAEREE--RAAEALELV--------GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 501 IGLDP--KTELSLIETMFSATEEKTVIWITHHLvgiehvDEVIFL-DR------GKIVMQGSHEQLL 558
Cdd:cd03294 189 SALDPliRREMQDELLRLQAELQKTIVFITHDL------DEALRLgDRiaimkdGRLVQVGTPEEIL 249
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
354-568 |
5.73e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.92 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHahtnlLSKY---------ISVLNQKPHLF-D 423
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD-----ITKLpmhkrarlgIGYLPQEASIFrK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 424 TTIGNNVR-----IGKPEATDEEIWKA-LEKAQLAsHIAtlpdglqtkmHEMGKRFSGGERQRVAFARTLMQEAPIIVLD 497
Cdd:cd03218 90 LTVEENILavleiRGLSKKEREEKLEElLEEFHIT-HLR----------KSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 498 EPTIGLDPKTeLSLIETMFSATEEKTV-IWITHHlvgieHVDEVIFL-DR------GKIVMQGSHEQLLkENEKYRKLY 568
Cdd:cd03218 159 EPFAGVDPIA-VQDIQKIIKILKDRGIgVLITDH-----NVRETLSItDRayiiyeGKVLAEGTPEEIA-ANELVRKVY 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
338-552 |
5.83e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.21 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNLLSKY--ISVL 415
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALrrIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLFDTTIG-NNVRI-----GKPeatDEEIWKALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQ 489
Cdd:cd03268 78 IEAPGFYPNLTArENLRLlarllGIR---KKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
338-555 |
5.92e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYpHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH--AHTNLLSKYISVL 415
Cdd:COG4161 3 IQLKNINCFY-GSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQK-----------PHL--FDTTIGNNVRI-GKPEAtdeeiwKALEKAQlaSHIATLpdGLQTKMHEMGKRFSGGERQRV 481
Cdd:COG4161 81 RQKvgmvfqqynlwPHLtvMENLIEAPCKVlGLSKE------QAREKAM--KLLARL--RLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIwITHHL-VGIEHVDEVIFLDRGKIVMQGSHE 555
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIreLSQTGITQVI-VTHEVeFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
338-560 |
1.15e-21 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 93.84 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHtNLL--SKYISVL 415
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPphKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQK----PHLfdtTIGNNVRIG------KPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFAR 485
Cdd:cd03300 78 FQNyalfPHL---TVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPK------TELSLIETMFsateEKTVIWITH-HLVGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKlrkdmqLELKRLQKEL----GITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
..
gi 2662793383 559 KE 560
Cdd:cd03300 220 EE 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
338-568 |
2.05e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLK----LLTGALSP-LHGEVLLNS------------ 400
Cdd:PRK09984 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAgSHIELLGRTvqregrlardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 401 -EHAHTNLLSKYISVLNQkphlfdTTIGNNVRIGKPEATdeEIWKA----LEKAQLASHIATLPD-GLQTKMHEMGKRFS 474
Cdd:PRK09984 83 kSRANTGYIFQQFNLVNR------LSVLENVLIGALGST--PFWRTcfswFTREQKQRALQALTRvGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 475 GGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSATEEKTVIwITHHLV--GIEHVDEVIFLDRGKIVM 550
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVV-VTLHQVdyALRYCERIVALRQGHVFY 233
|
250
....*....|....*...
gi 2662793383 551 QGSHEQLlkENEKYRKLY 568
Cdd:PRK09984 234 DGSSQQF--DNERFDHLY 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
354-513 |
5.39e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.19 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLLSKYISVLNQKPHLF-DTT 425
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklSSAAKAELRNQKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVR----IGKpEATDEEIWKALEkaQLAShiatlpDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK11629 104 ALENVAmpllIGK-KKPAEINSRALE--MLAA------VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170
....*....|..
gi 2662793383 502 GLDPKTELSLIE 513
Cdd:PRK11629 175 NLDARNADSIFQ 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
338-543 |
5.63e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.70 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKY---ISV 414
Cdd:PRK10247 8 LQLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYrqqVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLFDTTIGNN------VRIGKPEATdeEIWKALEKAQLASHIatlpdgLQTKMHEMgkrfSGGERQRVAFARTLM 488
Cdd:PRK10247 86 CAQTPTLFGDTVYDNlifpwqIRNQQPDPA--IFLDDLERFALPDTI------LTKNIAEL----SGGEKQRISLIRNLQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFL 543
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
338-552 |
6.86e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 91.19 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNL------- 407
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldIAARNRigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 --LSKYISVLNQKPHLFDttignnVRIGKPEATDEEIWKALEKAQLASHiatlpdgLQTKMHEMgkrfSGGERQRVAFAR 485
Cdd:cd03269 79 rgLYPKMKVIDQLVYLAQ------LKGLKKEEARRRIDEWLERLELSEY-------ANKRVEEL----SKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDP-KTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
338-568 |
7.37e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 91.31 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKyISVLNQ 417
Cdd:TIGR03740 1 LETKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK-IGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPHLFDT-TIGNNVRI-----GKPEATDEEIWKALekaqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEA 491
Cdd:TIGR03740 78 SPPLYENlTARENLKVhttllGLPDSRIDEVLNIV--------------DLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETMFSATEEK-TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSheqlLKENEKYRKLY 568
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQGiTVILSSHILSEVQQLaDHIGIISEGVLGYQGK----INKSENLEKLF 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
355-557 |
7.38e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.88 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLT-------GALSpLHGEVLLNSEHAHTNLLSKYISVLNQKPHlfdttiG 427
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTmietptgGELY-YQGQDLLKADPEAQKLLRQKIQIVFQNPY------G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 N-NVR------IGKPEATDEEIWKALEKAQLASHIATLpdGLQTkmhEMGKR----FSGGERQRVAFARTLMQEAPIIVL 496
Cdd:PRK11308 104 SlNPRkkvgqiLEEPLLINTSLSAAERREKALAMMAKV--GLRP---EHYDRyphmFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 497 DEPTIGLDPKTELSLIETMFSATEEKTV--IWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
355-564 |
9.15e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLT--GALSP---LHGEVLLN-----SEHAHTNLLSKYISVLNQKPHLFDT 424
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNghniySPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNNVRIG---KPEATDEEIWKALEKAQLAshiATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK14239 101 SIYENVVYGlrlKGIKDKQVLDEAVEKSLKG---ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 502 GLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL-----KENEKY 564
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMFmnpkhKETEDY 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
83-569 |
9.71e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 96.97 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 83 VLRILEKMRTKLYGIVEPQALFF----RSRFQTGDMLGVLSEDIEHLQN--LYLRTIFPSILALVVYSIFVLV-IGTFDV 155
Cdd:PLN03232 365 VGRVGFRLRSTLVAAIFHKSLRLtheaRKNFASGKVTNMITTDANALQQiaEQLHGLWSAPFRIIVSMVLLYQqLGVASL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 156 VFALIaacmlatIVFLLPFISLLLMKKHHVTlKQGRNRLYQQ--LTDAVFGLSD------WQAS------GRKDEFIDKY 221
Cdd:PLN03232 445 FGSLI-------LFLLIPLQTLIVRKMRKLT-KEGLQWTDKRvgIINEILASMDtvkcyaWEKSfesriqGIRNEELSWF 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 222 veQNAQLLKTekrmkrWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQiAPTVIAAFVLMTLsvtnaliPLSDAIDRIPS 301
Cdd:PLN03232 517 --RKAQLLSA------FNSFILNSIPVVVTLVSFGVFVLLGGDLTPAR-AFTSLSLFAVLRS-------PLNMLPNLLSQ 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 302 YVESAHRLNQVEgNGVLQDEKELPRDKDYV--APKhIDIELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKS 379
Cdd:PLN03232 581 VVNANVSLQRIE-ELLLSEERILAQNPPLQpgAPA-ISIKNGYFSWDSKTSKP-TLSDINLEIPVGSLVAIVGGTGEGKT 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 380 TLLKLLTGALSPLHGEVLLnsehahtnlLSKYISVLNQKPHLFDTTIGNNVRIGKpEATDEEIWKALEKAQLASHIATLP 459
Cdd:PLN03232 658 SLISAMLGELSHAETSSVV---------IRGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLP 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 460 DGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIET-MFSATEEKTVIWITHHLVGIEHVD 538
Cdd:PLN03232 728 GRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMD 807
|
490 500 510
....*....|....*....|....*....|.
gi 2662793383 539 EVIFLDRGKIVMQGSHEQLLKENEKYRKLYE 569
Cdd:PLN03232 808 RIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
337-557 |
1.02e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNLLSK------ 410
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKdrniam 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 -------YisvlnqkPHLfdtTIGNNV----RI-GKPEAT-DEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGE 477
Cdd:COG3839 80 vfqsyalY-------PHM---TVYENIafplKLrKVPKAEiDRRVREAAELLGLEDLLDRKPKQL-----------SGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 478 RQRVAFARTLMQEAPIIVLDEPTIGLDPK------TELSLIETMFSAteekTVIWITHHLV-----GiehvDEVIFLDRG 546
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKlrvemrAEIKRLHRRLGT----TTIYVTHDQVeamtlA----DRIAVMNDG 210
|
250
....*....|.
gi 2662793383 547 KIVMQGSHEQL 557
Cdd:COG3839 211 RIQQVGTPEEL 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-563 |
1.41e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 95.39 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnLLSKYISV--LNQ 417
Cdd:TIGR03719 7 MNRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----------RPQPGIKVgyLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPHLFDT-TIGNNVRIGKPEATD-----EEIWKAL-----EKAQLASHIATLPDGLQTK-MHEMGKR------------- 472
Cdd:TIGR03719 76 EPQLDPTkTVRENVEEGVAEIKDaldrfNEISAKYaepdaDFDKLAAEQAELQEIIDAAdAWDLDSQleiamdalrcppw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 473 ------FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT----ELSLIETmfsateEKTVIWITHHLVGIEHVDEVIF 542
Cdd:TIGR03719 156 dadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQEY------PGTVVAVTHDRYFLDNVAGWIL 229
|
250 260
....*....|....*....|...
gi 2662793383 543 -LDRGK-IVMQGSHEQLLKENEK 563
Cdd:TIGR03719 230 eLDRGRgIPWEGNYSSWLEQKQK 252
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
354-573 |
1.42e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.57 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT----------------NLLSKYISVLNQ 417
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPHLFD-TTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQTKMhemGKRFSGGERQRVAFARTLMQEAPIIVL 496
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKY---PVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 497 DEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKeNEKYRKLYELDKG 573
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLFG-NPQSPRLQQFLKG 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
355-505 |
1.82e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSP---LHGEVLLNSEHAHT-NLLSKYISVLNQKPHLFD-TTIGNN 429
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlPAEQRRIGILFQDDLLFPhLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIGKPEAT-----DEEIWKALEKAQLA----SHIATLpdglqtkmhemgkrfSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:COG4136 97 LAFALPPTIgraqrRARVEQALEEAGLAgfadRDPATL---------------SGGQRARVALLRALLAEPRALLLDEPF 161
|
....*
gi 2662793383 501 IGLDP 505
Cdd:COG4136 162 SKLDA 166
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
336-552 |
2.33e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 89.73 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 336 IDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYIS 413
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEarRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFD-TTIGNNVR-IGKpeatdeeiWKALEKAQLASHIATLPDGLQTK--MHEMGKRFSGGERQRVAFARTLMQ 489
Cdd:cd03266 82 FVSDSTGLYDrLTARENLEyFAG--------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
338-550 |
2.41e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.69 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF--VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN--------SEHAhtnl 407
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDgvpvtgpgADRG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 lskyisVLNQKPHLFD-TTIGNNV----RI-GKPEATDEEIwkALEKAQLAshiatlpdGLQtkmhEMGKRF----SGGE 477
Cdd:COG4525 80 ------VVFQKDALLPwLNVLDNVafglRLrGVPKAERRAR--AEELLALV--------GLA----DFARRRiwqlSGGM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 478 RQRVAFARTLMQEAPIIVLDEPTIGLDPKTElsliETM------FSATEEKTVIWITHhlvgieHVDEVIFLDRGKIVM 550
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTR----EQMqellldVWQRTGKGVFLITH------SVEEALFLATRLVVM 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
338-557 |
2.62e-20 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 90.09 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsnEFV-LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHA-HTNLLSKYISVL 415
Cdd:cd03296 3 IEVRNVSKRFG---DFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLF-DTTIGNNVRIG---KPEATDEeiwkalEKAQLASHIATLPDGLQtkMHEMGKRF----SGGERQRVAFARTL 487
Cdd:cd03296 80 FQHYALFrHMTVFDNVAFGlrvKPRSERP------PEAEIRAKVHELLKLVQ--LDWLADRYpaqlSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 488 MQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITH-HLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
354-540 |
3.54e-20 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 89.37 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLL------------------SKYISVL 415
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWVDLAqasprevlevrrktigyvSQFLRVI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLfDTTIGNNVRIGKPEAtdeeiwKALEKAQLASHIATLPDGLqtkMHEMGKRFSGGERQRVAFARTLMQEAPIIV 495
Cdd:TIGR02324 103 PRVSAL-EVVAEPLLERGVPRE------AARARARELLARLNIPERL---WHLPPATFSGGEQQRVNIARGFIADYPILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2662793383 496 LDEPTIGLDPKTELSLIETMFSATEEKTViwithhLVGIEHVDEV 540
Cdd:TIGR02324 173 LDEPTASLDAANRQVVVELIAEAKARGAA------LIGIFHDEEV 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
349-557 |
3.71e-20 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 91.30 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 349 HSNEFV-LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-----SEHAhtnLLSKYISVLNQKPHLF 422
Cdd:TIGR01188 2 VYGDFKaVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgydvvREPR---KVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 423 DTTIG--NNVRIGkpeatdeEIWkALEKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:TIGR01188 79 EDLTGreNLEMMG-------RLY-GLPKDEAEERAEELLElfELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 499 PTIGLDPKTE---LSLIETMFSatEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:TIGR01188 151 PTTGLDPRTRraiWDYIRALKE--EGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEEL 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-560 |
5.33e-20 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.88 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV--LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLH---GEVLLN-------SEHAHT 405
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDgedllklSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 406 NLLSKYISV--------LNqkPHLfdtTIGNNV-------RIGKPEATDEEIWKALEKAQLASHIATL---PdglqtkmH 467
Cdd:COG0444 82 KIRGREIQMifqdpmtsLN--PVM---TVGDQIaeplrihGGLSKAEARERAIELLERVGLPDPERRLdryP-------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 468 EmgkrFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHL-VGIEHVDEVIFLD 544
Cdd:COG0444 150 E----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLgVVAEIADRVAVMY 225
|
250
....*....|....*.
gi 2662793383 545 RGKIVMQGSHEQLLKE 560
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
354-557 |
5.65e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 90.30 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsEHahtnllSKYISVLNQKPHLFDTTIGNNVRIG 433
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KH------SGRISFSSQFSWIMPGTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 KpeATDEEIWKALEKA-QLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLI 512
Cdd:cd03291 122 V--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIF 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2662793383 513 ET-MFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:cd03291 200 EScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
354-552 |
6.25e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 88.93 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT---NLLSKYISVLNQKPHL-FDTTIGNN 429
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkKFLRRIGVVFGQKTQLwWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIGKpeatdeEIWKaLEKAQLASHIATLPDGLQTK--MHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT 507
Cdd:cd03267 116 FYLLA------AIYD-LPPARFKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2662793383 508 ELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03267 189 QENIRNFLKEYNRERgtTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
338-555 |
6.27e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEvlLNSEHAHTNLLS----KYIS 413
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGT--LNIAGNHFDFSKtpsdKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQK-----------PHLfdtTIGNN-----VRI---GKPEATDEEIwKALEKAQLASHIATLPdglqtkMHemgkrFS 474
Cdd:PRK11124 79 ELRRNvgmvfqqynlwPHL---TVQQNlieapCRVlglSKDQALARAE-KLLERLRLKPYADRFP------LH-----LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 475 GGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTE---LSLIETMfSATEEKTVIwITHHL-VGIEHVDEVIFLDRGKIVM 550
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITaqiVSIIREL-AETGITQVI-VTHEVeVARKTASRVVYMENGHIVE 221
|
....*
gi 2662793383 551 QGSHE 555
Cdd:PRK11124 222 QGDAS 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
354-562 |
6.81e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.53 E-value: 6.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYISVLN-----QKP--------- 419
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLeklviQKTrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 ---------------HLFDTTIGNNVRIGkPEATDEEIWKALEKAQLASHIATLP-DGLQTKMHEMgkrfSGGERQRVAF 483
Cdd:PRK13651 102 eirrrvgvvfqfaeyQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFEL----SGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGI-EHVDEVIFLDRGKIVMQG------SHE 555
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdtydilSDN 256
|
....*..
gi 2662793383 556 QLLKENE 562
Cdd:PRK13651 257 KFLIENN 263
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-568 |
7.21e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 7.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSP---LHGEVLLNSE---HAHTNLLSKYISVLNQKPHLFDT- 424
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNPIPNl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNNVRIG---------KPEaTDEEIWKALEKAQLAshiatlpDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIV 495
Cdd:PRK14247 98 SIFENVALGlklnrlvksKKE-LQERVRWALEKAQLW-------DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 496 LDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKE-----NEKY--RKL 567
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQIVEWGPTREVFTNprhelTEKYvtGRL 249
|
.
gi 2662793383 568 Y 568
Cdd:PRK14247 250 Y 250
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-555 |
7.26e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.08 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnsehahtnllSKYISVLNQKPHLFDTTIGNNVRIG 433
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA----------ERSIAYVPQQAWIMNATVRGNILFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 KPEATdEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT-ELSLI 512
Cdd:PTZ00243 745 DEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2662793383 513 ETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHE 555
Cdd:PTZ00243 824 ECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
338-553 |
7.97e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFV--LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHA----- 403
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalSERElraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 404 --------HTNLLSkyisvlnQKphlfdtTIGNNVrigkpeATDEEIWKaLEKAQLASHIATLPD--GLQTKMHEMGKRF 473
Cdd:COG1135 82 rkigmifqHFNLLS-------SR------TVAENV------ALPLEIAG-VPKAEIRKRVAELLElvGLSDKADAYPSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 474 SGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT-------------ELSLietmfsateekTVIWITHhlvgiE-HV-- 537
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETtrsildllkdinrELGL-----------TIVLITH-----EmDVvr 205
|
250
....*....|....*....
gi 2662793383 538 ---DEVIFLDRGKIVMQGS 553
Cdd:COG1135 206 ricDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
338-561 |
1.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-LLNSEHAHTNL--LSKYISV 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEkwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKP--HLFDTTIGNNVRIG--KPEATDEEIWKALEKAQLAShiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQE 490
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALKAV-------RMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 491 APIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
338-558 |
1.85e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 88.32 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF-------VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV------LLNSEHAH 404
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 405 TNLLSKYISVLNQK-PHLFDTTIGNNVRIGKPEATDEEIWKALEKAQlASHIATLPDGLQTKMHEMGKRFSGGERQRVAF 483
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKAR-IAELLDMVGLRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLL 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
355-569 |
2.06e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.88 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPL-HGEVLLNSEHAhtnllskYISvlnQKPHLFDTTIGNNVRIG 433
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsDASVVIRGTVA-------YVP---QVSWIFNATVRDNILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 KP-EAtdEEIWKALEKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLI 512
Cdd:PLN03130 703 SPfDP--ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 513 ETMFS-ATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENEKYRKLYE 569
Cdd:PLN03130 781 DKCIKdELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-557 |
2.23e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.28 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNLLSKYISVLN 416
Cdd:PRK11607 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKPHLF-DTTIGNNVRIGKPEatdeeiwKALEKAQLASHIATLPDGLQtkMHEMGKR----FSGGERQRVAFARTLMQEA 491
Cdd:PRK11607 98 QSYALFpHMTVEQNIAFGLKQ-------DKLPKAEIASRVNEMLGLVH--MQEFAKRkphqLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 492 PIIVLDEPTIGLDPK----TELSLIETMfsateEK---TVIWITH-HLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDIL-----ERvgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
352-535 |
2.56e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.39 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 352 EFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE--HAHTNLLSKYISVLNQKPHLFDT-TIGN 428
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLYLGHAPGIKTTlSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 NVRIGKPEATDEEIWKALEKAQLAshiatlpdGLQtkmHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTE 508
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLN--------GFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....*...
gi 2662793383 509 LSLIETMFSATEE-KTVIWITHHLVGIE 535
Cdd:cd03231 162 ARFAEAMAGHCARgGMVVLTTHQDLGLS 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
349-558 |
2.64e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 349 HSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAH---TNLLSKYISVLNQKPHL-FDT 424
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEVARRIGLLAQNATTpGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNNVRIGK-PEATDEEIWK-----ALEKAQLASHIATLPDglqtkmhEMGKRFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:PRK10253 97 TVQELVARGRyPHQPLFTRWRkedeeAVTKAMQATGITHLAD-------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 499 PTIGLDPKTELSLIETMFSATEEK--TVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
351-535 |
2.80e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 351 NEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLL---SKYISVLNQ-KPHLfdtTI 426
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeaCHYLGHRNAmKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 427 GNNVRI-----GKPEATDEEiwkALEKAQLAsHIATLPdglqtkmhemGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK13539 91 AENLEFwaaflGGEELDIAA---ALEAVGLA-PLAHLP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 2662793383 502 GLDPKTElSLIETMFSATEEK--TVIWITHHLVGIE 535
Cdd:PRK13539 157 ALDAAAV-ALFAELIRAHLAQggIVIAATHIPLGLP 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-570 |
2.88e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.83 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYS-YPHS-NEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHtnl 407
Cdd:COG1101 2 LELKNLSKTfNPGTvNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklPEYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 lSKYISVLNQKPHL---FDTTIGNNVRI----GKPE----ATDEEiwkalEKAQLASHIATLPDGLQTKMHEMGKRFSGG 476
Cdd:COG1101 79 -AKYIGRVFQDPMMgtaPSMTIEENLALayrrGKRRglrrGLTKK-----RRELFRELLATLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIE-TMFSATEEK-TVIWITHHLV-GIEHVDEVIFLDRGKIVMQGS 553
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNlTTLMVTHNMEqALDYGNRLIMMHEGRIILDVS 232
|
250
....*....|....*..
gi 2662793383 554 HEQllKENEKYRKLYEL 570
Cdd:COG1101 233 GEE--KKKLTVEDLLEL 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
354-557 |
3.11e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 92.28 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsEHahtnllSKYISVLNQKPHLFDTTIGNNVRIG 433
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----KH------SGRISFSPQTSWIMPGTIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 KpeATDEEIWKALEKA-QLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLI 512
Cdd:TIGR01271 511 L--SYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2662793383 513 ET-MFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:TIGR01271 589 EScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
355-558 |
3.20e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.92 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAH---TNLLSKYISVLNQKPhlfDTTIGNNVR 431
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdYSYRSQRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 432 IGK-------------PEATDEEIWKALEKAQLashiatLPDGLQTKMHemgkRFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:PRK15112 106 ISQildfplrlntdlePEQREKQIIETLRQVGL------LPDHASYYPH----MLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 499 PTIGLDPKTELSLIETMFSATEEKTV--IWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
354-568 |
4.69e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 86.56 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNLLSKY---ISVLNQKPHLF-DTTIGN 428
Cdd:TIGR04406 16 VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDiTHLPMHERArlgIGYLPQEASIFrKLTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 NVRIGKpeatdeEIWKALEKAQLASHIATLPDGLQTK--MHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPK 506
Cdd:TIGR04406 96 NIMAVL------EIRKDLDRAEREERLEALLEEFQIShlRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 507 TELSLIETMFSATEEKTVIWITHHLV----GIehVDEVIFLDRGKIVMQGSHEQLLkENEKYRKLY 568
Cdd:TIGR04406 170 AVGDIKKIIKHLKERGIGVLITDHNVretlDI--CDRAYIISDGKVLAEGTPAEIV-ANEKVRRVY 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-567 |
6.64e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS-------EHAHTNLLskYISVLNQ-KPHLfdtTIGN 428
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrDEYHQDLL--YLGHQPGiKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 NVRIGKP---EATDEEIWKALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPtigldp 505
Cdd:PRK13538 94 NLRFYQRlhgPGDDEALWEALAQV-----------GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP------ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 506 ktelslietmFSATEEKTVIWITHHLvgIEHvdevifLDRGKIVMQGSHEQLLKENEKYRKL 567
Cdd:PRK13538 157 ----------FTAIDKQGVARLEALL--AQH------AEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
338-552 |
6.71e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 85.38 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNLLSKY--ISVL 415
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDrdIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQK----PHL--FDT-TIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPdglqtkmhemgKRFSGGERQRVAFARTLM 488
Cdd:cd03301 78 FQNyalyPHMtvYDNiAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 489 QEAPIIVLDEPTIGLDPK------TELSLIETMFSAteekTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKlrvqmrAELKRLQQRLGT----TTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
354-546 |
1.13e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.18 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLL------------------SKYISVL 415
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAqaspreilalrrrtigyvSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLfDTTIGNNVRIGKPEATdeeiwkALEKAQ-LASHIAtLPDGL-----QTkmhemgkrFSGGERQRVAFARTLMQ 489
Cdd:COG4778 106 PRVSAL-DVVAEPLLERGVDREE------ARARAReLLARLN-LPERLwdlppAT--------FSGGEQQRVNIARGFIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEEKT-VIWITHHLVGIEHV-DEVIFLDRG 546
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
338-540 |
1.25e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYP--HsnefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-SEHAHTNL---LSKY 411
Cdd:COG1129 5 LEMRGISKSFGgvK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPVRFRSPrdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFDT-TIGNNVRIGKPEAT----DeeiWKALEkAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFART 486
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRggliD---WRAMR-RRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPK-TElSLIETMFSATEE-KTVIWITHHLvgiehvDEV 540
Cdd:COG1129 155 LSRDARVLILDEPTASLTEReVE-RLFRIIRRLKAQgVAIIYISHRL------DEV 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
340-574 |
1.60e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS---EHAHTNLLSKYISVLN 416
Cdd:PRK10575 14 LRNVSFRVP--GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqplESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QK-PHLFDTTIGNNVRIGK-PEATDEEIWKALEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPII 494
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRyPWHGALGRFGAADREKVEEAISLV--GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 495 VLDEPTIGLDPKTE---LSLIETMfSATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKeNEKYRKLYEL 570
Cdd:PRK10575 170 LLDEPTSALDIAHQvdvLALVHRL-SQERGLTVIAVLHDInMAARYCDYLVALRGGEMIAQGTPAELMR-GETLEQIYGI 247
|
....
gi 2662793383 571 DKGI 574
Cdd:PRK10575 248 PMGI 251
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-567 |
1.62e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE--HAHTNLLSKYIS-VLNQKPHLF-DTTIGNNV 430
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpFKRRKEFARRIGvVFGQRSQLWwDLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 431 RIGKpeatdeEIWKaLEKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTE 508
Cdd:COG4586 118 RLLK------AIYR-IPDAEYKKRLDELVEllDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 509 LSLIEtmF----SATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKENEKYRKL 567
Cdd:COG4586 191 EAIRE--FlkeyNRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-549 |
1.97e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 342 HVSYSYPHSNEF-------VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHahtnllskyISV 414
Cdd:PRK10419 8 GLSHHYAHGGLSgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP---------LAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPH---------LFDTTIG-----NNVR--IGKP------------EATDEEIWKALEKAqlASHIATLPDGLqtkm 466
Cdd:PRK10419 79 LNRAQRkafrrdiqmVFQDSISavnprKTVReiIREPlrhllsldkaerLARASEMLRAVDLD--DSVLDKRPPQL---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 467 hemgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIEtMFSATEEKT---VIWITHHLVGIEH-VDEVIF 542
Cdd:PRK10419 153 -------SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-LLKKLQQQFgtaCLFITHDLRLVERfCQRVMV 224
|
....*..
gi 2662793383 543 LDRGKIV 549
Cdd:PRK10419 225 MDNGQIV 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-562 |
2.51e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 349 HSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGAL-----SPLHGEVLLNSEHAHTNLLS-----KYISVLNQK 418
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpievrREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 PHLF-DTTIGNNVRIG--------KPEATDEEIWKALEKAqlashiaTLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQ 489
Cdd:PRK14267 94 PNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-531 |
2.63e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.83 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 349 HSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLK-------LLTGAlsPLHGEVL-----LNSEHAHTNLLSKYISVLN 416
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTfhgknLYAPDVDPVEVRRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKPHLFDTTIGNNV----RI-GKPEATDEEIWKALEKAqlashiaTLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEA 491
Cdd:PRK14243 98 QKPNPFPKSIYDNIaygaRInGYKGDMDELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHL 531
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
338-560 |
2.72e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.68 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-----HAHtnllSKYI 412
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlHAR----DRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLF-DTTIGNNVRIG--------KP--EATDEEIWKALEKAQLaSHIAT-LPDGLqtkmhemgkrfSGGERQR 480
Cdd:PRK10851 77 GFVFQHYALFrHMTVFDNIAFGltvlprreRPnaAAIKAKVTQLLEMVQL-AHLADrYPAQL-----------SGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITH-HLVGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
...
gi 2662793383 558 LKE 560
Cdd:PRK10851 225 WRE 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
355-550 |
2.77e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 84.05 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYisVLNQKPHLFD-TTIGNNVRIG 433
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPwLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 ----KPEATDEEiwkalEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTEL 509
Cdd:TIGR01184 79 vdrvLPDLSKSE-----RRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2662793383 510 SLIETMFSATEEK--TVIWITHhlvgieHVDEVIFL-DRgkIVM 550
Cdd:TIGR01184 152 NLQEELMQIWEEHrvTVLMVTH------DVDEALLLsDR--VVM 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
338-549 |
2.93e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF--VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE--------VLLNSEhAHTNL 407
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDAD-ALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVLNQKPHLFD-TTIGNNVRIgkpeatdEEIWKALEKAQ-LASHIATLPD-GLQTKMHEMGKRFSGGERQRVAFA 484
Cdd:PRK10535 84 RREHFGFIFQRYHLLShLTAAQNVEV-------PAVYAGLERKQrLLRAQELLQRlGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFLDRGKIV 549
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
338-530 |
2.98e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.20 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGaLSPLH-GEVllnSEHAHTNLLskYISvln 416
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWGsGRI---GMPEGEDLL--FLP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKPHLFDTTIgnnvrigkpeatdeeiwkaleKAQLAshiatlpdglqtkmHEMGKRFSGGERQRVAFARTLMQEAPIIVL 496
Cdd:cd03223 71 QRPYLPLGTL---------------------REQLI--------------YPWDDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*..
gi 2662793383 497 DEPTIGLDPKTE---LSLIETMFSateekTVIWITHH 530
Cdd:cd03223 116 DEATSALDEESEdrlYQLLKELGI-----TVISVGHR 147
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
338-545 |
4.33e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.01 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsEHAHtnllSKYISVLNQ 417
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNG----KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPHLFDT---TIGNNVRIgKPEATDEEIWKALEKAQlASHIatlpdgLQTKMhemgKRFSGGERQRVAFARTLMQEAPII 494
Cdd:PRK09544 75 KLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQ-AGHL------IDAPM----QKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITH--HLVgIEHVDEVIFLDR 545
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHdlHLV-MAKTDEVLCLNH 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-552 |
7.35e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 82.34 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIK---AGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehaHTNLLS-----------KYISVLNQK-- 418
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN----GTVLFDsrkkinlppqqRKIGLVFQQya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 --PHLfdtTIGNNVRIGKPEATDEEIwKALEKAQLAS-HIATLpdgLQTKMHEMgkrfSGGERQRVAFARTLMQEAPIIV 495
Cdd:cd03297 86 lfPHL---NVRENLAFGLKRKRNRED-RISVDELLDLlGLDHL---LNRYPAQL----SGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 496 LDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
338-559 |
7.70e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.16 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNLLSKYISVLN 416
Cdd:PRK11432 7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QK----PHLfdtTIGNNVRIG-------KPEaTDEEIWKALEKAQLAShiatlpdglqtkmheMGKRF----SGGERQRV 481
Cdd:PRK11432 85 QSyalfPHM---SLGENVGYGlkmlgvpKEE-RKQRVKEALELVDLAG---------------FEDRYvdqiSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQfnITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQELY 225
|
.
gi 2662793383 559 K 559
Cdd:PRK11432 226 R 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-299 |
1.18e-17 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 83.75 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 16 MTVTIFLGLLGVSSGAMLLFISGYLIsKSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLY 95
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLI-DDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 96 GIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNL---YLRTIFPSILALVVYSIFVLVIgtfDVVFALIAACMLATIVFLL 172
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvssGLLQLLSDVLTLIGALVILFYL---NWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 173 PFISLLLMKKHHVTLKQgRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGI 252
Cdd:cd07346 157 RYFRRRIRKASREVRES-LAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2662793383 253 VVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRI 299
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
342-558 |
1.57e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 82.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 342 HVSYsypHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLK---LL----TGALSpLHGEVLLNSEHAHTNL------- 407
Cdd:COG4598 15 HKSF---GDLE-VLKGVSLTARKGDVISIIGSSGSGKSTFLRcinLLetpdSGEIR-VGGEEIRLKPDRDGELvpadrrq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVL-------NQKPHLfdtTIGNNV--------RIGKPEATDEEIwKALEKAqlashiatlpdGLQTKMHEMGKR 472
Cdd:COG4598 90 LQRIRTRLgmvfqsfNLWSHM---TVLENVieapvhvlGRPKAEAIERAE-ALLAKV-----------GLADKRDAYPAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 473 FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVM 550
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDlAEEGRTMLVVTHEMGFARDVsSHVVFLHQGRIEE 234
|
....*...
gi 2662793383 551 QGSHEQLL 558
Cdd:COG4598 235 QGPPAEVF 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
318-560 |
1.91e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.62 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 318 LQDEKELPRDKDYVAPKHIdIELNHVSYSYPHSNEFVLK---DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHG 394
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPI-IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 395 E--VLLNSEHAHTNLL--------SKYISVLNQKPHLF--DTTIGNNVRIGKPEATDEeiwKALEKAQLASHIATLPDG- 461
Cdd:TIGR03269 340 EvnVRVGDEWVDMTKPgpdgrgraKRYIGILHQEYDLYphRTVLDNLTEAIGLELPDE---LARMKAVITLKMVGFDEEk 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 462 LQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-D 538
Cdd:TIGR03269 417 AEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVcD 496
|
250 260
....*....|....*....|..
gi 2662793383 539 EVIFLDRGKIVMQGSHEQLLKE 560
Cdd:TIGR03269 497 RAALMRDGKIVKIGDPEEIVEE 518
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
338-553 |
2.23e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.70 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYP-HSNEFV-LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-----------HA- 403
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekelrKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 404 --------HTNLLSKYisvlnqkphlfdtTIGNNVRIgkpeatdeeiwkALE-----KAQLASHIATLPD--GLQTKMHE 468
Cdd:PRK11153 82 rqigmifqHFNLLSSR-------------TVFDNVAL------------PLElagtpKAEIKARVTELLElvGLSDKADR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 469 MGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDR 545
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRIcDRVAVIDA 216
|
....*...
gi 2662793383 546 GKIVMQGS 553
Cdd:PRK11153 217 GRLVEQGT 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
338-549 |
2.28e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsnEFV-LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE--------HAhtnlL 408
Cdd:COG3845 6 LELRGITKRFG---GVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprDA----I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPHLFDT-TIGNNVRIGKPEATdeeiWKALEKAQLASHIATLPD--GLQ----TKMHEMgkrfSGGERQRV 481
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTK----GGRLDRKAARARIRELSEryGLDvdpdAKVEDL----SVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 482 AFARTLMQEAPIIVLDEPTIGLDPK-TElSLIETMFSATEE-KTVIWITHHL--VgIEHVDEVIFLDRGKIV 549
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQeAD-ELFEILRRLAAEgKSIIFITHKLreV-MAIADRVTVLRRGKVV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-558 |
3.74e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 327 DKDYVAPKhidieLNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHG-----EVLLN-- 399
Cdd:PRK14271 14 DVDAAAPA-----MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGgr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 400 SEHAHTNLLS--KYISVLNQKPHLFDTTIGNNVRIG--KPEATDEEIWKALEKAQLAShiATLPDGLQTKMHEMGKRFSG 475
Cdd:PRK14271 89 SIFNYRDVLEfrRRVGMLFQRPNPFPMSIMDNVLAGvrAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHVDE--VIFLDrGKIVMQGS 553
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDraALFFD-GRLVEEGP 245
|
....*
gi 2662793383 554 HEQLL 558
Cdd:PRK14271 246 TEQLF 250
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
338-565 |
4.98e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.35 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSypHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH----AHTNLLS--KY 411
Cdd:PRK11831 8 VDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamSRSRLYTvrKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLF-DTTIGNNVRIGKPEATD--EEIWKALEKAQLASHiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLM 488
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNVAYPLREHTQlpAPLLHSTVMMKLEAV------GLRGAAKLMPSELSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTE---LSLIETMFSATeEKTVIWITHhlvgieHVDEV--------IFLDRgKIVMQGSHEQl 557
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMgvlVKLISELNSAL-GVTCVVVSH------DVPEVlsiadhayIVADK-KIVAHGSAQA- 230
|
....*...
gi 2662793383 558 LKENEKYR 565
Cdd:PRK11831 231 LQANPDPR 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
357-557 |
5.80e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.09 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTnlLSK-----------------YISvLNqkP 419
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG--LSGrelrplrrrmqmvfqdpYAS-LN--P 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 HLfdtTIGNNV-------RIGKPEATDEEIWKALEKAQL-ASHIATLPdglqtkmHEmgkrFSGGERQRVAFARTLMQEA 491
Cdd:COG4608 111 RM---TVGDIIaeplrihGLASKAERRERVAELLELVGLrPEHADRYP-------HE----FSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 492 PIIVLDEPTIGLDP-------------KTELSLietmfsateekTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:COG4608 177 KLIVCDEPVSALDVsiqaqvlnlledlQDELGL-----------TYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDEL 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
355-559 |
7.21e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSP---LHGEVLLNSEHAHTNLLSKyISVLNQKPHLF--------D 423
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRA-ISAYVQQDDLFiptltvreH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 424 TTIGNNVRIGKPEATDEeiwkaleKAQLASHIAT---LPDGLQTKMHEMG--KRFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:TIGR00955 120 LMFQAHLRMPRRVTKKE-------KRERVDEVLQalgLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 499 PTIGLDPKTELSLIETMFS-ATEEKTVIWITH----HLvgIEHVDEVIFLDRGKIVMQGSHEQLLK 559
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHqpssEL--FELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
360-558 |
8.35e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 79.51 E-value: 8.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 360 LQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSehAHTNLLSKYISVLNQKpHLF--DTTI--------GNN 429
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG--ASPGKGWRHIGYVPQR-HEFawDFPIsvahtvmsGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIG---KPEATD-EEIWKALEKAQLAsHIATLPDGlqtkmhemgkRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP 505
Cdd:TIGR03771 78 GHIGwlrRPCVADfAAVRDALRRVGLT-ELADRPVG----------ELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 506 KTELSLIETMFS-ATEEKTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:TIGR03771 147 PTQELLTELFIElAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQ 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-547 |
1.18e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.24 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnLLSKYISV--LNQ 417
Cdd:PRK11819 9 MNRVSKVVP-PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA----------RPAPGIKVgyLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPHLFDT-TIGNNVRIGKPEATD-----EEIWKAL------------EKAQLASHIATLpDG--LQTKMhEMG------- 470
Cdd:PRK11819 78 EPQLDPEkTVRENVEEGVAEVKAaldrfNEIYAAYaepdadfdalaaEQGELQEIIDAA-DAwdLDSQL-EIAmdalrcp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 471 ------KRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLiETmFSATEEKTVIWITHHLVGIEHVDEVIF-L 543
Cdd:PRK11819 156 pwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL-EQ-FLHDYPGTVVAVTHDRYFLDNVAGWILeL 233
|
....
gi 2662793383 544 DRGK 547
Cdd:PRK11819 234 DRGR 237
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
354-553 |
1.49e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALS--------PLHGEVLLNSEHAH---TNLLSKYISVLNQKPH-L 421
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAaidAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 FDTTIGNNVRIGK-PEA---------TDEEIWKALEKAQ----LASHIATLpdglqtkmhemgkrfSGGERQRVAFARTL 487
Cdd:PRK13547 96 FAFSAREIVLLGRyPHArragalthrDGEIAWQALALAGatalVGRDVTTL---------------SGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 488 MQEAP---------IIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGS 553
Cdd:PRK13547 161 AQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPnLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-529 |
1.72e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 82.69 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnseHAHTNLLSKYisvlnqk 418
Cdd:PRK11147 321 EMENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCGTKLEVAY------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 phlFDT---------TIGNNVRIGKPEATDEEIwkalekaqlASHI-ATLPDGLQTKMHEMG--KRFSGGERQRVAFART 486
Cdd:PRK11147 387 ---FDQhraeldpekTVMDNLAEGKQEVMVNGR---------PRHVlGYLQDFLFHPKRAMTpvKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPKTeLSLIETMFsATEEKTVIWITH 529
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVET-LELLEELL-DSYQGTVLLVSH 495
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
369-552 |
2.12e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.14 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 369 AILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNL--LSKYISVLNQKPHLF-DTTIGNNVRIgkpeaTDEEIWKA 445
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLdaVRQSLGMCPQHNILFhHLTVAEHILF-----YAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 446 LEKAQLASHiATLPD-GLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTV 524
Cdd:TIGR01257 1035 WEEAQLEME-AMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
170 180
....*....|....*....|....*....
gi 2662793383 525 IWITHHLvgiehvDEVIFL-DRGKIVMQG 552
Cdd:TIGR01257 1114 IMSTHHM------DEADLLgDRIAIISQG 1136
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-548 |
2.35e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 16 MTVTIFLGLLGVssgAMLLFISGYLIsKSALRPENVMAVYVPIVA-----TRAFSIGQAVF--HYVERLVGhDVVLRILE 88
Cdd:PRK10522 19 MALSLASAALGI---GLIAFINQRLI-ETADTSLLVLPEFLGLLLllmavTLGSQLALTTLghHFVYRLRS-EFIKRILD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 89 KMRTKLYGIVEPQalffrsrfqtgdMLGVLSEDIEHLQNLYLRtifpsiLALVVYSIfVLVIGTFDVVFALIAACMLATI 168
Cdd:PRK10522 94 THVERIEQLGSAS------------LLASLTSDVRNITIAFVR------LPELVQGI-ILTLGSAAYLAWLSPKMLLVTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 169 VFLLPFI---SLLLMK--KHHVTLKQGRNRLYQqltdavfglsDWQA--SGRKD--------EFI-DKYVEQNAQLlkte 232
Cdd:PRK10522 155 IWMAVTIwggFVLVARvyKHMATLRETEDKLYN----------DYQTvlEGRKEltlnreraEYVfENEYEPDAQE---- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 233 krmKRWNHIRDSIIQL-------VVGIVVVSMIIWTGNeaaSEQIAPTVIAAfvlmTLSVTNALI--PLSDAIDRIPSYV 303
Cdd:PRK10522 221 ---YRHHIIRADTFHLsavnwsnIMMLGAIGLVFYMAN---SLGWADTNVAA----TYSLTLLFLrtPLLSAVGALPTLL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 304 ESAHRLNQVEGNGVLQDEKELPRDKdyVAPKHIDIELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLK 383
Cdd:PRK10522 291 SAQVAFNKLNKLALAPYKAEFPRPQ--AFPDWQTLELRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 384 LLTGALSPLHGEVLLNSEHAHTNLLSKY---ISVLNQKPHLFDTTIGNnvriGKPEATDEEIWKALEKAQLAsHIATLPD 460
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYrklFSAVFTDFHLFDQLLGP----EGKPANPALVEKWLERLKMA-HKLELED 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 461 GLQTKMhemgkRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP-------KTELSLIETMfsateEKTVIWITHHLVG 533
Cdd:PRK10522 443 GRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrefyQVLLPLLQEM-----GKTIFAISHDDHY 512
|
570
....*....|....*
gi 2662793383 534 IEHVDEVIFLDRGKI 548
Cdd:PRK10522 513 FIHADRLLEMRNGQL 527
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
355-561 |
2.51e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.73 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGaLSPLHGEVLLNS---EHAHTNLLSKYISVLNQK-PHLFDTTIGNNV 430
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGrplSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 431 RIGKP-EATDEEIWKALekAQLASHIatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQ-------EAPIIVLDEPTIG 502
Cdd:COG4138 91 ALHQPaGASSEAVEQLL--AQLAEAL-----GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 503 LD---PKTELSLIETMfsATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:COG4138 164 LDvaqQAALDRLLREL--CQQGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-557 |
2.99e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.77 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVL---------------------------------- 397
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 398 --LNSEHAHTNLLSKYISVLNQKPHLF--DTTIGNNVRIGKPEA---TDEEIWKALEKAQLAShiatlpdgLQTKMHEMG 470
Cdd:TIGR03269 95 dfWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIgyeGKEAVGRAVDLIEMVQ--------LSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 471 KRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTElSLIETMF--SATEEKTVIWITHHLVGI--EHVDEVIFLDRG 546
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHNALeeAVKASGISMVLTSHWPEVieDLSDKAIWLENG 245
|
250
....*....|.
gi 2662793383 547 KIVMQGSHEQL 557
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-568 |
3.04e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNL------- 407
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 --LSKYISVLNQ-------KphlfdttiGnnvrIGKPEATDE-EIWkaLEKAQLASHIATlpdglqtKMHEMgkrfSGGE 477
Cdd:COG4152 80 rgLYPKMKVGEQlvylarlK--------G----LSKAEAKRRaDEW--LERLGLGDRANK-------KVEEL----SKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 478 RQRVAFARTLMQEAPIIVLDEPTIGLDP-KTELsLIETMFSATEE-KTVIWITHHLvgiEHV----DEVIFLDRGKIVMQ 551
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPvNVEL-LKDVIRELAAKgTTVIFSSHQM---ELVeelcDRIVIINKGRKVLS 210
|
250
....*....|....*..
gi 2662793383 552 GSHEQlLKENEKYRKLY 568
Cdd:COG4152 211 GSVDE-IRRQFGRNTLR 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
338-552 |
3.34e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.96 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF--------------------VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEvl 397
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 398 lnsehahtnllskyISVLNQKPHLFDTTIGNNvrigkPEATDEE------IWKALEKAQLASHI------ATLPDGLQTK 465
Cdd:cd03220 79 --------------VTVRGRVSSLLGLGGGFN-----PELTGREniylngRLLGLSRKEIDEKIdeiiefSELGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 466 MhemgKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFL 543
Cdd:cd03220 140 V----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVL 215
|
....*....
gi 2662793383 544 DRGKIVMQG 552
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-558 |
3.88e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN-------SEHAHTNLLSKYISVLNQK----PHL-- 421
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakiSDAELREVRRKKIAMVFQSfalmPHMtv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 FDTTIGNNVRIGKPEATDEEiwKALEKAQLAshiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRE--KALDALRQV--------GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 502 GLDP--KTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK10070 194 ALDPliRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
347-553 |
4.34e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 347 YPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLS--KYISVLNQKP-- 419
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldYSKRGLLAlrQQVATVFQDPeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 HLFDTTIGNNV-----RIGKPEAtdeEIWKALEKAqlashiATLPDGlQTKMHEMGKRFSGGERQRVAFARTLMQEAPII 494
Cdd:PRK13638 89 QIFYTDIDSDIafslrNLGVPEA---EITRRVDEA------LTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 495 VLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLVGI--EHVDEVIFLDRGKIVMQGS 553
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLiyEISDAVYVLRQGQILTHGA 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-558 |
5.48e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 79.76 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 353 FVLkDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-----HAHTNLLS--KYISVLNQKPHLFDT- 424
Cdd:COG4148 14 FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsARGIFLPPhrRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNNVRIGKPEAtdeeiWKALEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLD 504
Cdd:COG4148 93 SVRGNLLYGRKRA-----PRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 505 P--KTE-LSLIETMfsATEEKT-VIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:COG4148 166 LarKAEiLPYLERL--RDELDIpILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVL 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
352-558 |
5.53e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.77 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 352 EFVLkDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE----HAHTNLLS---KYISVLNQKPHLF-D 423
Cdd:TIGR02142 11 DFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdSRKGIFLPpekRRIGYVFQEARLFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 424 TTIGNNVRIGKPEATDEEiwkalEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGL 503
Cdd:TIGR02142 90 LSVRGNLRYGMKRARPSE-----RRISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 504 DPKTELSLIETMFSATEEKT--VIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGipILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
24-294 |
6.85e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 78.48 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 24 LLGVSSGAmLLFISGYLISKS---ALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYGIVEP 100
Cdd:cd18561 3 LLGLLITA-LYIAQAWLLARAlarIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 101 QALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAACMlATIVFLLPFISLLLM 180
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVF-ALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 181 KKHHVTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIW 260
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270
....*....|....*....|....*....|....
gi 2662793383 261 TGNEAASEQIAPTviAAFVLMTLSVtNALIPLSD 294
Cdd:cd18561 241 GALRVLGGQLTLS--SLLLILFLSR-EFFRPLRD 271
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
354-563 |
7.53e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVLLNSEhahtNLLS---------------------K 410
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGE----DILElspderaragiflafqypveiP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 YISVLNqkphlFDTTIGNNVRIGKPEATD--EEIWKALEKAQLAShiatlpdglqtkmhEMGKR-----FSGGERQRVAF 483
Cdd:COG0396 91 GVSVSN-----FLRTALNARRGEELSAREflKLLKEKMKELGLDE--------------DFLDRyvnegFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDP---KTELSLIETMfsATEEKTVIWITHHLVGIEHV--DEVIFLDRGKIVMQGSHEqLL 558
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIdalRIVAEGVNKL--RSPDRGILIITHYQRILDYIkpDFVHVLVDGRIVKSGGKE-LA 228
|
....*
gi 2662793383 559 KENEK 563
Cdd:COG0396 229 LELEE 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
354-529 |
1.10e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL-------NSEHAHTNLLSKYISVLNQKPHLFDT-T 425
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqMDEEARAKLRAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVRI-----GKPEATDEEIWKALEKaQLashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:PRK10584 105 ALENVELpallrGESSRQSRNGAKALLE-QL---------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|.
gi 2662793383 501 IGLDPKTELSLIETMFSATEE--KTVIWITH 529
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhgTTLILVTH 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-558 |
1.32e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH--AHTNLLSKYISVL 415
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQKPHLF-DTTIGNNVRI-GKpeatdeeiWKALEKAQLASHIATLPD--GLQTKMHEMGKRFSGGERQRVAFARTLMQEA 491
Cdd:PRK13537 86 PQFDNLDpDFTVRENLLVfGR--------YFGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
354-563 |
1.89e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVLLNSEhahtnllskyiSVLNQKPHlfdttignnvr 431
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGE-----------DITDLPPE----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 432 igkpeatdeeiwkalEKAQLASHIA-----TLPdGLQTK--MHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLD 504
Cdd:cd03217 73 ---------------ERARLGIFLAfqyppEIP-GVKNAdfLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 505 pKTELSLIETMFS--ATEEKTVIWITHHLVGIEHV--DEVIFLDRGKIVMQGSHEqLLKENEK 563
Cdd:cd03217 137 -IDALRLVAEVINklREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKE-LALEIEK 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-557 |
2.02e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE---HAHTNLLSKY-IS 413
Cdd:PRK15439 12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcaRLTPAKAHQLgIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLF-DTTIGNNVRIGKPEatdeeiwKALEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAP 492
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGLPK-------RQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 493 IIVLDEPTIGLDPKTelslIETMFS---ATEEKTV--IWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK15439 161 ILILDEPTASLTPAE----TERLFSrirELLAQGVgiVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-560 |
2.23e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 336 IDIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE--VLLNSEHAHTNLLSKYIS 413
Cdd:PRK13536 40 VAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQkphlFDT-----TIGNNV----RIGKPEATDEE--IWKALEKAQLASHIatlpdglQTKMHEMgkrfSGGERQRVA 482
Cdd:PRK13536 118 VVPQ----FDNldlefTVRENLlvfgRYFGMSTREIEavIPSLLEFARLESKA-------DARVSDL----SGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 483 FARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
338-569 |
2.31e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.89 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYP-------------------HSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVL 397
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 398 LNSEHAhtnllskyisvlnqkpHLFDTTIG--------NNVRIG------KPEATDE---EIwkaLEKAQLASHIatlpd 460
Cdd:COG1134 85 VNGRVS----------------ALLELGAGfhpeltgrENIYLNgrllglSRKEIDEkfdEI---VEFAELGDFI----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 461 glQTKMhemgKRFSGGERQRVAFARTLMQEAPIIVLDEptiGL---DP----KTeLSLIETMFSatEEKTVIWITHHLVG 533
Cdd:COG1134 141 --DQPV----KTYSSGMRARLAFAVATAVDPDILLVDE---VLavgDAafqkKC-LARIRELRE--SGRTVIFVSHSMGA 208
|
250 260 270
....*....|....*....|....*....|....*..
gi 2662793383 534 IEHV-DEVIFLDRGKIVMQGSHEQLLKENEKYRKLYE 569
Cdd:COG1134 209 VRRLcDRAIWLEKGRLVMDGDPEEVIAAYEALLAGRE 245
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
338-562 |
2.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNL--LSKYIS 413
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELlTAENVwnLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKP--HLFDTTIGNNVRIGKPEA--TDEEIWKALEKAQLASHIatlpdgLQTKMHEMGkRFSGGERQRVAFARTLMQ 489
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIKRVDEALLAVNM------LDFKTREPA-RLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHEQLLKENE 562
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
356-557 |
2.47e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.89 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 356 KDVSLQIKAGKKIAILGRSGTGKS----TLLKLLTGALSPLHGEVLLNSEHAHTN-LLSKYISVLNQKPH-LFDT--TIG 427
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCaLRGRKIATIMQNPRsAFNPlhTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNVR-----IGKPeATDEEIWKALEKAQLASHIATLpdglqtKMH--EMgkrfSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:PRK10418 100 THARetclaLGKP-ADDATLTAALEAVGLENAARVL------KLYpfEM----SGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 501 IGLDPKTE---LSLIETMFsATEEKTVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK10418 169 TDLDVVAQariLDLLESIV-QKRALGMLLVTHDMgVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-558 |
5.23e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.80 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTL-LKLLtgALSPLHGEVLLNSEHAHTnlLS--------KYISVLNQKP------ 419
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLgLALL--RLIPSEGEIRFDGQDLDG--LSrralrplrRRMQVVFQDPfgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 -HLFDTTIGNNVRIGKPEATDEE----IWKALEKAQLAshiatlPDGLQTKMHEmgkrFSGGERQRVAFARTLMQEAPII 494
Cdd:COG4172 378 rMTVGQIIAEGLRVHGPGLSAAErrarVAEALEEVGLD------PAARHRYPHE----FSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 495 VLDEPTIGLDPKTELSLIEtMFSATEEK---TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:COG4172 448 VLDEPTSALDVSVQAQILD-LLRDLQREhglAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVF 514
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
339-560 |
9.61e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 339 ELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS-EHAHTNL---LSKYISV 414
Cdd:PRK11288 6 SFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqEMRFASTtaaLAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQKPHLF-DTTIGNNVRIGK-PEA---TDEEIWKALEKAQLAsHIATLPDGlQTKMhemgKRFSGGERQRVAFARTLMQ 489
Cdd:PRK11288 84 IYQELHLVpEMTVAENLYLGQlPHKggiVNRRLLNYEAREQLE-HLGVDIDP-DTPL----KYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 490 EAPIIVLDEPTIGLDPKTelslIETMFSATEE-----KTVIWITHHLVGIEHV-DEV-IFLDrGKIV-----MQG-SHEQ 556
Cdd:PRK11288 158 NARVIAFDEPTSSLSARE----IEQLFRVIRElraegRVILYVSHRMEEIFALcDAItVFKD-GRYVatfddMAQvDRDQ 232
|
....
gi 2662793383 557 LLKE 560
Cdd:PRK11288 233 LVQA 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
338-568 |
9.80e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN----SEHAHTNLLSKYIS 413
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkdiTDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQKPHLFD-TTIGNNVRIGKPEATDEEIWKALEKaqlashIATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAP 492
Cdd:PRK11614 84 IVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHLV--GIEHVDEVIFLDRGKIVMQGSHEQLLKeNEKYRKLY 568
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLA-NEAVRSAY 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
370-560 |
1.42e-14 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 74.84 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 370 ILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-AHTNLLSKYISVLNQKPHLF-DTTIGNNVRIG-KPEATDEEIWKAL 446
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvTNVPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 447 EKAQLAshIATLPDGLQTKMHEMgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKtelsLIETM---FSATEEK- 522
Cdd:TIGR01187 81 VLEALR--LVQLEEFADRKPHQL----SGGQQQRVALARALVFKPKILLLDEPLSALDKK----LRDQMqleLKTIQEQl 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2662793383 523 --TVIWITH-HLVGIEHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:TIGR01187 151 giTFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
354-568 |
1.47e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhTNLlSKY------ISVLNQKPHLF-DTTI 426
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THL-PMHkrarlgIGYLPQEASIFrKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 427 GNNVRI-----GKPEAT-DEEIWKALEKAQLaSHIAtlpdglqtkmHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:COG1137 96 EDNILAvlelrKLSKKErEERLEELLEEFGI-THLR----------KSKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 501 IGLDPKTELSLIETMFSATEEKTVIWITHHLV----GIehVDEVIFLDRGKIVMQGSHEQLLkENEKYRKLY 568
Cdd:COG1137 165 AGVDPIAVADIQKIIRHLKERGIGVLITDHNVretlGI--CDRAYIISEGKVLAEGTPEEIL-NNPLVRKVY 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
354-568 |
4.30e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.23 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSE-------HAHTNllsKYISVLNQKPHLFDT-T 425
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplHARAR---RGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNV----RIGKPEATDEEIWKALEKAQlASHIATLPDGLqtkmhemGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK10895 95 VYDNLmavlQIRDDLSAEQREDRANELME-EFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 502 GLDPKTELSLIETMFSATEEKTVIWITHHLV--GIEHVDEVIFLDRGKIVMQGSHEQLLkENEKYRKLY 568
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVreTLAVCERAYIVSQGHLIAHGTPTEIL-QDEHVKRVY 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-557 |
5.56e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKST----LLKLLtgalsPLHGEVLLNSEHAHT----NLL--SKYISVLNQKPHL-- 421
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNlnrrQLLpvRHRIQVVFQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 -----FDTTIGNNVRIGKPEAT----DEEIWKALEKAQLAShiatlpdglqTKMHEMGKRFSGGERQRVAFARTLMQEAP 492
Cdd:PRK15134 376 nprlnVLQIIEEGLRVHQPTLSaaqrEQQVIAVMEEVGLDP----------ETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 493 IIVLDEPTIGLDpKTELSLIETMFSATEEK---TVIWITHHLvgieHV-----DEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK15134 446 LIILDEPTSSLD-KTVQAQILALLKSLQQKhqlAYLFISHDL----HVvralcHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
343-555 |
7.95e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 343 VSYSYPHSnefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYISVLNQKPHL- 421
Cdd:PRK15056 14 VTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 --FDTTIGNNVRIGK---------PEATDEEIW-KALEKAqlashiatlpDGLQTKMHEMGKrFSGGERQRVAFARTLMQ 489
Cdd:PRK15056 91 wsFPVLVEDVVMMGRyghmgwlrrAKKRDRQIVtAALARV----------DMVEFRHRQIGE-LSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFLDRGKIVMQGSHE 555
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
338-552 |
8.14e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSeHAHTNLLSKY-----I 412
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNKLDHKLaaqlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 413 SVLNQKPHLFDT-TIGNNVRIG-----KPEATDEEIWKaleKAQLASHIATLPDGLQTKMHEMGKRFSGGERQRVAFART 486
Cdd:PRK09700 83 GIIYQELSVIDElTVLENLYIGrhltkKVCGVNIIDWR---EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 487 LMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQG 552
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
358-561 |
9.95e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 358 VSLQIKAGKKIAILGRSGTGKSTLLKLLTGaLSPLHGEVLLNS---EHAHTNLLSKYISVL--NQKP-------HLFDTT 425
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGqplEAWSAAELARHRAYLsqQQTPpfampvfQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNVRIGKPEATDEEIWKALekaqlashiatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPII-------VLDE 498
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEAL--------------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 499 PTIGLDPKTEL---SLIETMFSATeeKTVIWITHHLV-GIEHVDEVIFLDRGKIVMQGSHEQLLKEN 561
Cdd:PRK03695 160 PMNSLDVAQQAaldRLLSELCQQG--IAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-544 |
1.26e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.90 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 345 YSYPHS----NEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHahtnllskyISVlnqKPH 420
Cdd:cd03237 1 YTYPTMkktlGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------VSY---KPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 421 LFDTTIGNNVRIGKPEATDEeiwkALEKAQLASHIATlPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:cd03237 69 YIKADYEGTVRDLLSSITKD----FYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2662793383 501 IGLDPKTEL--SLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLD 544
Cdd:cd03237 144 AYLDVEQRLmaSKVIRRFAENNEKTAFVVEHDIIMIDYLaDRLIVFE 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
338-506 |
1.71e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS--------EHAHTNlls 409
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdithvpaENRHVN--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 kyiSVLNQK---PHLfdtTIGNNVRIG-----KPEA-TDEEIWKALEKAQLASHIatlpdglQTKMHEMgkrfSGGERQR 480
Cdd:PRK09452 90 ---TVFQSYalfPHM---TVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFA-------QRKPHQL----SGGQQQR 152
|
170 180
....*....|....*....|....*.
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPK 506
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-529 |
2.09e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnSEHA--------HTNLLS 409
Cdd:PRK15064 320 LEVENLTKGFD--NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SENAnigyyaqdHAYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 KYISvlnqkphLFD-----TTIGNN---VR--IGKPEATDEEIWKALekaqlashiatlpdglqtkmhemgKRFSGGERQ 479
Cdd:PRK15064 397 NDLT-------LFDwmsqwRQEGDDeqaVRgtLGRLLFSQDDIKKSV------------------------KVLSGGEKG 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDpkteLSLIETMFSATE--EKTVIWITH 529
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD----MESIESLNMALEkyEGTLIFVSH 493
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
354-545 |
2.14e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.61 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehahtnllskyisvlnqkphlfdttiGNNVRIG 433
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD---------------------------GKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 434 KPeatdeeiwkaleKAQLASHIATLPD-----GLqtkMHEM--------GKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:cd03215 68 SP------------RDAIRAGIAYVPEdrkreGL---VLDLsvaenialSSLLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2662793383 501 IGLDPKTELSLIETMFSATEE-KTVIWIThhlvgiEHVDEVIFL-DR 545
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAgKAVLLIS------SELDELLGLcDR 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
354-558 |
3.22e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKS----TLLKLLTGALSPLHGEVLLNSEhahtNLLSKYISVLN-----------QK 418
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQ----DLLGLSERELRrirgnriamifQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 P-------HlfdtTIGNNV--------RIGKPEATdEEIWKALEKAQL---ASHIATLPdglqtkmHEMgkrfSGGERQR 480
Cdd:COG4172 101 PmtslnplH----TIGKQIaevlrlhrGLSGAAAR-ARALELLERVGIpdpERRLDAYP-------HQL----SGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLvGI--EHVDEVIFLDRGKIVMQGSHEQ 556
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDL-GVvrRFADRVAVMRQGEIVEQGPTAE 243
|
..
gi 2662793383 557 LL 558
Cdd:COG4172 244 LF 245
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
243-515 |
3.84e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 72.12 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 243 DSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRipsYVESAHRLNQVEGNGVLQDEK 322
Cdd:PRK10636 210 DPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDR---FRAKATKAKQAQSRIKMLERM 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 323 ELprdkdyVAPKHIDIELnHVSYSYPHS----------------NEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLT 386
Cdd:PRK10636 287 EL------IAPAHVDNPF-HFSFRAPESlpnpllkmekvsagygDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 387 GALSPLHGEVllnsehahtnLLSKYISVLNQKPHLF------DTTIGNNVRIGkPEATDEeiwkalekaQLASHIATLpd 460
Cdd:PRK10636 360 GELAPVSGEI----------GLAKGIKLGYFAQHQLeflradESPLQHLARLA-PQELEQ---------KLRDYLGGF-- 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 461 GLQ-TKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETM 515
Cdd:PRK10636 418 GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
338-554 |
5.10e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnSEHAHTNL-------LSK 410
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-SGHDITRLknrevpfLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 411 YISVLNQKPHLF-DTTIGNNVRIGK--PEATDEEIWK----ALEKAqlashiatlpdGLQTKMHEMGKRFSGGERQRVAF 483
Cdd:PRK10908 80 QIGMIFQDHHLLmDRTVYDNVAIPLiiAGASGDDIRRrvsaALDKV-----------GLLDKAKNFPIQLSGGEQQRVGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 484 ARTLMQEAPIIVLDEPTIGLDPktelSLIETMFSATEE-----KTVIWITHHLVGIEHVD-EVIFLDRGKivMQGSH 554
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGH--LHGGV 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
335-557 |
5.88e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 335 HIDIELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV------LLNSEHAHTNLL 408
Cdd:PRK15079 17 HFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdLLGMKDDEWRAV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 409 SKYISVLNQKPhLFD----TTIGNNV----RIGKPEATDEEIwKALEKAQLAShIATLPDGLQTKMHEmgkrFSGGERQR 480
Cdd:PRK15079 97 RSDIQMIFQDP-LASlnprMTIGEIIaeplRTYHPKLSRQEV-KDRVKAMMLK-VGLLPNLINRYPHE----FSGGQCQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 481 VAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
338-543 |
6.40e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnsehahtnllskyisvlnq 417
Cdd:PRK11248 2 LQISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 kphlfdttigNNVRIGKPEAtdeeiwkalEKAQLASHIATLP---------DGLQ----------TKMHEM--------- 469
Cdd:PRK11248 61 ----------DGKPVEGPGA---------ERGVVFQNEGLLPwrnvqdnvaFGLQlagvekmqrlEIAHQMlkkvglega 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 470 GKRF----SGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHhlvgieHVDEVIFL 543
Cdd:PRK11248 122 EKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH------DIEEAVFM 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
357-558 |
1.30e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSehAHTNLLSKYISVLNQKPHLFDT------------ 424
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM--RDGQLRDLYALSEAERRRLLRTewgfvhqhprdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 -----TIGNNV-------------RIgKPEATDeeiWkaLEKAQL-ASHIATLPdglqtkmhemgKRFSGGERQRVAFAR 485
Cdd:PRK11701 102 lrmqvSAGGNIgerlmavgarhygDI-RATAGD---W--LERVEIdAARIDDLP-----------TTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLaVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
354-563 |
3.91e-12 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.52 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVLLN---------SEHAHTNLLSKY--------ISV 414
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKgqdllelepDERARAGLFLAFqypeeipgVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNqkphlFDTTIGNNVRigkpEATDEEIWKALE-KAQLASHIATLpdglqtKMHE-MGKR-----FSGGERQRVAFARTL 487
Cdd:TIGR01978 95 LE-----FLRSALNARR----SARGEEPLDLLDfEKLLKEKLALL------DMDEeFLNRsvnegFSGGEKKRNEILQMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 488 MQEAPIIVLDEPTIGLDP---KTELSLIETMfsATEEKTVIWITHHLVGIEHV--DEVIFLDRGKIVMQGSHEqLLKENE 562
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDIdalKIVAEGINRL--REPDRSFLIITHYQRLLNYIkpDYVHVLLDGRIVKSGDVE-LAKELE 236
|
.
gi 2662793383 563 K 563
Cdd:TIGR01978 237 A 237
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
342-557 |
5.55e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 342 HVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKS----TLLKLL-----TGALSPLHGEVLLN-SEHAHTNLLSKY 411
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaangrIGGSATFNGREILNlPEKELNKLRAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHlfdTTIGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLqtKMHEMGKR-------FSGGERQRVAFA 484
Cdd:PRK09473 99 ISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAV--KMPEARKRmkmypheFSGGMRQRVMIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHL---VGIehVDEVIFLDRGKIVMQGSHEQL 557
Cdd:PRK09473 174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHDLgvvAGI--CDKVLVMYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
338-504 |
6.49e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhsnEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEhahtnllskyISVlnq 417
Cdd:COG1245 342 VEYPDLTKSYG---GFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----------ISY--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KP----HLFDTTIGNNVRIGKPEATDEEIWKalekaqlaSHIATlPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPI 493
Cdd:COG1245 406 KPqyisPDYDGTVEEFLRSANTDDFGSSYYK--------TEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170
....*....|.
gi 2662793383 494 IVLDEPTIGLD 504
Cdd:COG1245 477 YLLDEPSAHLD 487
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
337-548 |
6.69e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 337 DIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKY-ISVL 415
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NQK----PHLfdtTIGNNVRIG-------KPEAtDEEIWKALEKAQLASHIATLPdglqtkmhemgKRFSGGERQRVAFA 484
Cdd:PRK11000 81 FQSyalyPHL---SVAENMSFGlklagakKEEI-NQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 485 RTLMQEAPIIVLDEPTIGLDP------KTELSLIETMFsateEKTVIWITHHLV-GIEHVDEVIFLDRGKI 548
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAalrvqmRIEISRLHKRL----GRTMIYVTHDQVeAMTLADKIVVLDAGRV 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
346-518 |
9.52e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 346 SYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSKYISVLNQKPHL-FDT 424
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLkADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNNVRI------GKPEATDEeiwKALEKAQLASHIATLPdglqtkmhemgKRFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:PRK13543 98 STLENLHFlcglhgRRAKQMPG---SALAIVGLAGYEDTLV-----------RQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180
....*....|....*....|
gi 2662793383 499 PTIGLDPKTeLSLIETMFSA 518
Cdd:PRK13543 164 PYANLDLEG-ITLVNRMISA 182
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
351-504 |
1.89e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 351 NEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEhahtnllskyISVlnqKPHL----FDTTI 426
Cdd:PRK13409 351 GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----------ISY---KPQYikpdYDGTV 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 427 GNNVRiGKPEATDEEIWKalekaqlaSHIATlPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLD 504
Cdd:PRK13409 418 EDLLR-SITDDLGSSYYK--------SEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-556 |
2.59e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSehaHTnllskyisvlnqkphLFDTTIGNNV-----R 431
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RV---------------LFDAEKGICLppekrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 432 IGKpeatdeeiwkALEKAQLASHI---ATLPDGLQTKMHEM--------G-----KRF----SGGERQRVAFARTLMQEA 491
Cdd:PRK11144 78 IGY----------VFQDARLFPHYkvrGNLRYGMAKSMVAQfdkivallGiepllDRYpgslSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 492 PIIVLDEPTIGLD-P-KTEL-SLIETMfsATEEKT-VIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQ 556
Cdd:PRK11144 148 ELLLMDEPLASLDlPrKRELlPYLERL--AREINIpILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEE 215
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
354-564 |
3.19e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVLLNSEhahtnllskyiSVLNQKP----HL------ 421
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE-----------SILDLEPeeraHLgiflaf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 -------------FDTTIGNNVRI--GKPEATDEEIWKAL-EKAQLASHIATLpdgLQTKMHEmgkRFSGGERQRVAFAR 485
Cdd:CHL00131 91 qypieipgvsnadFLRLAYNSKRKfqGLPELDPLEFLEIInEKLKLVGMDPSF---LSRNVNE---GFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDP---KTELSLIETMfsATEEKTVIWITHHLVGIEHV--DEVIFLDRGKIVMQGSHEqLLKE 560
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIdalKIIAEGINKL--MTSENSIILITHYQRLLDYIkpDYVHVMQNGKIIKTGDAE-LAKE 241
|
....
gi 2662793383 561 NEKY 564
Cdd:CHL00131 242 LEKK 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
355-552 |
3.38e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.67 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSP---LHGEVLLNSEHAHTNLlSKYI--SVLNQKPHLFDttignn 429
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFA-EKYPgeIIYVSEEDVHF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 vrigkPEATDEEiwkalekaqlashiaTLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTEL 509
Cdd:cd03233 96 -----PTLTVRE---------------TLDFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2662793383 510 ---SLIETMFSATEEKTVIWITHHLVGIEH-VDEVIFLDRGKIVMQG 552
Cdd:cd03233 156 eilKCIRTMADVLKTTTFVSLYQASDEIYDlFDKVLVLYEGRQIYYG 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
354-529 |
5.19e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLtgALSPLHG------------EVL----------LNSEHAHTNLLSKY 411
Cdd:PLN03073 192 LIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM--AMHAIDGipkncqilhveqEVVgddttalqcvLNTDIERTQLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 412 ISVLNQKPHLFDTTIGNNVRIGKPEATD--------EEIWKALE-------KAQLASHIATL---PDgLQTKMhemGKRF 473
Cdd:PLN03073 270 AQLVAQQRELEFETETGKGKGANKDGVDkdavsqrlEEIYKRLElidaytaEARAASILAGLsftPE-MQVKA---TKTF 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 474 SGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLiETmFSATEEKTVIWITH 529
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ET-YLLKWPKTFIVVSH 399
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
354-552 |
5.99e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGAL--SPLHGEVLLNSEHAHTNLLsKYISVLNQK----PHLF--DTT 425
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQIL-KRTGFVTQDdilyPHLTvrETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNV-RIGKPEATDEEIWKAlekaqlASHIATLpdGLqTKMHE--MGKRF----SGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:PLN03211 162 VFCSLlRLPKSLTKQEKILVA------ESVISEL--GL-TKCENtiIGNSFirgiSGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 499 PTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVG--IEHVDEVIFLDRGKIVMQG 552
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSlAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
338-530 |
7.31e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.42 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGE-------VLLNSEHAHTNL--- 407
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDatvagksILTNISDVHQNMgyc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 --LSKYISVLNQKPHLFdttIGNNVRiGKPEatdEEIWKALEKAqlashIATLpdGLQTKMHEMGKRFSGGERQRVAFAR 485
Cdd:TIGR01257 2018 pqFDAIDDLLTGREHLY---LYARLR-GVPA---EEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2662793383 486 TLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHH 530
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
345-552 |
7.86e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 61.18 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 345 YSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLkLLTGALSPLHGEVLLNSEHAHTNLLskyisVLNQKPHLFDT 424
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-NEGLYASGKARLISFLPKFSRNKLI-----FIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 425 TIGNnVRIGKPEATdeeiwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEAP--IIVLDEPTIG 502
Cdd:cd03238 75 GLGY-LTLGQKLST----------------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2662793383 503 LDPKTELSLIETMFSATEEK-TVIWITHHLVGIEHVDEVIFL------DRGKIVMQG 552
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-558 |
9.47e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKS----TLLKLL-TGALSPLHGEVLLNSE---HAHTNLLSKY----ISVLNQKP-- 419
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGEsllHASEQTLRGVrgnkIAMIFQEPmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 420 -----HLFDTTIGNNV---RIGKPEATDEEIWKALEKA---QLASHIATLPdglqtkmHEMgkrfSGGERQRVAFARTLM 488
Cdd:PRK15134 104 slnplHTLEKQLYEVLslhRGMRREAARGEILNCLDRVgirQAAKRLTDYP-------HQL----SGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 489 QEAPIIVLDEPTIGLDPKTELSLIETMFSATEE--KTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLL 558
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATLF 245
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
20-262 |
1.79e-10 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 61.89 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 20 IFLGLLGVSSGAMLLFISGYL------ISKSALRPENVMAVYVPIVAtrAFSIGQAVFHYVERLVGHDVVLRILEKMRTK 93
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLgrildvLLPDGDPETQALNVYSLALL--LLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 94 LYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLYLRTIFPSILALVVYSIFVLVIGTFDVVFALIAACMLativFLLP 173
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVL----PLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 174 FISLLLMKKHH---VTLKQGRNRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLvV 250
Cdd:pfam00664 156 LVSAVFAKILRklsRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF-I 234
|
250
....*....|..
gi 2662793383 251 GIVVVSMIIWTG 262
Cdd:pfam00664 235 GYLSYALALWFG 246
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-530 |
1.91e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 340 LNHVSYSYPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLS--KYISVLNQ 417
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTyqKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 K----PHLfdtTIGNNVRIG-KPEATDEEIWKALEKAQLaSHIATLPDGLqtkmhemgkrFSGGERQRVAFARTLMQEAP 492
Cdd:PRK13540 82 RsginPYL---TLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHH 530
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-553 |
3.42e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 349 HSNEF-VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnSEHAHTNLLSK------------YISVL 415
Cdd:TIGR00956 70 DTKTFdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV---EGVITYDGITPeeikkhyrgdvvYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 -NQKPHL--FDT--------TIGNnvrigKPEATDEEIWkalekaqlASHIATLPD---GL-QTKMHEMGKRF----SGG 476
Cdd:TIGR00956 147 dVHFPHLtvGETldfaarckTPQN-----RPDGVSREEY--------AKHIADVYMatyGLsHTRNTKVGNDFvrgvSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIetmfSATEEKTVIWITHHLVGI--------EHVDEVIFLDRGKI 548
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFI----RALKTSANILDTTPLVAIyqcsqdayELFDKVIVLYEGYQ 289
|
....*
gi 2662793383 549 VMQGS 553
Cdd:TIGR00956 290 IYFGP 294
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
362-531 |
5.01e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 362 IKAGKKIAILGRSGTGKSTLLKLLTGALSPLHG---------EVLlnsEHAHTNLLSKYISVLNQK-------------- 418
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdEVL---KRFRGTELQNYFKKLYNGeikvvhkpqyvdli 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 PHLFDTTIGNNVrigkpEATDE-----EIWKALE-KAQLASHIATLpdglqtkmhemgkrfSGGERQRVAFARTLMQEAP 492
Cdd:PRK13409 173 PKVFKGKVRELL-----KKVDErgkldEVVERLGlENILDRDISEL---------------SGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*....
gi 2662793383 493 IIVLDEPTIGLDPKTELSLIETMFSATEEKTVIWITHHL 531
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
363-541 |
6.07e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.07 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 363 KAGKKIAILGRSGTGKSTLLKLLTGALSPLHG---------EVLlnSEHAHTNLLSKYISVLN------QKPHLFDTtIG 427
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEIL--DEFRGSELQNYFTKLLEgdvkviVKPQYVDL-IP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNVRiGKpeaTDEEIWKALEKAQLASHIATLpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT 507
Cdd:cd03236 101 KAVK-GK---VGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*
gi 2662793383 508 ELSLIETMFS-ATEEKTVIWITHHLVGIEHVDEVI 541
Cdd:cd03236 175 RLNAARLIRElAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
338-548 |
7.06e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLN--------SEHaHTNLLS 409
Cdd:PLN03073 509 ISFSDASFGYP-GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSakvrmavfSQH-HVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 410 kyisvLNQKPHLFDTTIgnnvrigKPEATDEEIwkaleKAQLASHIATLPDGLQTkMHEMgkrfSGGERQRVAFARTLMQ 489
Cdd:PLN03073 587 -----LSSNPLLYMMRC-------FPGVPEQKL-----RAHLGSFGVTGNLALQP-MYTL----SGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 490 EAPIIVLDEPTIGLDPKTELSLIETMfsATEEKTVIWITH--HLVGiEHVDEVIFLDRGKI 548
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHdeHLIS-GSVDELWVVSEGKV 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-545 |
1.02e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHsnEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnllskyisvlnq 417
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 kphlfdtTIGNNVRIG----KPEATDEE--IWKALEKAQlashiatlpDGLQTKMHEMGKR------------------- 472
Cdd:TIGR03719 380 -------EIGETVKLAyvdqSRDALDPNktVWEEISGGL---------DIIKLGKREIPSRayvgrfnfkgsdqqkkvgq 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 473 FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDpktelslIETMfSATEEK------TVIWITHhlvgiehvdEVIFLDR 545
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-------VETL-RALEEAllnfagCAVVISH---------DRWFLDR 505
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-564 |
1.12e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.29 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALS------PLHGEVLLNSE---HAHTNLLSKYISVLNQKPHLF-D 423
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKdifQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 424 TTIGNNVRIG-KPEATDE--EIWKALEKAQLAshiATLPDGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:PRK14246 105 LSIYDNIAYPlKSHGIKEkrEIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 501 IGLDPKTELSLIETMFSATEEKTVIWITHHLVGIEHV-DEVIFLDRGKIVMQGSHEQLLKE-----NEKY 564
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIFTSpknelTEKY 251
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-547 |
2.80e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTN----LLSKYISVLNQK----PHLfdtTI 426
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpksSQEAGIGIIHQElnliPQL---TI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 427 GNNVRIGKpEATDE--EI-WKAL--EKAQLASHIatlpdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK10762 97 AENIFLGR-EFVNRfgRIdWKKMyaEADKLLARL-----NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 502 GL-DPKTelsliETMFSATEE-----KTVIWITHHLVGI-EHVDEVIFLDRGK 547
Cdd:PRK10762 171 ALtDTET-----ESLFRVIRElksqgRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
338-521 |
8.44e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphsNEFVL-KDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVllnsehahtnllskyisvln 416
Cdd:PRK11819 325 IEAENLSKSF---GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 qkphlfdtTIGNNVRIG---------KPEATdeeIWKALEkaqlashiatlpDGLQTKM---HEMGKR------------ 472
Cdd:PRK11819 382 --------KIGETVKLAyvdqsrdalDPNKT---VWEEIS------------GGLDIIKvgnREIPSRayvgrfnfkggd 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 473 -------FSGGERQRVAFARTLMQEAPIIVLDEPTIGLDpktelslIETMfSATEE 521
Cdd:PRK11819 439 qqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETL-RALEE 486
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
295-529 |
8.87e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 295 AIDRIPSYVESAHRLNQVEGNGVLQDEKELprdkdyvapkhidIELNHVSYSYPhSNEFVLKDVSLQIKAGKKIAILGRS 374
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQDNG-------------IKFENIPLVTP-NGDVLIESLSFEVPSGNNLLICGPN 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 375 GTGKSTLLKLLtGALSPLHGEVLlnSEHAHTNLLskYISvlnQKPHLFDTTIGNNV-------RIGKPEATDEEIWKALE 447
Cdd:TIGR00954 488 GCGKSSLFRIL-GELWPVYGGRL--TKPAKGKLF--YVP---QRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILD 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 448 KAQLaSHIATLPDGLQTkMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTElsliETMFSATEEK--TVI 525
Cdd:TIGR00954 560 NVQL-THILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLF 633
|
....
gi 2662793383 526 WITH 529
Cdd:TIGR00954 634 SVSH 637
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
355-559 |
1.12e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKS----TLLKLLTGALSPLHGEVLL----NSEHAHTNLLSKY---------ISVLNQ 417
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrSRQVIELSEQSAAqmrhvrgadMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 KPH-----LFDT--TIGNNVRIGKPEATDEeiwkALEKAQLASHIATLPDGlQTKMHEMGKRFSGGERQRVAFARTLMQE 490
Cdd:PRK10261 112 EPMtslnpVFTVgeQIAESIRLHQGASREE----AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 491 APIIVLDEPTIGLDPKTELSLIETMFSATEEKT--VIWITHHL-VGIEHVDEVIFLDRGKIVMQGSHEQLLK 559
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMgVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
363-531 |
1.16e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 363 KAGKKIAILGRSGTGKSTLLKLLTGALSPLHG---------EVL---LNSE-HAH-TNLLSKYISVLnQKPHLFDttign 428
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGdydeepswdEVLkrfRGTElQDYfKKLANGEIKVA-HKPQYVD----- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 nvRIgkPEATDEEIWKALEKAQ---LASHIATLPdGLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP 505
Cdd:COG1245 171 --LI--PKVFKGTVRELLEKVDergKLDELAEKL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*....
gi 2662793383 506 KTEL---SLIETMfsATEEKTVIWITHHL 531
Cdd:COG1245 246 YQRLnvaRLIREL--AEEGKYVLVVEHDL 272
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
359-560 |
4.03e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 359 SLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEvlLNSEHAHTNLLSkyisvLNQKPHLFDTTIGNNVRIGKPEAT 438
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--RQSQFSHITRLS-----FEQLQKLVSDEWQRNNTDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 439 DEEIWKALEKAQLASHIATLPDGLQTK---MHEMGKRF---SGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLI 512
Cdd:PRK10938 96 DDTGRTTAEIIQDEVKDPARCEQLAQQfgiTALLDRRFkylSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2662793383 513 ETMFSATEEK-TVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQLLKE 560
Cdd:PRK10938 176 ELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
354-530 |
6.08e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALS--PLHGEVLLNSEHAHTNLlskyiSVLNQKPHLFDTtignnvr 431
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREA-----SLIDAIGRKGDF------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 432 igkPEATdeeiwKALEKAQLASHIATLpdglqTKMHEMgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKT--EL 509
Cdd:COG2401 113 ---KDAV-----ELLNAVGLSDAVLWL-----RRFKEL----STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakRV 175
|
170 180
....*....|....*....|.
gi 2662793383 510 SLIETMFSATEEKTVIWITHH 530
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHH 196
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
22-213 |
6.53e-08 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 54.34 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 22 LGLLGVSSGAMLLFISGYL---ISKSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYGIV 98
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLariIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 99 EPQALFFRSRFQTGDMLGVLSEDIEHLQNlYLRTIFP-SILALVVYSIFVLVIGTFDVVFALIAACMLATIVFLLPFISL 177
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDG-YFARYLPqLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGK 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2662793383 178 L---LMKKHHVTLkqgrNRLYQQLTDAVFGLSDWQASGR 213
Cdd:cd18584 160 AaqaASRRQWAAL----SRLSGHFLDRLRGLPTLKLFGR 194
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
45-262 |
7.50e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 54.44 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 45 ALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEH 124
Cdd:cd18564 44 LLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 125 LQNLYLR---TIFPSILALVVYSIFVLVIgtfDVVFALIAacmLATIVFLLPFISLLLMKKHHVTLKQGRN--RLYQQLT 199
Cdd:cd18564 124 IQDLLVSgvlPLLTNLLTLVGMLGVMFWL---DWQLALIA---LAVAPLLLLAARRFSRRIKEASREQRRRegALASVAQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 200 DAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNhirdSIIQLVVGIVV---VSMIIWTG 262
Cdd:cd18564 198 ESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQ----ALLSPVVDVLVavgTALVLWFG 259
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
472-557 |
9.81e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 472 RFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHV-DEVIFLDRGKIV 549
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLaHELTVIDRGRVI 223
|
....*...
gi 2662793383 550 MQGSHEQL 557
Cdd:NF000106 224 ADGKVDEL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
355-553 |
2.34e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.23 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLL-KLLTGALSP-LHGEVLLNSEHAH---TNLLSKYIsVLNQKPhlfdttIGNN 429
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLInDTLYPALARrLHLKKEQPGNHDRiegLEHIDKVI-VIDQSP------IGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VR------------I-----------------------GKP-----EATDEEIWKALEK-AQLASHIATLPD-GLQ-TKM 466
Cdd:cd03271 84 PRsnpatytgvfdeIrelfcevckgkrynretlevrykGKSiadvlDMTVEEALEFFENiPKIARKLQTLCDvGLGyIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 467 HEMGKRFSGGERQRVAFARTLMQEAP---IIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIF 542
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVVIEHNLDVIKCADWIID 243
|
250
....*....|....*..
gi 2662793383 543 L-----DR-GKIVMQGS 553
Cdd:cd03271 244 LgpeggDGgGQVVASGT 260
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
468-554 |
2.67e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 468 EMGKRFSGGERQ------RVAFARTLMQEAPIIVLDEPTIGLDP-KTELSLIETMFSATEEKT--VIWITHHLVGIEHVD 538
Cdd:cd03240 111 DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNfqLIVITHDEELVDAAD 190
|
90
....*....|....*.
gi 2662793383 539 EVIFLdrGKIVMQGSH 554
Cdd:cd03240 191 HIYRV--EKDGRQKSR 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
318-546 |
2.78e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 318 LQDEKELPRDKDyvapkHIDIELNHVSYSYPHSNE--FVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLL-----TGALS 390
Cdd:TIGR00956 745 VNDEKDMEKESG-----EDIFHWRNLTYEVKIKKEkrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVIT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 391 PlhGEVLLNSeHAHTNLLSKYIS-VLNQKPHLFDTTIGNNVR----------IGKPEATD--EEIWKALEKAQLASHIAT 457
Cdd:TIGR00956 820 G--GDRLVNG-RPLDSSFQRSIGyVQQQDLHLPTSTVRESLRfsaylrqpksVSKSEKMEyvEEVIKLLEMESYADAVVG 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 458 LP-DGLQTKmhemgkrfsggERQRVAFARTLMQEAPIIV-LDEPTIGLDPKTELSLIETMFSATEEKTVIWITHH---LV 532
Cdd:TIGR00956 897 VPgEGLNVE-----------QRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpsAI 965
|
250
....*....|....
gi 2662793383 533 GIEHVDEVIFLDRG 546
Cdd:TIGR00956 966 LFEEFDRLLLLQKG 979
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-280 |
5.18e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 51.38 E-value: 5.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 16 MTVTIFLGLLgvSSGAMLLF--ISGYLISkSALRPENVMAVYVPIVATRAFS-IGQAVFHYVERLVGHDVVLRILEKMRT 92
Cdd:cd18778 1 LILTLLCALL--STLLGLVPpwLIRELVD-LVTIGSKSLGLLLGLALLLLGAyLLRALLNFLRIYLNHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 93 KLYGIVEPQAL-FFRSRfQTGDMLGVLSEDIEHLQNLYLRTI---FPSILALVVYSIFVLVIgtfDVVFALIAacmLATI 168
Cdd:cd18778 78 DLYDKLQRLSLrYFDDR-QTGDLMSRVINDVANVERLIADGIpqgITNVLTLVGVAIILFSI---NPKLALLT---LIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 169 VFLLpFISLLLMKKHHVTLKQGRNRLYQ---QLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKR-MKRWNhIRDS 244
Cdd:cd18778 151 PFLA-LGAWLYSKKVRPRYRKVREALGElnaLLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRaMKLWA-IFHP 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 2662793383 245 IIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVL 280
Cdd:cd18778 229 LMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLL 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
338-506 |
5.86e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYPHSNEfVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEhahtnllskyisVLNQ 417
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR------------VVNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 418 K-----------------PHLfdTTIGN------NVRIGKPE--ATDEEIWKALEKAQLashiatlpdgLQTKMHEMgkr 472
Cdd:PRK11650 71 LepadrdiamvfqnyalyPHM--SVRENmayglkIRGMPKAEieERVAEAARILELEPL----------LDRKPREL--- 135
|
170 180 190
....*....|....*....|....*....|....
gi 2662793383 473 fSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPK 506
Cdd:PRK11650 136 -SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
362-547 |
6.16e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 362 IKAGKKIAILGRSGTGKSTLLKLLTGALSPlhgevllnsEHAHTNLLSKYISVlnqkphlfdttignnvrigKPEATDee 441
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP---------NGDNDEWDGITPVY-------------------KPQYID-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 442 iwkalekaqlashiatlpdglqtkmhemgkrFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETM--FSAT 519
Cdd:cd03222 72 -------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrLSEE 120
|
170 180
....*....|....*....|....*...
gi 2662793383 520 EEKTVIWITHHLVGIEHVDEVIFLDRGK 547
Cdd:cd03222 121 GKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
355-546 |
7.08e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG--ALSPLHGEVLLNSEhahtnllskyisvlnQKPHLFDTTIG--NNV 430
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGR---------------PLDKNFQRSTGyvEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 431 RIGKPEATDEEiwkALEkaqlashIATLPDGLqtkmhemgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELS 510
Cdd:cd03232 88 DVHSPNLTVRE---ALR-------FSALLRGL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 2662793383 511 LIETMFSATEEKTVIWITHH---LVGIEHVDEVIFLDRG 546
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHqpsASIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
66-280 |
8.21e-07 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 50.85 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 66 IGQAVFHYVERLVGHDVVLRILEKMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNLY---LRTIFPSILALVV 142
Cdd:cd18544 52 LLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFtsgLVTLIGDLLLLIG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 143 YSIFVLVIgtfDVVFALIaacMLATIVFLLpFISLLLMKKHHVTLKQGRN---RLYQQLTDAVFGLSDWQASGRKDEFID 219
Cdd:cd18544 132 ILIAMFLL---NWRLALI---SLLVLPLLL-LATYLFRKKSRKAYREVREklsRLNAFLQESISGMSVIQLFNREKREFE 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 220 KYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVL 280
Cdd:cd18544 205 EFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQ 265
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
354-504 |
8.42e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAhtnllskyISVLNQKPHLFDTT-------- 425
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQ--------LAWVNQETPALPQPaleyvidg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 ------------IGNNVRIGKPEATDEEIWKALEKAQLASHIATLPDGL---QTKMHEMGKRFSGGERQRVAFARTLMQE 490
Cdd:PRK10636 88 dreyrqleaqlhDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICR 167
|
170
....*....|....
gi 2662793383 491 APIIVLDEPTIGLD 504
Cdd:PRK10636 168 SDLLLLDEPTNHLD 181
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
63-309 |
9.17e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 50.64 E-value: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 63 AFSIGQAVFHYVE----RLVGHDVVLRIlekmRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNlylrtIFPSIL 138
Cdd:cd18557 44 AIYLLQSVFTFVRyylfNIAGERIVARL----RRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQS-----AVTDNL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 139 ALVVYSIFVLVIGtfdVVFALIAACMLaTIVFLLPFISLLLMkkhhvTLKQGRN--RLYQQLTDAVFGLSDW-------- 208
Cdd:cd18557 115 SQLLRNILQVIGG---LIILFILSWKL-TLVLLLVIPLLLIA-----SKIYGRYirKLSKEVQDALAKAGQVaeeslsni 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 209 ---QASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSV 285
Cdd:cd18557 186 rtvRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMV 265
|
250 260
....*....|....*....|....
gi 2662793383 286 TNALIPLSDAIDRIPSYVESAHRL 309
Cdd:cd18557 266 ASSVGGLSSLLADIMKALGASERV 289
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
474-562 |
9.41e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.94 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 474 SGGERQRVAFARTLMQE--APIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFLDR----- 545
Cdd:TIGR00630 490 SGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLgNTLIVVEHDEDTIRAADYVIDIGPgageh 569
|
90
....*....|....*...
gi 2662793383 546 -GKIVMQGSHEQLLKENE 562
Cdd:TIGR00630 570 gGEVVASGTPEEILANPD 587
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
355-552 |
1.02e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.95 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTL----------LKLLTGaLSPLHGEVLLNSEHAHTNL---LSKYISVlNQKphl 421
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVES-LSAYARQFLGQMDKPDVDSiegLSPAIAI-DQK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 422 fdtTIGNNVR--IGkpeaTDEEIWKALE----KAQLASHIATLPD-GLQ-TKMHEMGKRFSGGERQRVAFARTLMQE--A 491
Cdd:cd03270 86 ---TTSRNPRstVG----TVTEIYDYLRllfaRVGIRERLGFLVDvGLGyLTLSRSAPTLSGGEAQRIRLATQIGSGltG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 492 PIIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITHHLVGIEHVDEVIFL------DRGKIVMQG 552
Cdd:cd03270 159 VLYVLDEPSIGLHPRDNDRLIETLKRLRDLgNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
354-504 |
1.06e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 354 VLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSK-------YIS--------VLNQk 418
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiaYVPedrkgeglVLDL- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 419 phlfdtTIGNNVRIgkpeATDEEIWKAL------EKAQLASHIATL---PDGLQTKMhemgKRFSGGERQRVAFARTLMQ 489
Cdd:COG1129 346 ------SIRENITL----ASLDRLSRGGlldrrrERALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLAT 411
|
170
....*....|....*
gi 2662793383 490 EAPIIVLDEPTIGLD 504
Cdd:COG1129 412 DPKVLILDEPTRGID 426
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
355-567 |
1.22e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHT------NLLSKYISVLNQKPHL-FD--TT 425
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgklQALRRDIQFIFQDPYAsLDprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 426 IGNNV-------RIGKPEATDEEIWKALEKAQLashiatLPDGLQTKMHEmgkrFSGGERQRVAFARTLMQEAPIIVLDE 498
Cdd:PRK10261 420 VGDSImeplrvhGLLPGKAAAARVAWLLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2662793383 499 PTIGLDPKTELSLIETMFSATEEKTV--IWITHHLVGIEHVD-EVIFLDRGKIVMQGSHEQLLkENEKY---RKL 567
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVF-ENPQHpytRKL 563
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
355-549 |
1.41e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNsehahTNLLskyISVLNQKP------HLFDtTIGN 428
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-----QDLI---VARLQQDPprnvegTVYD-FVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 NVrigkpeatdEEIWKALEKAQLASH-IATLPD--------GLQTKM-HEMGKRF----------------------SGG 476
Cdd:PRK11147 90 GI---------EEQAEYLKRYHDISHlVETDPSeknlnelaKLQEQLdHHNLWQLenrinevlaqlgldpdaalsslSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 477 ERQRVAFARTLMQEAPIIVLDEPTIGLDpktelslIETM-----FSATEEKTVIWITHHLVGIEH-----VDevifLDRG 546
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLD-------IETIewlegFLKTFQGSIIFISHDRSFIRNmatriVD----LDRG 229
|
...
gi 2662793383 547 KIV 549
Cdd:PRK11147 230 KLV 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
326-566 |
2.00e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 326 RDKDYVAPKHidielnhvsysyPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEhaht 405
Cdd:PRK13546 23 RMKDALIPKH------------KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 406 nllskyISVLNQKPHLFDTTIG-NNVRIG------KPEATDEEIWKALEKAQLASHIatlpdglqtkmHEMGKRFSGGER 478
Cdd:PRK13546 87 ------VSVIAISAGLSGQLTGiENIEFKmlcmgfKRKEIKAMTPKIIEFSELGEFI-----------YQPVKKYSSGMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 479 QRVAFARTLMQEAPIIVLDEP-TIGLDPKTELSLIETMFSATEEKTVIWITHHLVGI-EHVDEVIFLDRGKIVMQGSHEQ 556
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDD 229
|
250
....*....|
gi 2662793383 557 LLKENEKYRK 566
Cdd:PRK13546 230 VLPKYEAFLN 239
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
44-282 |
2.81e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 49.49 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 44 SALRPENVMA-VYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYGIVepQAL---FFRSRfQTGDMLGVLS 119
Cdd:cd18565 42 ASLGPADPRGqLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHV--QRLdmaFFEDR-QTGDLMSVLN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 120 EDIEHLQNlYLRTIFPSILALVVysiFVLVIGtfdVVFALIAAcMLATIVFL-LPFI---SLLLMKK---HHVTLKQGRN 192
Cdd:cd18565 119 NDVNQLER-FLDDGANSIIRVVV---TVLGIG---AILFYLNW-QLALVALLpVPLIiagTYWFQRRiepRYRAVREAVG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 193 RLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLlktekRMKRWNHIRDSI-----IQLVVGIVVVSMII----WT-- 261
Cdd:cd18565 191 DLNARLENNLSGIAVIKAFTAEDFERERVADASEEY-----RDANWRAIRLRAaffpvIRLVAGAGFVATFVvggyWVld 265
|
250 260
....*....|....*....|.
gi 2662793383 262 GNEAASEQIAPTVIAAFVLMT 282
Cdd:cd18565 266 GPPLFTGTLTVGTLVTFLFYT 286
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
338-558 |
6.57e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 338 IELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-LLN---SEHAHTNLLSKYIS 413
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGgdmADARHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 414 VLNQkphlfdttiGnnvrIGK---PEATDEEiwkALE---------KAQLASHIATLpdgLQ-TKMHE-----MGKrFSG 475
Cdd:NF033858 80 YMPQ---------G----LGKnlyPTLSVFE---NLDffgrlfgqdAAERRRRIDEL---LRaTGLAPfadrpAGK-LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 476 GERQRVAFARTLMQEAPIIVLDEPTIGLDPkteLS------LIETMFSATEEKTVIWITHHLVGIEHVDEVIFLDRGKIV 549
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDP---LSrrqfweLIDRIRAERPGMSVLVATAYMEEAERFDWLVAMDAGRVL 216
|
....*....
gi 2662793383 550 MQGSHEQLL 558
Cdd:NF033858 217 ATGTPAELL 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-540 |
7.69e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTG-------------ALSPLHGEVLLNSEHA-----HTNL-LSKYISVL 415
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyegeiifEGEELQASNIRDTERAgiaiiHQELaLVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 416 NqkpHLFdttIGNNVRIGKPEATDEEIWKA---LEKAQLASHIAtlpdglqTKMHEMGkrfsGGERQRVAFARTLMQEAP 492
Cdd:PRK13549 101 E---NIF---LGNEITPGGIMDYDAMYLRAqklLAQLKLDINPA-------TPVGNLG----LGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2662793383 493 IIVLDEPTIGLdpkTElSLIETMFSATEE-----KTVIWITHHLvgiehvDEV 540
Cdd:PRK13549 164 LLILDEPTASL---TE-SETAVLLDIIRDlkahgIACIYISHKL------NEV 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
357-505 |
7.79e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEV-LLNSEHAHTNLLSK----YIS---------------VLN 416
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwLFGQPVDAGDIATRrrvgYMSqafslygeltvrqnlELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 417 QKphLFDTTignnvrigkPEATDEEIWKALEKAQLASHIATLPDGLqtkmhemgkrfSGGERQRVAFARTLMQEAPIIVL 496
Cdd:NF033858 364 AR--LFHLP---------AAEIAARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLIL 421
|
....*....
gi 2662793383 497 DEPTIGLDP 505
Cdd:NF033858 422 DEPTSGVDP 430
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-504 |
9.25e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHTNLLSK-------YISVLNQKPHLfdtTIG 427
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivYISEDRKRDGL---VLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNVRIGKPEATDEEIWKALEKAQLASHIATLPDGLQT---KMHEMGKR---FSGGERQRVAFARTLMQEAPIIVLDEPTI 501
Cdd:PRK10762 345 MSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfniKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 2662793383 502 GLD 504
Cdd:PRK10762 425 GVD 427
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
321-530 |
9.97e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 EKELPRDKDYVAPKHIDIELNHVSYSYphSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGalsplhgevllns 400
Cdd:PRK10938 244 EPDEPSARHALPANEPRIVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 401 EH--AHTNLLS----------------KYISVLNQKPHLfDTTIGNNVR----------IGKPEA-TDEEIWKA---LEK 448
Cdd:PRK10938 309 DHpqGYSNDLTlfgrrrgsgetiwdikKHIGYVSSSLHL-DYRVSTSVRnvilsgffdsIGIYQAvSDRQQKLAqqwLDI 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 449 AQLASHIATLPdglqtkMHEMgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIGLDP---KTELSLIETMFSATEEKtVI 525
Cdd:PRK10938 388 LGIDKRTADAP------FHSL----SWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLISEGETQ-LL 456
|
....*
gi 2662793383 526 WITHH 530
Cdd:PRK10938 457 FVSHH 461
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
355-545 |
1.05e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 48.28 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGAL--SPLHGEVLLNSEHAHTNLLS----KYISVLNQKPHLF-DTTIG 427
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRdterAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNVRIGKpEAT--------DEEIWKA---LEKAQLASHIATLPDGlqtkmhemgkRFSGGERQRVAFARTLMQEAPIIVL 496
Cdd:TIGR02633 97 ENIFLGN-EITlpggrmayNAMYLRAknlLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 497 DEPTIGLDPKtELSLIETMFSATEEKTV--IWITHHLVGIEHVDEVIFLDR 545
Cdd:TIGR02633 166 DEPSSSLTEK-ETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTICVIR 215
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
474-557 |
1.24e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 474 SGGERQRVAFARTLMQEA---PIIVLDEPTIGL---DPKTELSLIETMFSATEekTVIWITHHLVGIEHVDEVIFL---- 543
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKLLEVLQRLVDKGN--TVVVIEHNLDVIKTADYIIDLgpeg 908
|
90
....*....|....*.
gi 2662793383 544 -DR-GKIVMQGSHEQL 557
Cdd:TIGR00630 909 gDGgGTVVASGTPEEV 924
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-568 |
1.37e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.91 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 358 VSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEHAHtNLLSKYISVLN-----QKPHLFD--TTIGN-- 428
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIARMGvvrtfQHVRLFRemTVIENll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 429 ---------NVRIG--KPEATDEEIWKALEKAqlashiATLPDglQTKMHEMGKRFSG----GERQRVAFARTLMQEAPI 493
Cdd:PRK11300 103 vaqhqqlktGLFSGllKTPAFRRAESEALDRA------ATWLE--RVGLLEHANRQAGnlayGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 494 IVLDEPTIGLDPKTELSLIETMFSATEEK--TVIWITH--HLV-GIEhvDEVIFLDRGKIVMQGSHEQlLKENEKYRKLY 568
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHdmKLVmGIS--DRIYVVNQGTPLANGTPEE-IRNNPDVIKAY 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
321-504 |
2.33e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 321 EKELPRDKDYVAPKHIDIELNHVSYSyPHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNS 400
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 401 EhahtnllskyiSVLNQKPHLF-------------------DTTIGNNV---RIGKPEATDEEI--WKALEKaqLASHIA 456
Cdd:COG3845 320 E-----------DITGLSPRERrrlgvayipedrlgrglvpDMSVAENLilgRYRRPPFSRGGFldRKAIRA--FAEELI 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2662793383 457 T----LPDGLQTKMhemgKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLD 504
Cdd:COG3845 387 EefdvRTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
22-309 |
2.45e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 46.32 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 22 LGLLGVSSGAMLLF--ISGYLIsKSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLYG--I 97
Cdd:cd18576 2 LILLLLSSAIGLVFplLAGQLI-DAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRhlQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 98 VEPQAlFFRSRfQTGDMLGVLSEDIEHLQNlylrtIFPSILALVVYSIFVLVIGtfdVVFALIAACMLATIV-FLLPFIS 176
Cdd:cd18576 81 RLPLS-FFHER-RVGELTSRLSNDVTQIQD-----TLTTTLAEFLRQILTLIGG---VVLLFFISWKLTLLMlATVPVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 177 LLLM---KKHHVTLKQGRNRLYQ---QLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVV 250
Cdd:cd18576 151 LVAVlfgRRIRKLSKKVQDELAEantIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 251 GIVVVSMIIWTGNEAASEQIAPTVIAAFVLMTLSVTNALIPLSDAIDRIPSYVESAHRL 309
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
350-504 |
2.54e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 350 SNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLnsEHAHTNLLskyisvlnQKPHLfdTTIGNN 429
Cdd:PRK13541 11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNI--------AKPYC--TYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 430 VRIgKPEATDEE-------IWKALEKAQLASHIATLPDGLQTKMHEMgkrfSGGERQRVAFARTLMQEAPIIVLDEPTIG 502
Cdd:PRK13541 79 LGL-KLEMTVFEnlkfwseIYNSAETLYAAIHYFKLHDLLDEKCYSL----SSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
..
gi 2662793383 503 LD 504
Cdd:PRK13541 154 LS 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
343-549 |
3.90e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 343 VSYSYPHSNefVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLL--------NSEHAHTNLLSKYISV 414
Cdd:PRK10982 4 ISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgkeidfkSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 415 LNQkphLFDTTIGNNVRIG----KPEATDEE--------IWKALE-KAQLASHIATLPDGlQTKMHEMGKRFSggerqrv 481
Cdd:PRK10982 82 LNL---VLQRSVMDNMWLGryptKGMFVDQDkmyrdtkaIFDELDiDIDPRAKVATLSVS-QMQMIEIAKAFS------- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 482 afartlmQEAPIIVLDEPTIGLDPKtELSLIETMFSATEEK--TVIWITHHLVGIEHV-DEVIFLDRGKIV 549
Cdd:PRK10982 151 -------YNAKIVIMDEPTSSLTEK-EVNHLFTIIRKLKERgcGIVYISHKMEEIFQLcDEITILRDGQWI 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
365-545 |
5.58e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.52 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 365 GKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSehahtnllskyisvlnqkphlfdttignnvrigkPEATDEEIWK 444
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID----------------------------------GEDILEEVLD 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 445 ALekaqlashiatlpdgLQTKMHEMGKRFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK-- 522
Cdd:smart00382 48 QL---------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlk 112
|
170 180
....*....|....*....|....*...
gi 2662793383 523 -----TVIWITHHLVGIEHVDEVIFLDR 545
Cdd:smart00382 113 seknlTVILTTNDEKDLGPALLRRRFDR 140
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
357-548 |
1.12e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.82 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 357 DVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLH-GEVLLNSEHAHTNLLSKYISV------LNQKPH--LFDTTIG 427
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDIRNPAQAIRAgiamvpEDRKRHgiVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 428 NNV---------RIGKPEATDEE--IWKALEKAQLASHIATLPDGlqtkmhemgkRFSGGERQRVAFARTLMQEAPIIVL 496
Cdd:TIGR02633 358 KNItlsvlksfcFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 497 DEPTIGLDPKTELSLIETMFS-ATEEKTVIWITHHLVGIEHV-DEVIFLDRGKI 548
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-279 |
3.56e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 42.88 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 18 VTIFLGLLGVSSGAMLL--FISGYLISK--SALRPENVMAVYVPIV----ATRAFSIG-QAVFHYVERLVGhdvvLRILE 88
Cdd:cd18563 1 LILGFLLMLLGTALGLVppYLTKILIDDvlIQLGPGGNTSLLLLLVlglaGAYVLSALlGILRGRLLARLG----ERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 89 KMRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNlYLRTIFPSILalvvySIFVLVIGTFDVVFALIAacMLATI 168
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQD-FLSDGLPDFL-----TNILMIIGIGVVLFSLNW--KLALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 169 VFL-LPFI---SLLLMKK-HHVTLKQGR--NRLYQQLTDAVFGLSDWQASGRKDEFIDKYVEQNAQLLKTEKRMKRWNHI 241
Cdd:cd18563 149 VLIpVPLVvwgSYFFWKKiRRLFHRQWRrwSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2662793383 242 RDSIIQLVVGIVVVsmIIWT--GNEAASEQIAPTVIAAFV 279
Cdd:cd18563 229 FFPLLTFLTSLGTL--IVWYfgGRQVLSGTMTLGTLVAFL 266
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
474-540 |
4.28e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2662793383 474 SGGERQRVAFARTLMQEAP---IIVLDEPTIGLDPKTELSLIETMFSATEE-KTVIWITH--HLVGI-EHVDEV 540
Cdd:PRK00635 811 SGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQgHTVVIIEHnmHVVKVaDYVLEL 884
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
474-559 |
4.66e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 474 SGGERQRVAFARTLMQEAPII--VLDEPTIGLDPKTELSLIETMFSATEEKTVIWIthhlvgIEHVDEVI-FLDR----- 545
Cdd:PRK00635 478 SGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLL------VEHDEQMIsLADRiidig 551
|
90 100
....*....|....*....|.
gi 2662793383 546 -------GKIVMQGSHEQLLK 559
Cdd:PRK00635 552 pgagifgGEVLFNGSPREFLA 572
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
16-171 |
5.46e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 42.08 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 16 MTVTIFLGLLGVSSGAMLLFISGYLISkSALRPENVMAVYVPIVATRAFSIGQAVFHYVERLVGHDVVLRILEKMRTKLY 95
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAID-GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2662793383 96 GIVEPQALFFRSRFQTGDMLGVLSEDIEHLQNL--YLRTIFPSILALVVYSIFVLVIgtfDVVFALIAACMLATIVFL 171
Cdd:cd18543 80 AHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFlaFGPFLLGNLLTLVVGLVVMLVL---SPPLALVALASLPPLVLV 154
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-529 |
6.48e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 6.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 474 SGGERQRVA----FARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFSATEEK-TVIWITH 529
Cdd:cd03227 79 SGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITH 139
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
355-549 |
8.14e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 355 LKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGaLSPlH----GEVLLNSEHAHTNLLS----KYISVLNQK----PHLf 422
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYP-HgsyeGEILFDGEVCRFKDIRdseaLGIVIIHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 423 dtTIGNNVRIGKPEATDEEI-W-KALEKAQLASHIATLPDGLQTKMHEMGKrfsgGERQRVAFARTLMQEAPIIVLDEPT 500
Cdd:NF040905 94 --SIAENIFLGNERAKRGVIdWnETNRRARELLAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2662793383 501 IGLDPKTELSLIETMFSATEEK-TVIWITHHLVGIEHV-DEVIFLDRGKIV 549
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRVaDSITVLRDGRTI 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
472-560 |
2.34e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 472 RFSGGERQRVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS--ATEEKTVIWITHHLVGI-EHVDEVIFLDRGKI 548
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
90
....*....|..
gi 2662793383 549 VMQGSHEQLLKE 560
Cdd:PRK11022 233 VETGKAHDIFRA 244
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
459-521 |
2.72e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2662793383 459 PDGLQTKMHEMGKRFSGGERQRVAF------ARTLMQEAP-------IIVLDEPTIGLDPKTelslIETMFSATEE 521
Cdd:pfam13558 19 EDGSEVETYRRSGGLSGGEKQLLAYlplaaaLAAQYGSAEgrppaprLVFLDEAFAKLDEEN----IRTALELLRA 90
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
333-564 |
5.09e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 333 PKHIDIELNHVSysypHSNEFVLKDVSLQIKAGKKIAILGRSGTGKSTLLKLLTGALSPLHGEVLLNSEH-----AHTNL 407
Cdd:PRK10982 246 PGEVILEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnANEAI 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 408 LSKYISVLNQKPhlfDTTIGNNVRIG-----KPEATDEEIWKALEKAQLASHIATLPDGLQTKM---HEMGKRFSGGERQ 479
Cdd:PRK10982 322 NHGFALVTEERR---STGIYAYLDIGfnsliSNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTpghRTQIGSLSGGNQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 480 RVAFARTLMQEAPIIVLDEPTIGLDPKTELSLIETMFS-ATEEKTVIWITH---HLVGIehVDEVIFLDRGKIV-----M 550
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSempELLGI--TDRILVMSNGLVAgivdtK 476
|
250
....*....|....
gi 2662793383 551 QGSHEQLLKENEKY 564
Cdd:PRK10982 477 TTTQNEILRLASLH 490
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
367-390 |
5.82e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 5.82e-03
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
368-531 |
9.31e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 368 IAILGRSGTGKSTLLKLLTGAL-SPLHGEVLLNSEHAHTNLLSKYISVlnqkphLFdTTIGNNVRIGKP--------EAT 438
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYALyGKARSRSKLRSDLINVGSEEASVEL------EF-EHGGKRYRIERRqgefaeflEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 439 DEEIWKALEK-------AQLASHIATLPDGLQTKMHEMG-------------------KRFSGGERQRVAFARTLMqeap 492
Cdd:COG0419 99 PSERKEALKRllgleiyEELKERLKELEEALESALEELAelqklkqeilaqlsgldpiETLSGGERLRLALADLLS---- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2662793383 493 iIVLDepTIGLDPKTELSLIETMFSATEektviwITHHL 531
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEELAI------ITHVI 204
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
63-280 |
9.41e-03 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 38.16 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 63 AFSIGQAVFHYVER--LVGhdvVLRILEK-MRTKLYGIVEPQALFFRSRFQTGDMLGVLSEDIEHLQnlylRTIFPSILA 139
Cdd:cd18541 48 LLALLIGIFRFLWRylIFG---ASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVR----MALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2662793383 140 LV---VYSIFVLVI-GTFDVVFALIAACMLATIVFLLPFISLLLMKKHHVTLKQgrnrlYQQLTDAV---F-GLSDWQAS 211
Cdd:cd18541 121 LVdalFLGVLVLVMmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEA-----FSDLSDRVqesFsGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2662793383 212 GRKDEFIDKYVEQNAQLLKTEKRMKRWNHIRDSIIQLVVGIVVVSMIIWTGNEAASEQIAPTVIAAFVL 280
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNS 264
|
|
| |
