|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-578 |
4.23e-132 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 398.00 E-value: 4.23e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 21 RAARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTII 100
Cdd:COG1132 14 RYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 101 TRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVL 180
Cdd:COG1132 94 ADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 181 YGLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTLVVRLLA 260
Cdd:COG1132 174 LLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 261 GEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDK--PAVSERY 338
Cdd:COG1132 254 LGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIpdPPGAVPL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 339 QRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMTSGH 408
Cdd:COG1132 334 PPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdlTLESLR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 409 ARTVLISQEIHTFSGTLFDDVALGlagqAEDWPDERVRdavlAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQV 487
Cdd:COG1132 414 RQIGVVPQDTFLFSGTIRENIRYG----RPDATDEEVE----EAAKAAQAhEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 488 ALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
570
....*....|.
gi 488473579 568 GPFAALWRVWS 578
Cdd:COG1132 566 GLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-575 |
5.61e-92 |
|
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: 297.52 E-value: 5.61e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 21 RAARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTII 100
Cdd:COG2274 149 RLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 101 TRLRESMIAVGLGLDQQRVEKAGTADLVSRASDdVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVL 180
Cdd:COG2274 229 LRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 181 YGLAIrefLRTAPPVYRAERNASTTQSQR---ILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTLVVR 257
Cdd:COG2274 308 YVLLG---LLFQPRLRRLSREESEASAKRqslLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 258 LLAGEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVSER 337
Cdd:COG2274 385 SGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSK 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 338 YQRGPT--SIHVDQVSFGY-QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------M 404
Cdd:COG2274 465 LSLPRLkgDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 405 TSGHARTVLISQEIHTFSGTLFDDVALGlagqAEDWPDERVRdavlAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQ 483
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLG----DPDATDEEII----EAARLAGLhDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 484 AQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV--------RGRTALVVAHRLSQVTMADEVAVMDNGRIV 555
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATS--------ALDAETEAIIlenlrrllKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
570 580
....*....|....*....|
gi 488473579 556 EVGAPEQLRQSDGPFAALWR 575
Cdd:COG2274 689 EDGTHEELLARKGLYAELVQ 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
13-568 |
5.48e-71 |
|
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: 238.12 E-value: 5.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 13 AQVRQEVHRAARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAA-KAHRPTSALLTPALVMAAAVIGSGICNGAAQSL 91
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLiIGGAPLSALLPLLGLLLAVLLLRALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 92 TPSFFTTIITRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP--- 168
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWlsg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 169 ---LFFVPVL-LAGVLYGLAIREflrtappvyRAERNASTTQ--SQRILSTIHGVDVVRAFGLENLRTRAVANGSWQair 242
Cdd:COG4988 162 lilLVTAPLIpLFMILVGKGAAK---------ASRRQWRALArlSGHFLDRLRGLTTLKLFGRAKAEAERIAEASED--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 243 wnLRGRFLGnTLVVRLLAG---EAVATIGVAWTGYLLVTtdRLSVG--AAATAVLVLL---RLFSPVRFLLMF----LNN 310
Cdd:COG4988 230 --FRKRTMK-VLRVAFLSSavlEFFASLSIALVAVYIGF--RLLGGslTLFAALFVLLlapEFFLPLRDLGSFyharANG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 311 LQAAwvclQRVVGVIQARHDKPAVSER--YQRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLA 388
Cdd:COG4988 305 IAAA----EKIFALLDAPEPAAPAGTAplPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 389 ALVAGLLEPRQGSIT----------MTSGHARTVLISQEIHTFSGTLFDDVALGlAGQAEDwpdervrDAVLAALERVGA 458
Cdd:COG4988 381 NLLLGFLPPYSGSILingvdlsdldPASWRRQIAWVPQNPYLFAGTIRENLRLG-RPDASD-------EELEAALEAAGL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 459 -DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV--------RGRT 529
Cdd:COG4988 453 dEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA--------HLDAETEAEIlqalrrlaKGRT 524
|
570 580 590
....*....|....*....|....*....|....*....
gi 488473579 530 ALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:COG4988 525 VILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-575 |
1.32e-68 |
|
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: 231.96 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 20 HRAARGVRGYFIGAIVVITAASLLDLTvpvatGWIIDAAKAHRPTSALLTPAlvmaAAVIGSGICNGA---AQSLTpSFF 96
Cdd:COG4987 12 PHRGRLLLGVLLGLLTLLAGIGLLALS-----GWLIAAAALAPPILNLFVPI----VGVRAFAIGRTVfryLERLV-SHD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 97 TT--IITRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDA-ANGALPrLVNTMIMVIVSVGALASLHPLF--- 170
Cdd:COG4987 82 ATlrLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLyLRVLLP-LLVALLVILAAVAFLAFFSPALalv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 171 -FVPVLLAGVLYGLAireFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAV--ANGSWQAIRWNLRG 247
Cdd:COG4987 161 lALGLLLAGLLLPLL---AARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLdaAEARLAAAQRRLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 248 RFLGNTLVVRLLAGeaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQA 327
Cdd:COG4987 238 LSALAQALLQLAAG--LAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 328 rhdKPAVSERYQ----RGPTSIHVDQVSFGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI 402
Cdd:COG4987 316 ---PPAVTEPAEpapaPGGPSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 403 TM----------TSGHARTVLISQEIHTFSGTLFDDVALGlAGQAEDwpdervrDAVLAALERVG-ADWVEQLPHGVDTV 471
Cdd:COG4987 393 TLggvdlrdldeDDLRRRIAVVPQRPHLFDTTLRENLRLA-RPDATD-------EELWAALERVGlGDWLAALPDGLDTW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 472 VGRLGIRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV--------RGRTALVVAHRLSQVTMA 543
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTE--------GLDAATEQALladllealAGRTVLLITHRLAGLERM 536
|
570 580 590
....*....|....*....|....*....|..
gi 488473579 544 DEVAVMDNGRIVEVGAPEQLRQSDGPFAALWR 575
Cdd:COG4987 537 DRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-576 |
3.85e-62 |
|
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: 214.97 E-value: 3.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 23 ARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITR 102
Cdd:TIGR02203 9 VRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 103 LRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLH-PLFFVPVLLAGVLy 181
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSwQLTLIVVVMLPVL- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 182 GLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLG--NTLVVRLL 259
Cdd:TIGR02203 168 SILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGsiSSPITQLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 260 AGEAVATIgVAWTGYLLVTtDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVSERYQ 339
Cdd:TIGR02203 248 ASLALAVV-LFIALFQAQA-GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 340 RGPTSIHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMTSGH 408
Cdd:TIGR02203 326 RARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladyTLASLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 409 ARTVLISQEIHTFSGTLFDDVALGLAGQAedwPDERVRDAVLAALERvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVA 488
Cdd:TIGR02203 406 RQVALVSQDVVLFNDTIANNIAYGRTEQA---DRAEIERALAAAYAQ---DFVDKLPLGLDTPIGENGVLLSGGQRQRLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 489 LARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNG 559
|
....*...
gi 488473579 569 PFAALWRV 576
Cdd:TIGR02203 560 LYAQLHNM 567
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-574 |
2.46e-59 |
|
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: 197.45 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV----------L 413
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtlaslrrqigL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSGTLFDDVALGlagqAEDWPDERVRDAVLAALERvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARAL 493
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYG----RPGATREEVEEAARAANAH---EFIMELPEGYDTVIGERGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 494 LADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAAL 573
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
.
gi 488473579 574 W 574
Cdd:cd03251 234 H 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
345-568 |
3.59e-55 |
|
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: 186.28 E-value: 3.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV----------LI 414
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIsrkslrsmigVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSGTLFDDVALGlagqAEDWPDERVrdavLAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARAL 493
Cdd:cd03254 83 LQDTFLFSGTIMENIRLG----RPNATDEEV----IEAAKEAGAhDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 494 LADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
345-575 |
1.33e-52 |
|
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: 179.73 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMTSGHARTVLI 414
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSGTLFDDVALGlagqAEDWPDERVRDAVLAAleRVgADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALL 494
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYG----RPDATDEEVIEAAKAA--QI-HDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAALW 574
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
.
gi 488473579 575 R 575
Cdd:cd03253 234 K 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
345-575 |
6.95e-52 |
|
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: 177.73 E-value: 6.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD--VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV---------- 412
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLnlrwlrsqig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSGTLFDDVALGlagqAEDWPDERVRDAVLAALervGADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARA 492
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG----KPDATDEEVEEAAKKAN---IHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 493 LLADPPVIILDEATaeagssgaTALD--------RAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLR 564
Cdd:cd03249 154 LLRNPKILLLDEAT--------SALDaeseklvqEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
250
....*....|.
gi 488473579 565 QSDGPFAALWR 575
Cdd:cd03249 226 AQKGVYAKLVK 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
263-575 |
6.94e-50 |
|
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: 181.94 E-value: 6.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 263 AVATIGVAWTGYLLVTTDRLSVGAAataVLV---LLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQAR---HDKP-AVS 335
Cdd:COG5265 274 ALGLTAMMLMAAQGVVAGTMTVGDF---VLVnayLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPpevADAPdAPP 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 336 ERYQRGptSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMT 405
Cdd:COG5265 351 LVVGGG--EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdirdvTQA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 406 SGHARTVLISQEIHTFSGTLFDDVALGlagqAEDWPDERVRDAV-LAALErvgaDWVEQLPHGVDTVVGRLGIRLSPAQA 484
Cdd:COG5265 429 SLRAAIGIVPQDTVLFNDTIAYNIAYG----RPDASEEEVEAAArAAQIH----DFIESLPDGYDTRVGERGLKLSGGEK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 485 QQVALARALLADPPVIILDEATAeagssgatALD--------RAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVE 556
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATS--------ALDsrteraiqAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
330
....*....|....*....
gi 488473579 557 VGAPEQLRQSDGPFAALWR 575
Cdd:COG5265 573 RGTHAELLAQGGLYAQMWA 591
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
345-576 |
5.78e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 176.36 E-value: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQ--DGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMTSGHARTV 412
Cdd:PRK11176 342 IEFRNVTFTYPgkEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEIlldghdlrdyTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSgtlfDDVALGLAGQAEDwpdERVRDAVLAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:PRK11176 421 LVSQNVHLFN----DTIANNIAYARTE---QYSREQIEEAARMAYAmDFINKMDNGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFA 571
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
....*
gi 488473579 572 ALWRV 576
Cdd:PRK11176 574 QLHKM 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-573 |
1.22e-46 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 174.53 E-value: 1.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 29 YFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMI 108
Cdd:TIGR00958 162 WLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 109 AVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVP-VLLAGVLY 181
Cdd:TIGR00958 242 RSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrltmvtLINLPlVFLAEKVF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 182 GLAIREFLRTAppvyraeRNASTTQSQRILSTIHGVDVVRAFGLENL----------------RTRAVANGSWQAIRwnl 245
Cdd:TIGR00958 322 GKRYQLLSEEL-------QEAVAKANQVAEEALSGMRTVRSFAAEEGeasrfkealeetlqlnKRKALAYAGYLWTT--- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 246 rgRFLGNTLVVrllageavatiGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVI 325
Cdd:TIGR00958 392 --SVLGMLIQV-----------LVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 326 QARHD-KPAVSERYQRGPTSIHVDQVSFGYQDGPD--VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI 402
Cdd:TIGR00958 459 DRKPNiPLTGTLAPLNLEGLIEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 403 TMT----------SGHARTVLISQEIHTFSGTLFDDVALGLagqaEDWPDERVRDAVLAAlervGA-DWVEQLPHGVDTV 471
Cdd:TIGR00958 539 LLDgvplvqydhhYLHRQVALVGQEPVLFSGSVRENIAYGL----TDTPDEEIMAAAKAA----NAhDFIMEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 472 VGRLGIRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALDRAAAEAVR------GRTALVVAHRLSQVTMADE 545
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT--------SALDAECEQLLQesrsraSRTVLLIAHRLSTVERADQ 682
|
570 580
....*....|....*....|....*...
gi 488473579 546 VAVMDNGRIVEVGAPEQLRQSDGPFAAL 573
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
27-537 |
1.56e-46 |
|
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: 171.39 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 27 RGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRES 106
Cdd:TIGR02868 12 RRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGALRVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 107 MIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFfVPVLLAGVLYGLAI- 185
Cdd:TIGR02868 92 VYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA-ALILAAGLLLAGFVa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 186 -REFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAV--ANGSWQAIRwNLRGRFLGNTLVVRLLAGe 262
Cdd:TIGR02868 171 pLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVeeADRELTRAE-RRAAAATALGAALTLLAA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 263 AVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVS----ERY 338
Cdd:TIGR02868 249 GLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSapaaGAV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 339 QRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGH---------- 408
Cdd:TIGR02868 329 GLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPvssldqdevr 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 409 ARTVLISQEIHTFSGTLFDDVALGlagqAEDWPDErvrdAVLAALERVG-ADWVEQLPHGVDTVVGRLGIRLSPAQAQQV 487
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLRLA----RPDATDE----ELWAALERVGlADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488473579 488 ALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRL 537
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
345-553 |
1.64e-43 |
|
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: 152.92 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MTSGHARTVL 413
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidgvdlrdldLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSGTLFDDValglagqaedwpdervrdavlaalervgadwveqlphgvdtvvgrlgirLSPAQAQQVALARAL 493
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 494 LADPPVIILDEATAeagssgatALDRAAAEAV--------RGRTALVVAHRLSQVTMADEVAVMDNGR 553
Cdd:cd03228 112 LRDPPILILDEATS--------ALDPETEALIlealralaKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-573 |
8.00e-42 |
|
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: 150.71 E-value: 8.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGH-----------ARTV 412
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHdlaladpawlrRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSGTLFDDVALGLAGQaedwPDERVRDAVLAAlervGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGM----SMERVIEAAKLA----GAhDFISELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFA 571
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
..
gi 488473579 572 AL 573
Cdd:cd03252 232 YL 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
344-555 |
8.08e-42 |
|
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: 150.05 E-value: 8.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV---------- 412
Cdd:cd03245 2 RIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLdpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSGTLFDDVALGlAGQAEDwpdervrDAVLAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLG-APLADD-------ERILRAAELAGVtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIV 555
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-562 |
1.85e-41 |
|
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: 157.60 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 10 ATAAQVRQEVHRAARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGIcngaaq 89
Cdd:COG4618 2 SRASAGRSELRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 90 sltpsfFTTIITRLresMIAVGLGLDQQ---RV-EKAGTADLVSRASDDVTAVRD-------AANGALPRLVNTMIMVIV 158
Cdd:COG4618 76 ------LDAVRSRI---LVRVGARLDRRlgpRVfDAAFRAALRGGGGAAAQALRDldtlrqfLTGPGLFALFDLPWAPIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 159 sVGALASLHPLF-FVPVLLAGVLYGLAIREFLRTAPPVYRAERnASTTQSQRILSTIHGVDVVRAFG-LENLRTR---AV 233
Cdd:COG4618 147 -LAVLFLFHPLLgLLALVGALVLVALALLNERLTRKPLKEANE-AAIRANAFAEAALRNAEVIEAMGmLPALRRRwqrAN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 234 ANGSWQAIRWNLRGRFLGN-TLVVRLLAGeaVATIGVawtGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQ 312
Cdd:COG4618 225 ARALALQARASDRAGGFSAlSKFLRLLLQ--SAVLGL---GAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 313 AAWVCLQRVVGVIQARHDKPAvSERYQRGPTSIHVDQVSFGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALV 391
Cdd:COG4618 300 SARQAYRRLNELLAAVPAEPE-RMPLPRPKGRLSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 392 AGLLEPRQGSITM----TSGHARTVL------ISQEIHTFSGTLFDDVALglAGQAEDwpdervrDAVLAALERVGA-DW 460
Cdd:COG4618 379 VGVWPPTAGSVRLdgadLSQWDREELgrhigyLPQDVELFDGTIAENIAR--FGDADP-------EKVVAAAKLAGVhEM 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 461 VEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEA-VRGRTALVVAHRLSQ 539
Cdd:COG4618 450 ILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSL 529
|
570 580
....*....|....*....|...
gi 488473579 540 VTMADEVAVMDNGRIVEVGAPEQ 562
Cdd:COG4618 530 LAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-549 |
1.89e-40 |
|
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: 154.37 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVpvaTGWIIDAAkahrPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:TIGR02857 13 VLGALLIIAQAWLLARVV---DGLISAGE----PLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFL 189
Cdd:TIGR02857 86 AVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 190 RTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVAngswqAIRWNLRGRFLGnTLVVRLLAG---EAVAT 266
Cdd:TIGR02857 166 WAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIR-----RSSEEYRERTMR-VLRIAFLSSavlELFAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 267 IGVAWTG-YLLVttdRLSVG--AAATAVLVLL---RLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVSERYQR 340
Cdd:TIGR02857 240 LSVALVAvYIGF---RLLAGdlDLATGLFVLLlapEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 341 GP-TSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----------TMTSGHA 409
Cdd:TIGR02857 317 APaSSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladaDADSWRD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 410 RTVLISQEIHTFSGTLFDDVALGLAGQAEdwpdervrDAVLAALERVGAD-WVEQLPHGVDTVVGRLGIRLSPAQAQQVA 488
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIRLARPDASD--------AEIREALERAGLDeFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 489 LARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVM 549
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
345-563 |
6.71e-40 |
|
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: 145.17 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHT---- 420
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKDITKKNLRELRRkvgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 ---------FSGTLFDDVALGLAGQAedWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:COG1122 80 vfqnpddqlFAPTVEEDVAFGPENLG--LPREEIRERVEEALELVGlEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAP 560
Cdd:COG1122 147 GVLAMEPEVLVLDEPTA--------GLDPRGRRELlellkrlnkEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTP 218
|
...
gi 488473579 561 EQL 563
Cdd:COG1122 219 REV 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
344-568 |
1.28e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 152.95 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM------TSGHA----RTVL 413
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrplsSLSHSvlrqGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSGTLFDDVALGlagqaedwpDERVRDAVLAALERVG-ADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARA 492
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLG---------RDISEEQVWQALETVQlAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473579 493 LLADPPVIILDEATAEAGSSGATALDRAAAeAVRGRTALVV-AHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
364-573 |
2.16e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 151.92 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLePRQGSIT----------MTSGHARTVLISQEIHTFSGTLFDDVALGl 433
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKingielreldPESWRKHLSWVGQNPQLPHGTLRDNVLLG- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 434 agqAEDWPDERVRdavlAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSS 512
Cdd:PRK11174 447 ---NPDASDEQLQ----QALENAWVsEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 513 GATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAAL 573
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
344-560 |
4.66e-39 |
|
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: 142.63 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGY-QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM----TSGHARTVL----- 413
Cdd:cd03244 2 DIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdgvdISKIGLHDLrsris 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 -ISQEIHTFSGTLFDDvaLGLAGQAEDwpdervrDAVLAALERVG-ADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:cd03244 82 iIPQDPVLFSGTIRSN--LDPFGEYSD-------EELWQALERVGlKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAP 560
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
325-575 |
8.94e-38 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 147.41 E-value: 8.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 325 IQARHDKPAVSErYQRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM 404
Cdd:PRK13657 316 VPDVRDPPGAID-LGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 405 TSGHARTVLIS----------QEIHTFSGTLFDDVALGlagqAEDWPDERVRDAvlaaLERVGA-DWVEQLPHGVDTVVG 473
Cdd:PRK13657 395 DGTDIRTVTRAslrrniavvfQDAGLFNRSIEDNIRVG----RPDATDEEMRAA----AERAQAhDFIERKPDGYDTVVG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 474 RLGIRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALD-------RAAAEAVR-GRTALVVAHRLSQVTMADE 545
Cdd:PRK13657 467 ERGRQLSGGERQRLAIARALLKDPPILILDEAT--------SALDveteakvKAALDELMkGRTTFIIAHRLSTVRNADR 538
|
250 260 270
....*....|....*....|....*....|
gi 488473579 546 VAVMDNGRIVEVGAPEQLRQSDGPFAALWR 575
Cdd:PRK13657 539 ILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
350-554 |
1.08e-37 |
|
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: 139.14 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDGPD--VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG----------HARTVLISQE 417
Cdd:cd03248 17 VTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 IHTFSGTLFDDVALGLAGQaedwPDERVRDAVLAAlervGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLAD 496
Cdd:cd03248 97 PVLFARSLQDNIAYGLQSC----SFECVKEAAQKA----HAhSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 497 PPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRI 554
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
324-563 |
8.41e-36 |
|
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: 140.81 E-value: 8.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 324 VIQARHDKPAVSERYQRGPTSIHVDQVSFGYQDGPD----VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQ 399
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTS 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 400 GSITMtSGHARTVLISQEIHTFSG-----------------TLFDDVALGLAgQAEDWPDERVRDAVLAALERVG--ADW 460
Cdd:COG1123 320 GSILF-DGKDLTKLSRRSLRELRRrvqmvfqdpysslnprmTVGDIIAEPLR-LHGLLSRAERRERVAELLERVGlpPDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 461 VEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTA 530
Cdd:COG1123 398 ADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTS--------ALDVSVQAQIlnllrdlqreLGLTY 458
|
250 260 270
....*....|....*....|....*....|....
gi 488473579 531 LVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG1123 459 LFISHDLAVVrYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
345-570 |
1.48e-35 |
|
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: 133.40 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTF--- 421
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 422 ------SGTLFDD------VALGLAgQAEDWPDERVRDAVLAALERVGadwveqLPHGVDtvvgRLGIRLSPAQAQQVAL 489
Cdd:cd03261 79 mgmlfqSGALFDSltvfenVAFPLR-EHTRLSEEEIREIVLEKLEAVG------LRGAED----LYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 490 ARALLADPPVIILDEATAEagssgataLDRAAAEAV----------RGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03261 148 ARALALDPELLLYDEPTAG--------LDPIASGVIddlirslkkeLGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEG 219
|
250
....*....|..
gi 488473579 559 APEQLRQSDGPF 570
Cdd:cd03261 220 TPEELRASDDPL 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
347-553 |
9.89e-34 |
|
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: 127.58 E-value: 9.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYQDG-PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTFSGTL 425
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 F-------------DDVALGLAGQAedWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALAR 491
Cdd:cd03225 81 FqnpddqffgptveEEVAFGLENLG--LPEEEIEERVEEALELVGlEGLRDRSPF-----------TLSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 492 ALLADPPVIILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGR 553
Cdd:cd03225 148 VLAMDPDILLLDEPTA--------GLDPAGRRELlellkklkaEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
345-570 |
4.19e-33 |
|
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: 126.63 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTF--- 421
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DGQDITGLSEKELYELrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 422 ------SGTLFDD------VALGLAgQAEDWPDERVRDAVLAALERVGadwveqLPHGVDtvvgrlgirLSPAQ-----A 484
Cdd:COG1127 84 igmlfqGGALFDSltvfenVAFPLR-EHTDLSEAEIRELVLEKLELVG------LPGAAD---------KMPSElsggmR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 485 QQVALARALLADPPVIILDEATaeAGssgataLDRAAAEAV----------RGRTALVVAHRLSQV-TMADEVAVMDNGR 553
Cdd:COG1127 148 KRVALARALALDPEILLYDEPT--AG------LDPITSAVIdelirelrdeLGLTSVVVTHDLDSAfAIADRVAVLADGK 219
|
250
....*....|....*..
gi 488473579 554 IVEVGAPEQLRQSDGPF 570
Cdd:COG1127 220 IIAEGTPEELLASDDPW 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-566 |
9.01e-33 |
|
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: 126.07 E-value: 9.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD---VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM---------TSGHARTV 412
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 -LISQE----IHTFsGTLFDDVALGLAGQAEDWPDERVRdavlAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQ 485
Cdd:COG1124 82 qMVFQDpyasLHPR-HTVDRILAEPLRIHGLPDREERIA----ELLEQVGlpPSFLDRYPH-----------QLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 486 QVALARALLADPPVIILDEATaeagssgaTALD------------RAAAEavRGRTALVVAHRLSQVT-MADEVAVMDNG 552
Cdd:COG1124 146 RVAIARALILEPELLLLDEPT--------SALDvsvqaeilnllkDLREE--RGLTYLFVSHDLAVVAhLCDRVAVMQNG 215
|
250
....*....|....
gi 488473579 553 RIVEVGAPEQLRQS 566
Cdd:COG1124 216 RIVEELTVADLLAG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-575 |
1.45e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 131.87 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGH-----------ART 411
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL-NGQpiadyseaalrQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 412 VLISQEIHTFSGTLFDDVALGLAgQAEDwpdervrDAVLAALERVGADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNLLLAAP-NASD-------EALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAeagssgatALDRAA--------AEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK11160 489 ALLHDAPLLLLDEPTE--------GLDAETerqilellAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
250
....*....|..
gi 488473579 564 RQSDGPFAALWR 575
Cdd:PRK11160 561 LAQQGRYYQLKQ 572
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
345-558 |
1.22e-31 |
|
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: 120.50 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV---------LI 414
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLekalsslisVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSGTLFDDvalglagqaedwpdervrdavlaalervgadwveqlphgvdtvvgrLGIRLSPAQAQQVALARALL 494
Cdd:cd03247 81 NQRPYLFDTTLRNN----------------------------------------------LGRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 495 ADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVG 558
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
350-558 |
4.08e-31 |
|
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: 120.69 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT------------MTSGHARTV-LIS 415
Cdd:cd03257 9 VSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdllklsrrLRKIRRKEIqMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHT---FSGTLFDDVALGLAGQAEDWPDERVRDAVLAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:cd03257 89 QDPMSslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpEEVLNRYPH-----------ELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 491 RALLADPPVIILDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03257 158 RALALNPKLLIADEPT--------SALDVSVQAQIldllkklqeeLGLTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
345-563 |
4.94e-31 |
|
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: 121.30 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT--------MTSGH-ARTV-LI 414
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlasLSRRElARRIaYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHT-FSGTLFDDVALGLAGQAEDW--PDERVRDAVLAALERVG-ADWVEQLphgVDTvvgrlgirLSPAQAQQVALA 490
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYPHLGLFgrPSAEDREAVEEALERTGlEHLADRP---VDE--------LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATaeagssgaTALD------------RAAAEavRGRTALVVAHRLSQVTM-ADEVAVMDNGRIVEV 557
Cdd:COG1120 150 RALAQEPPLLLLDEPT--------SHLDlahqlevlellrRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQ 219
|
....*.
gi 488473579 558 GAPEQL 563
Cdd:COG1120 220 GPPEEV 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
361-507 |
9.27e-31 |
|
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: 117.36 E-value: 9.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MTSGHARTVLISQEIHTFSG-TLFDDV 429
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltddeRKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 430 ALGLAGQAedWPDERVRDAVLAALERVGadwveqLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATA 507
Cdd:pfam00005 81 RLGLLLKG--LSKREKDARAEEALEKLG------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
345-567 |
1.25e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVL-----ISQEIH 419
Cdd:COG1121 7 IELENLTVSYGGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 420 ---TFSGTLFDDVALGLAGQ--AEDWPDERVRDAVLAALERVG-ADWVEQlphgvdtvvgRLGiRLSPAQAQQVALARAL 493
Cdd:COG1121 86 vdwDFPITVRDVVLMGRYGRrgLFRRPSRADREAVDEALERVGlEDLADR----------PIG-ELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 494 LADPPVIILDEATaeagssgaTALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMdNGRIVEVGAPEQL 563
Cdd:COG1121 155 AQDPDLLLLDEPF--------AGVDAATEEALyellrelrrEGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEV 225
|
....
gi 488473579 564 RQSD 567
Cdd:COG1121 226 LTPE 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
345-557 |
4.05e-30 |
|
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: 117.57 E-value: 4.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-----TSGHARTVLISQ 416
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFS-GTLFDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALL 494
Cdd:cd03293 81 QDALLPwLTVLDNVALGL--ELQGVPKAEARERAEELLELVGlSGFENAYPH-----------QLSGGMRQRVALARALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 495 ADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQ-VTMADEVAVMDN--GRIVEV 557
Cdd:cd03293 148 VDPDVLLLDEPFS--------ALDALTREQLQeelldiwretGKTVLLVTHDIDEaVFLADRVVVLSArpGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
342-563 |
6.87e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.59 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 342 PTSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTV-L 413
Cdd:COG3842 3 MPALELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgrdvTGLPPEKRNVgM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQeihtfSGTLF------DDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQ 486
Cdd:COG3842 82 VFQ-----DYALFphltvaENVAFGL--RMRGVPKAEIRARVAELLELVGlEGLADRYPH-----------QLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHrlSQ---VTMADEVAVMDNGR 553
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLS--------ALDAKLREEMReelrrlqrelGITFIYVTH--DQeeaLALADRIAVMNDGR 213
|
250
....*....|
gi 488473579 554 IVEVGAPEQL 563
Cdd:COG3842 214 IEQVGTPEEI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
345-563 |
1.09e-29 |
|
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: 116.90 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGpDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLE-----PRQGSI------------TMTSG 407
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVlldgkdiydldvDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 408 HARTVLISQEIHTFSGTLFDDVALGLAGQAEdWPDERVRDAVLAALERVGADwveqlphgvDTVVGRLGIR-LSPAQAQQ 486
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRLHGI-KLKEELDERVEEALRKAALW---------DEVKDRLHALgLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATAeagssgatALDRAAAEAV--------RGRTALVVAHRLSQVT-MADEVAVMDNGRIVEV 557
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTS--------ALDPISTAKIeeliaelkKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEF 221
|
....*.
gi 488473579 558 GAPEQL 563
Cdd:cd03260 222 GPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-563 |
1.16e-29 |
|
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: 122.70 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLL---------------EPRQGSITMTSGH 408
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggrisgevlldgrDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 409 ARTVLISQEIHTFSGTLFDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQV 487
Cdd:COG1123 85 IGMVFQDPMTQLNPVTVGDQIAEAL--ENLGLSRAEARARVLELLEAVGlERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 488 ALARALLADPPVIILDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQV-TMADEVAVMDNGRIVE 556
Cdd:COG1123 152 AIAMALALDPDLLIADEPT--------TALDVTTQAEIldllrelqreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVE 223
|
....*..
gi 488473579 557 VGAPEQL 563
Cdd:COG1123 224 DGPPEEI 230
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
30-321 |
1.54e-29 |
|
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: 118.04 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFL 189
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 190 RTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTL--VVRLLAGeaVATI 267
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFspLIGLLTA--LGTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488473579 268 GVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd07346 239 LVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
124-575 |
4.16e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 121.74 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 124 TADLVSRASDDVTAVRDAANGALPRLVNTMIM-----VIVSVGALASLHPLFFVPVLLAGVL---YGLAIREFLRTAPPV 195
Cdd:PRK10789 92 TGDLMARATNDVDRVVFAAGEGVLTLVDSLVMgcavlIVMSTQISWQLTLLALLPMPVMAIMikrYGDQLHERFKLAQAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 196 YRAERNasttQSQRILSTIHgvdVVRAFGLENLRTRAVANGSWQAIRWNLR-----GRFlGNTLVVRLLAGEAVATIGVA 270
Cdd:PRK10789 172 FSSLND----RTQESLTSIR---MIKAFGLEDRQSALFAADAEDTGKKNMRvaridARF-DPTIYIAIGMANLLAIGGGS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 271 WtgylLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQ---AAWvclQRVVGVIQarhDKPAV---SERYQRGPTS 344
Cdd:PRK10789 244 W----MVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVErgsAAY---SRIRAMLA---EAPVVkdgSEPVPEGRGE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGY-QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MTSGHARTVL 413
Cdd:PRK10789 314 LDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipltklqLDSWRSRLAV 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSGTLFDDVALGL--AGQAEDwpdERVrdavlAALERVGADwVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:PRK10789 394 VSQTPFLFSDTVANNIALGRpdATQQEI---EHV-----ARLASVHDD-ILRLPQGYDTEVGERGVMLSGGQKQRISIAR 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFA 571
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYR 544
|
....
gi 488473579 572 ALWR 575
Cdd:PRK10789 545 DMYR 548
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-558 |
5.31e-29 |
|
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: 114.54 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTV-LISQ 416
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvTGVPPERRNIgMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSG-TLFDDVALGLAGQAedWPDERVRDAVLAALERVGADWVEQ-LPHGvdtvvgrlgirLSPAQAQQVALARALL 494
Cdd:cd03259 80 DYALFPHlTVAENIAFGLKLRG--VPKAEIRARVRELLELVGLEGLLNrYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 495 ADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVG 558
Cdd:cd03259 147 REPSLLLLDEPLS--------ALDAKLREELReelkelqrelGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
345-566 |
8.10e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 114.39 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTvlISQEIHTFSGT 424
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LFDDVA----------LGLAGQAEDWPDERVRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALL 494
Cdd:COG1131 78 VPQEPAlypdltvrenLRFFARLYGLPRKEARERIDELLELFG------LTDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATaeagssgaTALDRAAAEAVR---------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLR 564
Cdd:COG1131 148 HDPELLILDEPT--------SGLDPEARRELWellrelaaeGKTVLLSTHYLEEAErLCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 488473579 565 QS 566
Cdd:COG1131 220 AR 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
346-555 |
1.29e-28 |
|
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: 113.40 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 346 HVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-----TSGHARTVLISQ--EI 418
Cdd:cd03235 1 EVEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkplEKERKRIGYVPQrrSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 -HTFSGTLFDDVALGLAGQAE--DWPDERVRDAVLAALERVGADWVEQLPHGvdtvvgrlgiRLSPAQAQQVALARALLA 495
Cdd:cd03235 80 dRDFPISVRDVVLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIG----------ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 496 DPPVIILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQVT-MADEVAVMdNGRIV 555
Cdd:cd03235 150 DPDLLLLDEPFA--------GVDPKTQEDIyellrelrrEGMTILVVTHDLGLVLeYFDRVLLL-NRTVV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-553 |
2.91e-28 |
|
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: 111.12 E-value: 2.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-TSGHARTVLISQEIHTFSG 423
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALglagqaedwpdervrdavlaalervgadwveqLPHgvDTVVGRLGIRLSPAQAQQVALARALLADPPVIILD 503
Cdd:cd03229 80 MVFQDFAL--------------------------------FPH--LTVLENIALGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 504 EATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQV-TMADEVAVMDNGR 553
Cdd:cd03229 126 EPTS--------ALDPITRREVRallkslqaqlGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-557 |
3.50e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 342 PTSIHVDQVSFGYQDGPD---VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-----TSGHARTVL 413
Cdd:COG1116 5 APALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEihtfsGTLF------DDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQ 486
Cdd:COG1116 85 VFQE-----PALLpwltvlDNVALGL--ELRGVPKAERRERARELLELVGlAGFEDAYPH-----------QLSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATAeagssgatALD------------RAAAEavRGRTALVVAHRLSQ-VTMADEVAVMDN-- 551
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFG--------ALDaltrerlqdellRLWQE--TGKTVLFVTHDVDEaVFLADRVVVLSArp 216
|
....*.
gi 488473579 552 GRIVEV 557
Cdd:COG1116 217 GRIVEE 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
345-565 |
3.63e-28 |
|
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: 113.03 E-value: 3.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--TSGHARTVLISQEIhtfs 422
Cdd:COG4555 2 IEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdgEDVRKEPREARRQI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 GTLFDDVALglagqaedWPDERVRD--AVLAALERVgadWVEQLPHGVDTVVGRLGIR---------LSPAQAQQVALAR 491
Cdd:COG4555 77 GVLPDERGL--------YDRLTVREniRYFAELYGL---FDEELKKRIEELIELLGLEefldrrvgeLSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAeagssgatALDRAAAEAVR---------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPE 561
Cdd:COG4555 146 ALVHDPKVLLLDEPTN--------GLDVMARRLLReilralkkeGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLD 217
|
....
gi 488473579 562 QLRQ 565
Cdd:COG4555 218 ELRE 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-563 |
8.72e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 8.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsGH----ARTVL-ISQEI 418
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV--GGmvlsEETVWdVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 --------HTFSG-TLFDDVALGLAGQAEDWPD--ERVRDAvlaaLERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQ 486
Cdd:PRK13635 84 gmvfqnpdNQFVGaTVQDDVAFGLENIGVPREEmvERVDQA----LRQVGmEDFLNREPH-----------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQVTMADEVAVMDNGRIVE 556
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEAT--------SMLDPRGRREVletvrqlkeqKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
....*..
gi 488473579 557 VGAPEQL 563
Cdd:PRK13635 221 EGTPEEI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
344-563 |
1.67e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVLISQEIHTfsG 423
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRV--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 ------------TLFDDVALGLagQAEDWPDERVRDAVLAALERVGADWVEQ-LPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:COG1118 79 fvfqhyalfphmTVAENIAFGL--RVRPPSKAEIRARVEELLELVQLEGLADrYPS-----------QLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAH------RLsqvtmADEVAVMDNGRI 554
Cdd:COG1118 146 RALAVEPEVLLLDEPFG--------ALDAKVRKELRrwlrrlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRI 212
|
....*....
gi 488473579 555 VEVGAPEQL 563
Cdd:COG1118 213 EQVGTPDEV 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
345-569 |
2.26e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdvlHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTV-LISQ 416
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqdlTALPPAERPVsMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSG-TLFDDVALGLAgqaedwPDERV----RDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGLR------PGLKLtaeqRAQVEQALERVGlAGLLDRLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRA------------AAEavRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEV 557
Cdd:COG3840 142 RCLVRKRPILLLDEPFS--------ALDPAlrqemldlvdelCRE--RGLTVLMVTHDPEDAaRIADRVLLVADGRIAAD 211
|
250
....*....|..
gi 488473579 558 GAPEQLRQSDGP 569
Cdd:COG3840 212 GPTAALLDGEPP 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
120-575 |
7.22e-27 |
|
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: 116.20 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 120 EKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAE 199
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLE 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 200 RNASTTQSQRILSTIHGVDVVRAFG-------LENLRTRAVANGSWQAI---RW-NLRGRFLGNTLVvrlLAGEAVATIG 268
Cdd:TIGR00957 1137 SVSRSPVYSHFNETLLGVSVIRAFEeqerfihQSDLKVDENQKAYYPSIvanRWlAVRLECVGNCIV---LFAALFAVIS 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 269 vawtgyllvtTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVSERYQRGPTSIHVD 348
Cdd:TIGR00957 1214 ----------RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRG 1283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 349 QVSFG-----YQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGH----------ARTV 412
Cdd:TIGR00957 1284 RVEFRnyclrYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhdlrFKIT 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSGTLfdDVALGLAGQaedWPDERVRDAV-LAALErvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:TIGR00957 1364 IIPQDPVLFSGSL--RMNLDPFSQ---YSDEEVWWALeLAHLK----TFVSALPDKLDHECAEGGENLSVGQRQLVCLAR 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFA 571
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
....
gi 488473579 572 ALWR 575
Cdd:TIGR00957 1515 SMAK 1518
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
345-554 |
1.76e-26 |
|
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: 106.15 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDG-PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTFSG 423
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALgLAGQaedwpderVRDAVLaalervgadwveqlphgvdtvvgrlgirlSPAQAQQVALARALLADPPVIILD 503
Cdd:cd03246 80 YLPQDDEL-FSGS--------IAENIL-----------------------------SGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488473579 504 EATAEAGSSGATALDRAAAEA-VRGRTALVVAHRLSQVTMADEVAVMDNGRI 554
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
345-554 |
2.85e-26 |
|
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: 106.81 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHARTVLI 414
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdgtdiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIhtfsGTLF------------DDVALGLAGQAEDWPDERVRdaVLAALERVGadwveqLPHGVDTVVGrlgiRLSPA 482
Cdd:cd03255 81 RRHI----GFVFqsfnllpdltalENVELPLLLAGVPKKERRER--AEELLERVG------LGDRLNHYPS----ELSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 483 QAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQVTMADEVAVMDNG 552
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTG--------NLDSETGKEVmellrelnkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
..
gi 488473579 553 RI 554
Cdd:cd03255 217 KI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
345-559 |
3.59e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvLISQEIHTFSG- 423
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVL---------VNGQDLSRLKRr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 ----------------------TLFDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLS 480
Cdd:COG2884 73 eipylrrrigvvfqdfrllpdrTVYENVALPL--RVTGKSRKEIRRRVREVLDLVGlSDKAKALPH-----------ELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 481 PAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMD 550
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTG--------NLDPETSWEImelleeinrRGTTVLIATHDLELVdRMPKRVLELE 211
|
....*....
gi 488473579 551 NGRIVEVGA 559
Cdd:COG2884 212 DGRLVRDEA 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-553 |
5.53e-26 |
|
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: 105.63 E-value: 5.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD----VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsgHARTVLISQEIHT 420
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV---PGSIAYVSQEPWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSGTLFDDVALGlagqaEDWPDERVRDAVLA-ALERvgaDwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPV 499
Cdd:cd03250 78 QNGTIRENILFG-----KPFDEERYEKVIKAcALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 500 IILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQVTMADEVAVMDNGR 553
Cdd:cd03250 149 YLLDDPLS--------AVDAHVGRHIfencilglllNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
345-563 |
6.23e-26 |
|
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: 106.62 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV----------LI 414
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelrrkigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSG-TLFDDVALGLagQAEDWPDERVRDAVLAALERVGAD---WVEQLPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVP--KLLKWPKEKIRERADELLALVGLDpaeFADRYPH-----------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALD---RAA--AEAVR-----GRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGA 559
Cdd:cd03295 148 RALAADPPLLLMDEPFG--------ALDpitRDQlqEEFKRlqqelGKTIVFVTHDIDEaFRLADRIAIMKNGEIVQVGT 219
|
....
gi 488473579 560 PEQL 563
Cdd:cd03295 220 PDEI 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
344-560 |
6.29e-26 |
|
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: 105.57 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MTSGHARTV 412
Cdd:cd03369 6 EIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistipLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSGTLFDDValglagqaeDWPDERVRDAVLAALErvgadwveqlphgvdtvVGRLGIRLSPAQAQQVALARA 492
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL---------DPFDEYSDEEIYGALR-----------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 493 LLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAP 560
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
345-554 |
7.90e-26 |
|
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: 104.02 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--TSGHARTVLISQEIhtfs 422
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlgKDIKKEPEEVKRRI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 GTLFDDVALglagqaedWPDERVRDAvlaalervgadwveqlphgvdtvvgrlgIRLSPAQAQQVALARALLADPPVIIL 502
Cdd:cd03230 76 GYLPEEPSL--------YENLTVREN----------------------------LKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 503 DEATaeagssgaTALDRAAAEAVR---------GRTALVVAHRLSQV-TMADEVAVMDNGRI 554
Cdd:cd03230 120 DEPT--------SGLDPESRREFWellrelkkeGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
346-553 |
1.71e-25 |
|
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: 102.71 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 346 HVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvlisqeihtfsgtl 425
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGlagqaeDWPDERVRDAVLaalervgadWVEQLPHGvdtvvgrlgirlspaQAQQVALARALLADPPVIILDEA 505
Cdd:cd00267 58 IDGKDIA------KLPLEELRRRIG---------YVPQLSGG---------------QRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 506 TAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQVTMA-DEVAVMDNGR 553
Cdd:cd00267 108 TS--------GLDPASRERLlellrelaeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-555 |
2.29e-25 |
|
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: 103.88 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 346 HVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM------TSGHARTV-LISQEI 418
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikAKERRKSIgYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 --HTFSGTLFDDVALGLAGQAEDwpDERVRDaVLAALERvgADWVEQLPHGvdtvvgrlgirLSPAQAQQVALARALLAD 496
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAG--NEQAET-VLKDLDL--YALKERHPLS-----------LSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 497 PPVIILDEATaeagsSGataLDRAAAEAV---------RGRTALVVAHRLSQVTM-ADEVAVMDNGRIV 555
Cdd:cd03226 145 KDLLIFDEPT-----SG---LDYKNMERVgelirelaaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
345-563 |
3.53e-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: 104.20 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD---VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHA----- 409
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdlTLLSGKElrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 410 -RTVLISQEIHTFSG-TLFDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQ 486
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPL--EIAGVPKAEIEERVLELLELVGlEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQV-TMADEVAVMDNGRIV 555
Cdd:cd03258 149 VGIARALANNPKVLLCDEAT--------SALDPETTQSIlallrdinreLGLTIVLITHEMEVVkRICDRVAVMEKGEVV 220
|
....*...
gi 488473579 556 EVGAPEQL 563
Cdd:cd03258 221 EEGTVEEV 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
347-558 |
5.31e-25 |
|
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: 102.13 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvLISQEIHTFSgtlf 426
Cdd:cd03214 2 VENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------LDGKDLASLS---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 427 ddvalglagqaedwPDERVRD-AVLA-ALERVGadwVEQLPH-GVDTvvgrlgirLSPAQAQQVALARALLADPPVIILD 503
Cdd:cd03214 68 --------------PKELARKiAYVPqALELLG---LAHLADrPFNE--------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 504 EATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVG 558
Cdd:cd03214 123 EPT--------SHLDIAHQIELlellrrlareRGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
345-563 |
6.35e-25 |
|
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: 103.80 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTF--- 421
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-DGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 422 SGTLFDDVAL------------GLAGQ-------AEDWPDERVRDAvLAALERVG-ADWVEQLphgVDTvvgrlgirLSP 481
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsGRLGRrstwrslFGLFPKEEKQRA-LAALERVGlLDKAYQR---ADQ--------LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 482 AQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHrlsQVTMA----DEVA 547
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVA--------SLDPASSRQVmdllkrinreEGITVIVSLH---QVDLAreyaDRIV 216
|
250
....*....|....*.
gi 488473579 548 VMDNGRIVEVGAPEQL 563
Cdd:cd03256 217 GLKDGRIVFDGPPAEL 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
272-579 |
8.55e-25 |
|
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: 110.04 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 272 TGYLLVTTDRLSVGAAATAvLVLLRLFSPVRFLL----MFLNNLQAAWVCLQRVVGVIQARHDKPAVSERYQRGP---TS 344
Cdd:TIGR00957 558 TFAVYVTVDENNILDAEKA-FVSLALFNILRFPLnilpMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPgegNS 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGY-QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHArtvLISQEIHTFSG 423
Cdd:TIGR00957 637 ITVHNATFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVA---YVPQQAWIQND 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALGLAGQAEDWPDERVRDAVLAALervgadwvEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILD 503
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLEACALLPDL--------EILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 504 EATAEAGSS-GATALDRAAAE--AVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAALWRVWSN 579
Cdd:TIGR00957 786 DPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
344-569 |
1.30e-24 |
|
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: 102.80 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHA-------RTV-LIS 415
Cdd:cd03296 2 SIEVRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAtdvpvqeRNVgFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSG-TLFDDVALGLAGQ--AEDWPDERVRDAVLAALERVGADWVEQlphgvdtvvgRLGIRLSPAQAQQVALARA 492
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGLRVKprSERPPEAEIRAKVHELLKLVQLDWLAD----------RYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 493 LLADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPE 561
Cdd:cd03296 151 LAVEPKVLLLDEPFG--------ALDAKVRKELRrwlrrlhdelHVTTVFVTHDQEEaLEVADRVVVMNKGRIEQVGTPD 222
|
....*...
gi 488473579 562 QLrqSDGP 569
Cdd:cd03296 223 EV--YDHP 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
345-570 |
2.12e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDG-PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSghartVLISQE----IH 419
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG-----ITISKEnlkeIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 420 TFSGTLF-------------DDVALGLAGQAEdwPDERVRDAVLAALERVGADW-VEQLPHgvdtvvgrlgiRLSPAQAQ 485
Cdd:PRK13632 83 KKIGIIFqnpdnqfigatveDDIAFGLENKKV--PPKKMKDIIDDLAKKVGMEDyLDKEPQ-----------NLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 486 QVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQVTMADEVAVMDNGRIV 555
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTS--------MLDPKGKREIkkimvdlrktRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
250 260
....*....|....*....|....
gi 488473579 556 EVGAPE---------QLRQSDGPF 570
Cdd:PRK13632 222 AQGKPKeilnnkeilEKAKIDSPF 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-563 |
1.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.22 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVLISQEIHTFSGT 424
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LFDDVALGLAGQA--ED---------WPDERVRDAVLAALERVGadwVEQLPHgvdtvvgRLGIRLSPAQAQQVALARAL 493
Cdd:PRK13644 82 VFQNPETQFVGRTveEDlafgpenlcLPPIEIRKRVDRALAEIG---LEKYRH-------RSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 494 LADPPVIILDEATAEAG-SSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDpDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
360-558 |
1.06e-23 |
|
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: 99.25 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTV-LISQEIHTFSG-TLFDDVA 430
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvTDLPPKDRDIaMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 431 LGL--AGQAEDWPDERVRDAvlAALervgadwveqlpHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATae 508
Cdd:cd03301 95 FGLklRKVPKDEIDERVREV--AEL------------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL-- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 509 agsSGATALDRAA--AEAVR-----GRTALVVAHrlSQV---TMADEVAVMDNGRIVEVG 558
Cdd:cd03301 159 ---SNLDAKLRVQmrAELKRlqqrlGTTTIYVTH--DQVeamTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
345-563 |
1.70e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.58 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGY---QDGPDvLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVL----ISQE 417
Cdd:PRK13650 5 IEVKNLTFKYkedQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLLTEEnvwdIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 I--------HTFSG-TLFDDVALGLAGQAedWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQV 487
Cdd:PRK13650 83 IgmvfqnpdNQFVGaTVEDDVAFGLENKG--IPHEEMKERVNEALELVGmQDFKEREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 488 ALARALLADPPVIILDEATAEAGSSGATALDRaAAEAVR---GRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIK-TIKGIRddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
343-563 |
2.02e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 101.69 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT-----MTSGHAR------- 410
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPPKdrniamv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 411 ----------TVlisqeihtfsgtlFDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHGvdtvvgrlgirL 479
Cdd:COG3839 81 fqsyalyphmTV-------------YENIAFPL--KLRKVPKAEIDRRVREAAELLGlEDLLDRKPKQ-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 480 SPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHrlSQV---TMADEV 546
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLS--------NLDAKLRVEMRaeikrlhrrlGTTTIYVTH--DQVeamTLADRI 204
|
250
....*....|....*..
gi 488473579 547 AVMDNGRIVEVGAPEQL 563
Cdd:COG3839 205 AVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-563 |
5.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVLISQEIHTFSG 423
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFD-------------DVALGLAGQAEdwPDERVRDAVLAALERVGA-DWVEQLPHGvdtvvgrlgirLSPAQAQQVAL 489
Cdd:PRK13648 87 IVFQnpdnqfvgsivkyDVAFGLENHAV--PYDEMHRRVSEALKQVDMlERADYEPNA-----------LSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 490 ARALLADPPVIILDEATAEAGSSGATALDRAAAE--AVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
360-563 |
7.59e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--------TSGHART---VLISQEIhtfsgTLFDD 428
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrSPRDAQAagiAIIHQEL-----NLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 --VA----LG---LAGQAEDWPdeRVRDAVLAALERVGADwveqLPhgVDTVVGRLGIrlspAQAQQVALARALLADPPV 499
Cdd:COG1129 94 lsVAenifLGrepRRGGLIDWR--AMRRRARELLARLGLD----ID--PDTPVGDLSV----AQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 500 IILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG1129 162 LILDEPTA--------SLTEREVERLfriirrlkaQGVAIIYISHRLDEVfEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
30-321 |
7.87e-23 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU 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: 349986 [Multi-domain] Cd Length: 292 Bit Score: 98.66 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP-LFFVPVLLAGVLYGLAIReF 188
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWkLTLISLAIIPFIALFSYV-F 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 189 LRTAPPVYRA--ERNASttqsqriLST-----IHGVDVVRAFGLE------------NLRTRAVANGSWQAIRWNLrGRF 249
Cdd:cd18542 160 FKKVRPAFEEirEQEGE-------LNTvlqenLTGVRVVKAFAREdyeiekfdkeneEYRDLNIKLAKLLAKYWPL-MDF 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 250 LGNTLVVrllageavatiGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18542 232 LSGLQIV-----------LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
361-563 |
7.95e-23 |
|
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: 98.48 E-value: 7.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI----TMTSGHARTVLISQEIHTFS-----------GTL 425
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgQDIAAMSRKELRELRRKKISmvfqsfallphRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGLAGQAEDwPDERVRDAvLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDE 504
Cdd:cd03294 120 LENVAFGLEVQGVP-RAEREERA-AEALELVGlEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 505 ATaeagssgaTALD---RA-------AAEAVRGRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:cd03294 187 AF--------SALDpliRRemqdellRLQAELQKTIVFITHDLDEaLRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
307-536 |
1.26e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 307 FLNNLQ--AAWV-CLQRVVG---VIQARHDKPAVSERYQRGP-TSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGE 379
Cdd:COG4178 318 FVDNYQslAEWRaTVDRLAGfeeALEAADALPEAASRIETSEdGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGP 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 380 SGAGKSTLAALVAGLLEPRQGSITMTSGhARTVLISQEIHTFSGTLFDdvALGLAGQAEDWPDERVRdavlAALERVG-A 458
Cdd:COG4178 398 SGSGKSTLLRAIAGLWPYGSGRIARPAG-ARVLFLPQRPYLPLGTLRE--ALLYPATAEAFSDAELR----EALEAVGlG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 459 DWVEQLphgvDTVVgRLGIRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----RGR---TAL 531
Cdd:COG4178 471 HLAERL----DEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS--------ALDEENEAALyqllREElpgTTV 537
|
....*.
gi 488473579 532 V-VAHR 536
Cdd:COG4178 538 IsVGHR 543
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
345-563 |
3.19e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 96.73 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG--HARTV--------LI 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevNAENEkwvrskvgLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEI--HTFSGTLFDDVALGLA--GQAEDWPDERVRDavlaALERVGA-DWVEQLPHgvdtvvgrlgiRLSPAQAQQVAL 489
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGPVnmGLDKDEVERRVEE----ALKAVRMwDFRDKPPY-----------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 490 ARALLADPPVIILDEATAEAGSSGA----TALDRAAAEavrGRTALVVAHRLS-QVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQetlmEILDRLHNQ---GKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
364-563 |
4.41e-22 |
|
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: 97.43 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRqgsiTMTSGHARtvLISQEIHTFSG-------------------- 423
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP----GITSGEIL--FDGEDLLKLSEkelrkirgreiqmifqdpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 ------TLFDDVALGLAgQAEDWPDERVRDAVLAALERVG----ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARAL 493
Cdd:COG0444 98 slnpvmTVGDQIAEPLR-IHGGLSKAEARERAIELLERVGlpdpERRLDRYPH-----------ELSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 494 LADPPVIILDEATaeagssgaTALD---RA---------AAEavRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAP 560
Cdd:COG0444 166 ALEPKLLIADEPT--------TALDvtiQAqilnllkdlQRE--LGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPV 235
|
...
gi 488473579 561 EQL 563
Cdd:COG0444 236 EEL 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
364-563 |
4.84e-22 |
|
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: 99.76 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLA-ALVAglLEPRQGSItmtsghartVLISQEIHTFSGT-----------LFDD--- 428
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGlALLR--LIPSEGEI---------RFDGQDLDGLSRRalrplrrrmqvVFQDpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 -----------VALGLAGQAEDWPDERVRDAVLAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLA 495
Cdd:COG4172 374 slsprmtvgqiIAEGLRVHGPGLSAAERRARVAEALEEVGldPAARHRYPH-----------EFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 496 DPPVIILDEATaeagssgaTALDR----------AAAEAVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG4172 443 EPKLLVLDEPT--------SALDVsvqaqildllRDLQREHGLAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
347-565 |
7.58e-22 |
|
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: 94.04 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHART----VLIS 415
Cdd:cd03224 3 VENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditgLPPHERAragiGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSG-TLFDDVALGLAGQAEDwPDERVRDAVLAALERVGADWveqlphgvdtvvGRLGIRLSPAQAQQVALARALL 494
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARRRA-KRKARLERVYELFPRLKERR------------KQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATAeagssG---------ATALDRAAAEavrGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQLR 564
Cdd:cd03224 149 SRPKLLLLDEPSE-----GlapkiveeiFEAIRELRDE---GVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELL 220
|
.
gi 488473579 565 Q 565
Cdd:cd03224 221 A 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
345-563 |
7.90e-22 |
|
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: 94.61 E-value: 7.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQG-------SITMTSGHARTV-LISQ 416
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeilldgkDITNLPPHKRPVnTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSG-TLFDDVALGLagQAEDWPDERVRDAVLAALERVGADWVEQ-LPHgvdtvvgrlgiRLSPAQAQQVALARALL 494
Cdd:cd03300 80 NYALFPHlTVFENIAFGL--RLKKLPKAEIKERVAEALDLVQLEGYANrKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:cd03300 147 NEPKVLLLDEPLG--------ALDLKLRKDMQlelkrlqkelGITFVFVTHDQEEaLTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
364-563 |
8.29e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 96.72 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgsitmTSGharTVLI-SQEIHTFSG------------------- 423
Cdd:COG4608 37 VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP-------TSG---EILFdGQDITGLSGrelrplrrrmqmvfqdpya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 ------TLFDDVALGLAGQaEDWPDERVRDAVLAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLA 495
Cdd:COG4608 107 slnprmTVGDIIAEPLRIH-GLASKAERRERVAELLELVGlrPEHADRYPH-----------EFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 496 DPPVIILDEATAeagssgatALD---RAA---------AEavRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQ 562
Cdd:COG4608 175 NPKLIVCDEPVS--------ALDvsiQAQvlnlledlqDE--LGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDE 244
|
.
gi 488473579 563 L 563
Cdd:COG4608 245 L 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
360-561 |
1.32e-21 |
|
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: 93.94 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVLiSQEIHTFS-----------GTLFDD 428
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGKDITNL-PPEKRDISyvpqnyalfphMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 VALGLAGQAEDWP--DERVRD--AVLaalervgadwveqlphGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDE 504
Cdd:cd03299 92 IAYGLKKRKVDKKeiERKVLEiaEML----------------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 505 ATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPE 561
Cdd:cd03299 156 PFS--------ALDVRTKEKLReelkkirkefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPE 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-563 |
1.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD-VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS--------ITMTsghARTVLIS 415
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLT---AKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEI---------HTFSG-TLFDDVALGLAGQAEdwPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQA 484
Cdd:PRK13640 83 REKvgivfqnpdNQFVGaTVGDDVAFGLENRAV--PRPEMIKIVRDVLADVGmLDYIDSEPA-----------NLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 485 QQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAV--RGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQ 562
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
.
gi 488473579 563 L 563
Cdd:PRK13640 230 I 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
102-568 |
2.75e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 102 RLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAV-RDAANGA------LPRLVNTMIMV-IVSVGALASLHPLFFVp 173
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdRNVANLMnmfmnqLWQLLSTFALIgTVSTISLWAIMPLLIL- 1062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 174 VLLAGVLYGLAIREFLR----TAPPVYRAERNAsttqsqrilstIHGVDVVRAFglENLRTRAVANGSW--QAIRWNLRG 247
Cdd:PLN03232 1063 FYAAYLYYQSTSREVRRldsvTRSPIYAQFGEA-----------LNGLSSIRAY--KAYDRMAKINGKSmdNNIRFTLAN 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 248 RFLGNTLVVRLLAGEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCL---QRVVGV 324
Cdd:PLN03232 1130 TSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLnsvERVGNY 1209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 325 IQARHDKPAVSERyQRGPT------SIHVDQVSFGYQDG-PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEP 397
Cdd:PLN03232 1210 IDLPSEATAIIEN-NRPVSgwpsrgSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL 1288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 398 RQGSITMTS--------GHARTVL--ISQEIHTFSGTL-FDDVALGLAGQAEDWpdervrdavlAALERVG-ADWVEQLP 465
Cdd:PLN03232 1289 EKGRIMIDDcdvakfglTDLRRVLsiIPQSPVLFSGTVrFNIDPFSEHNDADLW----------EALERAHiKDVIDRNP 1358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 466 HGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADE 545
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDK 1438
|
490 500
....*....|....*....|...
gi 488473579 546 VAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:PLN03232 1439 ILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
360-572 |
2.76e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTVLIS-QEIHTFSG-TLFDDVA 430
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvTHRSIQQRDICMVfQSYALFPHmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 431 LGLAGQAEdwPDERVRDAVLAALERVGADWVEQlpHGVDTVVGrlgirlspAQAQQVALARALLADPPVIILDEATaeag 510
Cdd:PRK11432 101 YGLKMLGV--PKEERKQRVKEALELVDLAGFED--RYVDQISG--------GQQQRVALARALILKPKVLLFDEPL---- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 511 SSGATALDRAAAEAVR------GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL-RQSDGPFAA 572
Cdd:PRK11432 165 SNLDANLRRSMREKIRelqqqfNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQIGSPQELyRQPASRFMA 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
360-555 |
5.94e-21 |
|
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: 89.80 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvlisqeihtfsgtlfddvalgLAGQAED 439
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL-----------------------------VDGKEVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 WPDerVRDAVlaalervgadwveqlphgvdtvvgRLGIR----LSPAQAQQVALARALLADPPVIILDEATAeagssgat 515
Cdd:cd03216 66 FAS--PRDAR------------------------RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTA-------- 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473579 516 ALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGRIV 555
Cdd:cd03216 112 ALTPAEVERLfkvirrlraQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
364-564 |
6.97e-21 |
|
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: 91.73 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-------ITMTSGHARTVL-IS---QEIHTFSG-TLFDDVAL 431
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgedITGLPPHEIARLgIGrtfQIPRLFPElTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 GL-------AGQAEDWPDER-VRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILD 503
Cdd:cd03219 99 AAqartgsgLLLARARREEReARERAEELLERVG------LADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 504 EATAeagssGATALDRAAAEAV------RGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLR 564
Cdd:cd03219 169 EPAA-----GLNPEETEELAELirelreRGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
345-558 |
7.34e-21 |
|
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: 91.02 E-value: 7.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdvlHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTS---GHA----RTV-LISQ 416
Cdd:cd03298 1 VRLDKIRFSYGEQP---MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAppadRPVsMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSG-TLFDDVALGLAGQAEDWPDErvRDAVLAALERVGADWVEQlphgvdtvvgRLGIRLSPAQAQQVALARALLA 495
Cdd:cd03298 78 ENNLFAHlTVEQNVGLGLSPGLKLTAED--RQAIEVALARVGLAGLEK----------RLPGELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 496 DPPVIILDEATAEAGSSGATALDRAAAE--AVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVG 558
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKrLAQRVVFLDNGRIAAQG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-568 |
3.09e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 95.58 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 319 QRVVGVIQARHDKPAVSERYQRGPT-----SIHVDQVSFGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVA 392
Cdd:PLN03130 1207 ERVGTYIDLPSEAPLVIENNRPPPGwpssgSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALF 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 393 GLLEPRQGSITM------TSGHA--RTVL--ISQEIHTFSGTL-FDDVALGLAGQAEDWpdervrdavlAALERVG-ADW 460
Cdd:PLN03130 1287 RIVELERGRILIdgcdisKFGLMdlRKVLgiIPQAPVLFSGTVrFNLDPFNEHNDADLW----------ESLERAHlKDV 1356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 461 VEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAeAGSSGATAL-DRAAAEAVRGRTALVVAHRLSQ 539
Cdd:PLN03130 1357 IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA-AVDVRTDALiQKTIREEFKSCTMLIIAHRLNT 1435
|
250 260
....*....|....*....|....*....
gi 488473579 540 VTMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:PLN03130 1436 IIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-563 |
3.81e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.07 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQV--SFGYQDgpdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT-----MTSGHAR---TVL 413
Cdd:PRK10851 2 SIEIANIkkSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdVSRLHARdrkVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSG-TLFDDVALGLA--GQAEDWPDERVRDAVLAALERVgadwveQLPHgvdtVVGRLGIRLSPAQAQQVALA 490
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGLTvlPRRERPNAAAIKAKVTQLLEMV------QLAH----LADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRAAAEAVRgR-----------TALVVAHRLSQVT-MADEVAVMDNGRIVEVG 558
Cdd:PRK10851 149 RALAVEPQILLLDEPFG--------ALDAQVRKELR-RwlrqlheelkfTSVFVTHDQEEAMeVADRVVVMSQGNIEQAG 219
|
....*
gi 488473579 559 APEQL 563
Cdd:PRK10851 220 TPDQV 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
364-565 |
5.28e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 89.71 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHARTVL-IS---QEIHTFSG-TLFDDVAL 431
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditgLPPHRIARLgIArtfQNPRLFPElTVLENVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 GLAGQAEDWP-------------DERVRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALLADPP 498
Cdd:COG0411 103 AAHARLGRGLlaallrlprarreEREARERAEELLERVG------LADRADEPAG----NLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 499 VIILDEATA---EAGSSGATALDRAAAEAvRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQ 565
Cdd:COG0411 173 LLLLDEPAAglnPEETEELAELIRRLRDE-RGITILLIEHDMDLVMgLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
361-559 |
6.44e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVLISQEIHTF---------------SGTL 425
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDLTALSEKELRKArrqigmifqhfnllsSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDE 504
Cdd:PRK11153 100 FDNVALPL--ELAGTPKAEIKARVTELLELVGlSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 505 ATaeagssgaTALDRAAAEAV--------R--GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGA 559
Cdd:PRK11153 167 AT--------SALDPATTRSIlellkdinRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
360-554 |
7.73e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG---HAR--TVLISQEIHTFS-GTLFDDVALGL 433
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEARedTRLMFQDARLLPwKKVIDNVGLGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 434 AGqaeDWpdervRDAVLAALERVG-ADWVEQLPHGvdtvvgrlgirLSPAQAQQVALARALLADPPVIILDEATaeagss 512
Cdd:PRK11247 107 KG---QW-----RDAALQALAAVGlADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPL------ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473579 513 GA-TALDRAAAEAV-------RGRTALVVAHRLSQ-VTMADEVAVMDNGRI 554
Cdd:PRK11247 162 GAlDALTRIEMQDLieslwqqHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
345-563 |
1.05e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVS--FGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgsitmTSGharTVLIS-QEIHT 420
Cdd:COG1135 2 IELENLSktFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERP-------TSG---SVLVDgVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSG-----------------------TLFDDVALGL--AGqaedWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgr 474
Cdd:COG1135 72 LSErelraarrkigmifqhfnllssrTVAENVALPLeiAG----VPKAEIRKRVAELLELVGlSDKADAYPS-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 475 lgiRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQV-TMA 543
Cdd:COG1135 140 ---QLSGGQKQRVGIARALANNPKVLLCDEATS--------ALDPETTRSIldllkdinreLGLTIVLITHEMDVVrRIC 208
|
250 260
....*....|....*....|
gi 488473579 544 DEVAVMDNGRIVEVGAPEQL 563
Cdd:COG1135 209 DRVAVLENGRIVEQGPVLDV 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
343-562 |
1.15e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYQdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHA----RT 411
Cdd:PRK13548 1 AMLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLngrpladWSPAElarrRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 412 VLiSQEIH-TFSGTLFDDVALGLAgqaeDWPDERVRD--AVLAALERVgadwveqlphGVDTVVGRLGIRLSPAQAQQVA 488
Cdd:PRK13548 80 VL-PQHSSlSFPFTVEEVVAMGRA----PHGLSRAEDdaLVAAALAQV----------DLAHLAGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 489 LARALL------ADPPVIILDEATAeagssgatALD--------RAAAEAVR--GRTALVVAHRLSQVTM-ADEVAVMDN 551
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTS--------ALDlahqhhvlRLARQLAHerGLAVIVVLHDLNLAARyADRIVLLHQ 216
|
250
....*....|.
gi 488473579 552 GRIVEVGAPEQ 562
Cdd:PRK13548 217 GRLVADGTPAE 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
360-554 |
1.93e-19 |
|
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: 87.20 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT-----MTSGHARTVLISQEI-HTF-SGTLF------ 426
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIidglkLTDDKKNINELRQKVgMVFqQFNLFphltvl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 427 DDVALGLAgQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEA 505
Cdd:cd03262 95 ENITLAPI-KVKGMSKAEAEERALELLEKVGlADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 506 TAeagssgatALD-----------RAAAEavRGRTALVVAHRLS---QVtmADEVAVMDNGRI 554
Cdd:cd03262 163 TS--------ALDpelvgevldvmKDLAE--EGMTMVVVTHEMGfarEV--ADRVIFMDDGRI 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
345-562 |
3.18e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 87.48 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHA------------RTV 412
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL-NGRPlaawspwelarrRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LiSQEIH-TFSGTLFDDVALGLAGQAEdwPDERVRDAVLAALERVgadwveqlphGVDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:COG4559 80 L-PQHSSlAFPFTVEEVVALGRAPHGS--SAAQDRQIVREALALV----------GLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALL-------ADPPVIILDEATAeagssgatALD--------RAAAE-AVRGRTALVVAHRLSQVTM-ADEVAVMDNGRI 554
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTS--------ALDlahqhavlRLARQlARRGGGVVAVLHDLNLAAQyADRILLLHQGRL 218
|
....*...
gi 488473579 555 VEVGAPEQ 562
Cdd:COG4559 219 VAQGTPEE 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
345-558 |
5.30e-19 |
|
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: 85.73 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHARTVLISQE 417
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgksyqkNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 IHTFSGTLFDDVALGLAGQAEDWPDERVRDavlaALERVGadwveqLPHGVDTVVGR--LGIRlspaqaQQVALARALLA 495
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVG------LKDSAKKKVKGfsLGMK------QRLGIALALLG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 496 DPPVIILDEATaeagssgaTALDRAAAEAVR---------GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03268 144 NPDLLILDEPT--------NGLDPDGIKELRelilslrdqGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
347-567 |
7.31e-19 |
|
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: 85.80 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHART----VLIS 415
Cdd:COG0410 6 VENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdgeditgLPPHRIArlgiGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSG-TLFDDVALGLAGQAEDWPDERVRDAVLAALERVGadwvEQLphgvdtvvGRLGIRLSPAQAQQVALARALL 494
Cdd:COG0410 85 EGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELFPRLK----ERR--------RQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATAeagssG---------ATALDRAAAEavrGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQLR 564
Cdd:COG0410 153 SRPKLLLLDEPSL-----GlapliveeiFEIIRRLNRE---GVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELL 224
|
...
gi 488473579 565 QSD 567
Cdd:COG0410 225 ADP 227
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
30-314 |
7.69e-19 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. Moreover, 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: 349995 [Multi-domain] Cd Length: 289 Bit Score: 87.10 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPtsaLLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGS---SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFL 189
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 190 RTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTLVVRLLAGEAVATIGV 269
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488473579 270 AWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAA 314
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKA 282
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-561 |
1.12e-18 |
|
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: 85.18 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGH--------ARTVL 413
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-AGQdlfaldedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEI----HTF----SGTLFDDVA--LGLAGQAEDwpdervRDAVLAALERVGadwveqlphgvdtvvgrLGIRLS--P 481
Cdd:COG4181 88 RARHVgfvfQSFqllpTLTALENVMlpLELAGRRDA------RARARALLERVG-----------------LGHRLDhyP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 482 AQ-----AQQVALARALLADPPVIILDEATAEagssgataLDRAAAEAV----------RGRTALVVAHRLSQVTMADEV 546
Cdd:COG4181 145 AQlsggeQQRVALARAFATEPAILFADEPTGN--------LDAATGEQIidllfelnreRGTTLVLVTHDPALAARCDRV 216
|
250
....*....|....*
gi 488473579 547 AVMDNGRIVEVGAPE 561
Cdd:COG4181 217 LRLRAGRLVEDTAAT 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
345-550 |
1.57e-18 |
|
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: 84.07 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--TSGHARTVLISQEIHtfs 422
Cdd:COG4133 3 LEAENLSCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngEPIRDAREDYRRRLA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 gTLFDDVAL--------GLAGQAEDWPDERVRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALL 494
Cdd:COG4133 79 -YLGHADGLkpeltvreNLRFWAALYGLRADREAIDEALEAVG------LAGLADLPVR----QLSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 495 ADPPVIILDEATaeagssgaTALDRAAAEAV---------RGRTALVVAHRLSQVTMADEVAVMD 550
Cdd:COG4133 148 SPAPLWLLDEPF--------TALDAAGVALLaeliaahlaRGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
345-563 |
1.95e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHA------------RTV 412
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPikydkksllevrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LI---SQEIHTFSGTLFDDVALGLA--GQAEDWPDERVRDAvlaaLERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQ 486
Cdd:PRK13639 81 GIvfqNPDDQLFAPTVEEDVAFGPLnlGLSKEEVEKRVKEA----LKAVGmEGFENKPPH-----------HLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 487 VALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR-GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-558 |
2.32e-18 |
|
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: 83.96 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTV---SLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSghARTVLISQEIHTF 421
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVdgvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 422 SGTLFDDVALglagqaedWPDERVRDAVL--AALERVGADwveQLPHGVDTVVGRLGIR---------LSPAQAQQVALA 490
Cdd:cd03266 80 LGFVSDSTGL--------YDRLTARENLEyfAGLYGLKGD---ELTARLEELADRLGMEelldrrvggFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 491 RALLADPPVIILDEATaeagssgaTALDRAAAEAVR---------GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03266 149 RALVHDPPVLLLDEPT--------TGLDVMATRALRefirqlralGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
360-575 |
2.46e-18 |
|
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: 84.96 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MTSGHARTVLISQEIHTFSGTlfddV 429
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVidgidisklpLHTLRSRLSIILQDPILFSGS----I 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLAGQAEdWPDERVRDAV-LAALERVgadwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAE 508
Cdd:cd03288 112 RFNLDPECK-CTDDRLWEALeIAQLKNM----VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 509 AGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL-RQSDGPFAALWR 575
Cdd:cd03288 187 IDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLlAQEDGVFASLVR 254
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
345-558 |
2.53e-18 |
|
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: 83.78 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGpDVLHTVSLDIPAGHTVvLVGESGAGKSTLAALVAGLLEPRQGSITM---------TSGHARTVLIS 415
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlkqpQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSG-TLFDdvALGLAGQAEDWPDERVRDAVLAALERVgadwveqlphGVDTVVGRLGIRLSPAQAQQVALARALL 494
Cdd:cd03264 79 QEFGVYPNfTVRE--FLDYIAWLKGIPSKEVKARVDEVLELV----------NLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 495 ADPPVIILDEATAeagssgatALDRAAAEAVR--------GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03264 147 GDPSILIVDEPTA--------GLDPEERIRFRnllselgeDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
30-321 |
2.99e-18 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. Moreover, 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: 349996 [Multi-domain] Cd Length: 292 Bit Score: 85.55 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFL 189
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 190 RtappvyRAERNASTTQSQ--RILS----TIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLG--NTLVVRLLAG 261
Cdd:cd18552 161 K------RLRKISRRSQESmgDLTSvlqeTLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARalSSPLMELLGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 262 EAVAtiGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18552 235 IAIA--LVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
344-558 |
3.31e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGpDVLHTVSLDIPAGHTVVLVGESGAGKSTLAAlVAGLLE-PRQGSITMTSGHARtvlISQEIHTFS 422
Cdd:PRK11124 2 SIQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGNHFD---FSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 G-TLFDDVALgLAGQAEDWPDERVRDAVLAALERVGADWVEQLPHGVDTVVGRLGI---------RLSPAQAQQVALARA 492
Cdd:PRK11124 77 IrELRRNVGM-VFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLkpyadrfplHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 493 LLADPPVIILDEATAeagssgatALD-RAAAEAVR--------GRTALVVAHrlsQVTMADEVAV----MDNGRIVEVG 558
Cdd:PRK11124 156 LMMEPQVLLFDEPTA--------ALDpEITAQIVSiirelaetGITQVIVTH---EVEVARKTASrvvyMENGHIVEQG 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-506 |
4.48e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGhARTVLISQEIHTFSG-TL 425
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-LRIGYLPQEPPLDDDlTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDValgLAGQAEDWPDERVRDAVLAALERVGADWVEQ--------------LPHGVDTVVGRLGIR----------LSP 481
Cdd:COG0488 79 LDTV---LDGDAELRALEAELEELEAKLAEPDEDLERLaelqeefealggweAEARAEEILSGLGFPeedldrpvseLSG 155
|
170 180
....*....|....*....|....*
gi 488473579 482 AQAQQVALARALLADPPVIILDEAT 506
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPT 180
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
343-562 |
8.62e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG---------HARTV- 412
Cdd:PRK11231 1 MTLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqLARRLa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSG-TLFDDVALGLAGQAEDWPDERVRD--AVLAALERVgadwveqlphGVDTVVGRLGIRLSPAQAQQVAL 489
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGRSPWLSLWGRLSAEDnaRVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 490 ARALLADPPVIILDEATaeagssgaTALD-RAAAEAVR--------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGA 559
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPT--------TYLDiNHQVELMRlmrelntqGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGT 221
|
...
gi 488473579 560 PEQ 562
Cdd:PRK11231 222 PEE 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-562 |
1.42e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.17 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGP----DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT------------MTSG 407
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdkkvkLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 408 HARTVLISQ--EIHTFSGTLFDDVALGLAGQAEDwpDERVRDAVLAALERVGADWveqlphgvDTVVGRLGIRLSPAQAQ 485
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGPINLGLS--EEEIENRVKRAMNIVGLDY--------EDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 486 QVALARALLADPPVIILDEATAeagssgatALDRAAAEAVRGR----------TALVVAHRLSQVT-MADEVAVMDNGRI 554
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTA--------GLDPKGRDEILNKikelhkeynmTIILVSHSMEDVAkLADRIIVMNKGKC 223
|
....*...
gi 488473579 555 VEVGAPEQ 562
Cdd:PRK13637 224 ELQGTPRE 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
29-321 |
2.01e-17 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 82.90 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 29 YFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMI 108
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 109 AVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVLLAGVLYg 182
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVrlalvtLAVLPLLVLVVFL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 183 laIREFLRTAppvYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTL--VVRLLA 260
Cdd:cd18545 160 --LRRRARKA---WQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFwpLVELIS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 261 GeaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18545 235 A--LGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-563 |
2.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDV--LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGsITMTSGHART----------- 411
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG-KVKIDGELLTaenvwnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 412 -VLISQEIHTFSG-TLFDDVALGLAGQAedWPDERVRDAVLAALERVGA-DWVEQLPhgvdtvvgrlgIRLSPAQAQQVA 488
Cdd:PRK13642 84 gMVFQNPDNQFVGaTVEDDVAFGMENQG--IPREEMIKRVDEALLAVNMlDFKTREP-----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 489 LARALLADPPVIILDEATAEAGSSGATALDRAAAEaVRGR---TALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
343-563 |
2.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTS---GHAR--------- 410
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpiDYSRkglmklres 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 411 --TVLISQEIHTFSGTLFDDVALGLAGQAedWPDERVRDAVLAALERVGADWVEQLP-HGvdtvvgrlgirLSPAQAQQV 487
Cdd:PRK13636 84 vgMVFQDPDNQLFSASVYQDVSFGAVNLK--LPEDEVRKRVDNALKRTGIEHLKDKPtHC-----------LSFGQKKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 488 ALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-554 |
3.25e-17 |
|
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: 80.53 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHA-------RTVLISQE 417
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-RVNGQDvsdlrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 IHT--------FSGTLFDDVALGLagQAEDWPDERVRDAVLAALERVGadwveqLPHGVDTvvgrLGIRLSPAQAQQVAL 489
Cdd:cd03292 80 IGVvfqdfrllPDRNVYENVAFAL--EVTGVPPREIRKRVPAALELVG------LSHKHRA----LPAELSGGEQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 490 ARALLADPPVIILDEATAEagssgataLDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGRI 554
Cdd:cd03292 148 ARAIVNSPTILIADEPTGN--------LDPDTTWEImnllkkinkAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
345-567 |
4.54e-17 |
|
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: 80.90 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgsitmTSGHARTVL----------- 413
Cdd:COG1119 4 LELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPP-------TYGNDVRLFgerrggedvwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIHTFSGTLFDDVAlglagqaedwPDERVRDAVLAAL--------------ERVGADWVEQLphGVDTVVGRLGIRL 479
Cdd:COG1119 76 LRKRIGLVSPALQLRFP----------RDETVLDVVLSGFfdsiglyreptdeqRERARELLELL--GLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 480 SPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAVR---------GRTALV-VAHRLSQVTMA-DEVAV 548
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTA--------GLDLGARELLLalldklaaeGAPTLVlVTHHVEEIPPGiTHVLL 215
|
250
....*....|....*....
gi 488473579 549 MDNGRIVEVGAPEQLRQSD 567
Cdd:COG1119 216 LKDGRVVAAGPKEEVLTSE 234
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
30-321 |
4.87e-17 |
|
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: 81.76 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 VGLGLDQQRVEKAGTADLVSRASDDVTAVRdAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFL 189
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQ-RFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 190 RTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSwQAIRW------NLRGRFlgnTLVVRLLAGea 263
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAA-RRLRAtrlraaRLRARF---WPLLEALPE-- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 264 VATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
345-556 |
5.03e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDG--------PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQ 416
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSGTL---FDDvALGLAGqaedwPDERVRDAV------LAALERVG-ADWVEQLPHGVD---TVVGRLGIRLSPAQ 483
Cdd:PRK10419 83 QRKAFRRDIqmvFQD-SISAVN-----PRKTVREIIreplrhLLSLDKAErLARASEMLRAVDlddSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 484 AQQVALARALLADPPVIILDEATAEAGSS-GATALDRAAAEAVRGRTA-LVVAHRLSQVT-MADEVAVMDNGRIVE 556
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVlQAGVIRLLKKLQQQFGTAcLFITHDLRLVErFCQRVMVMDNGQIVE 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
360-569 |
5.85e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIhtfsGTLfddvalglagqaed 439
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPLDPEDRRRI----GYL-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 wPDER-------VRDAV--LAAL--------ERVGADWVEqlphgvdtvvgRLGI---------RLSPAQAQQVALARAL 493
Cdd:COG4152 77 -PEERglypkmkVGEQLvyLARLkglskaeaKRRADEWLE-----------RLGLgdrankkveELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 494 LADPPVIILDEAtaeagSSGataLDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG4152 145 LHDPELLILDEP-----FSG---LDPVNVELLkdvirelaaKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
....*.
gi 488473579 564 RQSDGP 569
Cdd:COG4152 217 RRQFGR 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
345-563 |
6.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPD-----VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM----TSGHARTvlis 415
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldTSDEENL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSGTLF-------------DDVALGlagqAEDW--PDERVRDAVLAALERVGA-DWVEQLPHgvdtvvgrlgiRL 479
Cdd:PRK13633 81 WDIRNKAGMVFqnpdnqivativeEDVAFG----PENLgiPPEEIRERVDESLKKVGMyEYRRHAPH-----------LL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 480 SPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQVTMADEVAVMDNGRIVEV 557
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
....*.
gi 488473579 558 GAPEQL 563
Cdd:PRK13633 226 GTPKEI 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-563 |
8.19e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 359 DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-----ITMTSGHARTVLISQE-------IHTFSG-TL 425
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLIRQEagmvfqqFYLFPHlTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGlagqaedwPdERVRDAVLAALERVGADWVEQLphGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEA 505
Cdd:PRK09493 95 LENVMFG--------P-LRVRGASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 506 TaeagssgaTALD-----------RAAAEavRGRTALVVAHrlsQVTMADEVA----VMDNGRIVEVGAPEQL 563
Cdd:PRK09493 164 T--------SALDpelrhevlkvmQDLAE--EGMTMVIVTH---EIGFAEKVAsrliFIDKGRIAEDGDPQVL 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
364-558 |
1.41e-16 |
|
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: 78.88 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGhTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSgharTVLISQEIHTFS-------GTLFDDVALglagq 436
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKINLppqqrkiGLVFQQYAL----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 437 aedWPDERVRDAVLAALER----VGADWVEQLPH--GVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATaeag 510
Cdd:cd03297 87 ---FPHLNVRENLAFGLKRkrnrEDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF---- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 511 ssgaTALDRAAAEAVRGR----------TALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03297 160 ----SALDRALRLQLLPElkqikknlniPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
345-573 |
1.99e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.86 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdvlHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG-HARTV-------LISQ 416
Cdd:PRK10771 2 LKLTDITWLYHHLP---MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPpsrrpvsMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 EIHTFSG-TLFDDVALGLAgqaedwPDERV----RDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALA 490
Cdd:PRK10771 79 ENNLFSHlTVAQNIGLGLN------PGLKLnaaqREKLHAIARQMGiEDLLARLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRA--------AAEAVRGR--TALVVAHRLSQVT-MADEVAVMDNGRIVEVGA 559
Cdd:PRK10771 142 RCLVREQPILLLDEPFS--------ALDPAlrqemltlVSQVCQERqlTLLMVSHSLEDAArIAPRSLVVADGRIAWDGP 213
|
250
....*....|....
gi 488473579 560 PEQLRQSDGPFAAL 573
Cdd:PRK10771 214 TDELLSGKASASAL 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-565 |
2.12e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPD----VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-------ITMTSGHA--- 409
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSvrvddtlITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 410 ---RTV-LISQ--EIHTFSGTLFDDVALGLA--GQAEDWPDERVRDavlaALERVGADwveqlphgvDTVVGRLGIRLSP 481
Cdd:PRK13649 82 qirKKVgLVFQfpESQLFEETVLKDVAFGPQnfGVSQEEAEALARE----KLALVGIS---------ESLFEKNPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 482 AQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR-GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGA 559
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGK 228
|
....*.
gi 488473579 560 PEQLRQ 565
Cdd:PRK13649 229 PKDIFQ 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
356-563 |
2.38e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 356 DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGHARTV-LISQEIHTFSG-TLF 426
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdgvdlshVPPYQRPInMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 427 DDVALGLagQAEDWPDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEA 505
Cdd:PRK11607 110 QNIAFGL--KQDKLPKAEIASRVNEMLGLVHmQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 506 TaeaGSSGATALDRAAAEAVR-----GRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK11607 177 M---GALDKKLRDRMQLEVVDilervGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
30-321 |
4.07e-16 |
|
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: 78.97 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDA--AKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESM 107
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 108 IA--VGLGL---DQQRVekaGTadLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVLL 176
Cdd:cd18544 81 FShiQRLPLsffDRTPV---GR--LVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWrlalisLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 177 agvlygLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENlRTRA---VANGSWQaiRWNLRGRFLGNT 253
Cdd:cd18544 156 ------LATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREK-REFEefdEINQEYR--KANLKSIKLFAL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 254 L--VVRLLAgeAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18544 227 FrpLVELLS--SLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
345-563 |
5.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.52 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDG-P---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-----TSG-------- 407
Cdd:PRK13634 3 ITFQKVEHRYQYKtPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgerviTAGkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 408 ---HARTVLISQEIHTFSGTLFDDVALGLA--GQAEDWPDERVRdavlAALERVGadwveqLPHgvdTVVGRLGIRLSPA 482
Cdd:PRK13634 83 lrkKVGIVFQFPEHQLFEETVEKDICFGPMnfGVSEEDAKQKAR----EMIELVG------LPE---ELLARSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 483 QAQQVALARALLADPPVIILDEATAeagssgatALD-RAAAEAV---------RGRTALVVAHRLSQVT-MADEVAVMDN 551
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTA--------GLDpKGRKEMMemfyklhkeKGLTTVLVTHSMEDAArYADQIVVMHK 221
|
250
....*....|..
gi 488473579 552 GRIVEVGAPEQL 563
Cdd:PRK13634 222 GTVFLQGTPREI 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
364-563 |
5.50e-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: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsghARTVLISQEIHTFS-------GTLFDDVALglagq 436
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL----GGEVLQDSARGIFLpphrrriGYVFQEARL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 437 aedWPDERVRDAVLAALERVGAdwvEQLPHGVDTVVGRLGI---------RLSPAQAQQVALARALLADPPVIILDEATA 507
Cdd:COG4148 89 ---FPHLSVRGNLLYGRKRAPR---AERRISFDEVVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473579 508 eagssgatALDRAAA-------EAVRGRTA---LVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG4148 163 --------ALDLARKaeilpylERLRDELDipiLYVSHSLDEVArLADHVVLLEQGRVVASGPLAEV 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-563 |
5.85e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 342 PTSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTL-------AALVAGLlepR-QGSITM--TSGHART 411
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLlrclnrmNDLIPGA---RvEGEILLdgEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 412 V----------LISQEIHTFSGTLFDDVALGL-----AGQAEdwPDERVRDAvlaaLERVGAdWveqlphgvDTVVGRL- 475
Cdd:COG1117 85 VdvvelrrrvgMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSE--LDEIVEES----LRKAAL-W--------DEVKDRLk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 476 --GIRLSPAQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV-------RGR-TALVVAHRLSQVT-MAD 544
Cdd:COG1117 150 ksALGLSGGQQQRLCIARALAVEPEVLLMDEPTS--------ALDPISTAKIeelilelKKDyTIVIVTHNMQQAArVSD 221
|
250
....*....|....*....
gi 488473579 545 EVAVMDNGRIVEVGAPEQL 563
Cdd:COG1117 222 YTAFFYLGELVEFGPTEQI 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
285-551 |
6.01e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.61 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 285 GAAATAVL--VLLRLFspvrFLLMFLNNLQAAWVCLQRVVGVIQARHDKPAVsERYQRGPT-----SIHVDQVSFGYQDG 357
Cdd:PTZ00265 321 GGSVISILlgVLISMF----MLTIILPNITEYMKSLEATNSLYEIINRKPLV-ENNDDGKKlkdikKIQFKNVRFHYDTR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 358 PDV--LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGH-----------ARTVLISQEIHTFSGT 424
Cdd:PTZ00265 396 KDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrSKIGVVSQDPLLFSNS 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LFDDVALGL-------------------------------AGQAEDWPD-----------------ERVRDAVLAALER- 455
Cdd:PTZ00265 476 IKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrAKCAGDLNDmsnttdsneliemrknyQTIKDSEVVDVSKk 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 456 -VGADWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSgATALDRAAAEAVRG---RTAL 531
Cdd:PTZ00265 556 vLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGnenRITI 634
|
330 340
....*....|....*....|
gi 488473579 532 VVAHRLSQVTMADEVAVMDN 551
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLSN 654
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
356-560 |
8.97e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 356 DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG----------HARTVLISQEI--HTfsg 423
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrHVNTVFQSYALfpHM--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALGLAGQ--AEDWPDERVRDAV-LAALErvgaDWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVI 500
Cdd:PRK09452 102 TVFENVAFGLRMQktPAAEITPRVMEALrMVQLE----EFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 501 ILDEATaeagssgaTALDRAAAEAVR----------GRTALVVAH-RLSQVTMADEVAVMDNGRIVEVGAP 560
Cdd:PRK09452 167 LLDESL--------SALDYKLRKQMQnelkalqrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-566 |
1.18e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 80.98 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 342 PTSIHVDQVSFGYQDG-PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsgHARTV-------- 412
Cdd:PTZ00243 1306 AGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV---NGREIgayglrel 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 -----LISQEIHTFSGTLFDDVALGL-AGQAEDWpdervrdavlAALERVGA-DWVEQLPHGVDTVVGRLGIRLSPAQAQ 485
Cdd:PTZ00243 1383 rrqfsMIPQDPVLFDGTVRQNVDPFLeASSAEVW----------AALELVGLrERVASESEGIDSRVLEGGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 486 QVALARALLA-DPPVIILDEATAEAGSsgatALDRAAAEAVR----GRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAP 560
Cdd:PTZ00243 1453 LMCMARALLKkGSGFILMDEATANIDP----ALDRQIQATVMsafsAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
....*....
gi 488473579 561 EQL---RQS 566
Cdd:PTZ00243 1529 RELvmnRQS 1537
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
30-321 |
1.36e-15 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 77.53 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 --VGLGLDQQRVEKAGtaDLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIRE 187
Cdd:cd18546 81 hlQRLSLDFHERETSG--RIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 188 FLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTL--VVRLLAgeAVA 265
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYfpGVELLG--NLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 266 TIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
360-558 |
1.41e-15 |
|
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: 75.78 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVLISQEIhtfsGTLFDDVALglagqaed 439
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-LFDGKPLDIAARNRI----GYLPEERGL-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 WPDERVRDAV--LAALERVGAdwvEQLPHGVDTVVGRLGIR---------LSPAQAQQVALARALLADPPVIILDEATae 508
Cdd:cd03269 82 YPKMKVIDQLvyLAQLKGLKK---EEARRRIDEWLERLELSeyankrveeLSKGNQQKVQFIAAVIHDPELLILDEPF-- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 509 agsSGataLDRAAAEAVR---------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVG 558
Cdd:cd03269 157 ---SG---LDPVNVELLKdvirelaraGKTVILSTHQMELVEeLCDRVLLLNKGRAVLYG 210
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
295-569 |
1.47e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.55 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 295 LRLFSPVRFLLMFLNNL--QA--AWVCLQRVVGVIQARHDKPAVSERYQRGPTSIHVDQVSFGYQDGPD--VLHTVSLDI 368
Cdd:PLN03130 561 LSLFAVLRFPLFMLPNLitQAvnANVSLKRLEELLLAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAErpTLSNINLDV 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 369 PAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGhaRTVLISQEIHTFSGTLFDDVALGLAGQAEDWpdERVRDA 448
Cdd:PLN03130 641 PVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG--TVAYVPQVSWIFNATVRDNILFGSPFDPERY--ERAIDV 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 449 vlAALERvgaDwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEA-TAEAGSSGATALDRAAAEAVRG 527
Cdd:PLN03130 717 --TALQH---D-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPlSALDAHVGRQVFDKCIKDELRG 790
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488473579 528 RTALVVA---HRLSQVtmaDEVAVMDNGRIVEVGAPEQLrQSDGP 569
Cdd:PLN03130 791 KTRVLVTnqlHFLSQV---DRIILVHEGMIKEEGTYEEL-SNNGP 831
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
364-563 |
1.49e-15 |
|
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: 79.46 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS---------ITMTS------GHARTVL--ISQEIHTFS-GTL 425
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnvrvgdewVDMTKpgpdgrGRAKRYIgiLHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDV--ALGLagqaeDWPDERVRDAVLAALERVGADWVEqlphgVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILD 503
Cdd:TIGR03269 383 LDNLteAIGL-----ELPDELARMKAVITLKMVGFDEEK-----AEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 504 EATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVGAPEQL 563
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEI 515
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
364-562 |
1.67e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--------TSGHART---VLISQE---IHTFsgTLFDDV 429
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdgkpvrirSPRDAIAlgiGMVHQHfmlVPNL--TVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLAGQAEDWPD-ERVRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILDEATA- 507
Cdd:COG3845 102 VLGLEPTKGGRLDrKAARARIRELSERYG------LDVDPDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAv 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 508 ----EAGSSGATaLDRAAAEavrGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQ 562
Cdd:COG3845 172 ltpqEADELFEI-LRRLAAE---GKSIIFITHKLREVmAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
29-321 |
1.87e-15 |
|
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: 77.07 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 29 YFIGAIVVItAASLLDLTVPVATGWIIDAAKAHRPT-SALLTPALVMAAAVIGSGICNGAAQSLtpsFFTT---IITRLR 104
Cdd:cd18541 1 YLLGILFLI-LVDLLQLLIPRIIGRAIDALTAGTLTaSQLLRYALLILLLALLIGIFRFLWRYL---IFGAsrrIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 105 ESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVLLAG 178
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPkltliaLLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 179 VLYglaIREFLRTAppvYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLR-----GRFlgnT 253
Cdd:cd18541 157 VYR---LGKKIHKR---FRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRlarvdALF---F 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 254 LVVRLLAGeaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18541 228 PLIGLLIG--LSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
345-551 |
3.16e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDV--LHTVSLDIPAGHTVVLVGESGAGKSTLAALV------------------------------- 391
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 392 ----AGLLEPRQGSITMTSGHARTV-----------------------------LISQEIHTFSGTLFDDVALGlagqAE 438
Cdd:PTZ00265 1246 eeqnVGMKNVNEFSLTKEGGSGEDStvfknsgkilldgvdicdynlkdlrnlfsIVSQEPMLFNMSIYENIKFG----KE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 439 DWPDERVRDAV-LAALErvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATAL 517
Cdd:PTZ00265 1322 DATREDVKRACkFAAID----EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270
....*....|....*....|....*....|....*.
gi 488473579 518 DRAAAEA--VRGRTALVVAHRLSQVTMADEVAVMDN 551
Cdd:PTZ00265 1398 EKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
295-573 |
3.35e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.25 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 295 LRLFSPVRFLLMFLNNLQA----AWVCLQRVVGVIQARHDKPAVSERYQRGPTSIHVDQVSFGYQDGPD--VLHTVSLDI 368
Cdd:PLN03232 561 LSLFAVLRSPLNMLPNLLSqvvnANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEI 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 369 PAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGhaRTVLISQEIHTFSGTLFDDVALGlagqaEDWPDERVRDA 448
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRG--SVAYVPQVSWIFNATVRENILFG-----SDFESERYWRA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 449 V-LAALERVgadwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGA-TALDRAAAEAVR 526
Cdd:PLN03232 714 IdVTALQHD----LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAhQVFDSCMKDELK 789
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488473579 527 GRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAAL 573
Cdd:PLN03232 790 GKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
364-563 |
3.42e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 77.38 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGL-----------------LEPRQGSITMtsghartVLISQEI--HTfsgT 424
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLeditsgdlfigekrmndVPPAERGVGM-------VFQSYALypHL---S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LFDDVALG--LAGQAEDWPDERVRDAvlaalervgADwVEQLPHGVDtvvgRLGIRLSPAQAQQVALARALLADPPVIIL 502
Cdd:PRK11000 92 VAENMSFGlkLAGAKKEEINQRVNQV---------AE-VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 503 DEATAEagssgataLDRAAAEAVR----------GRTALVVAHrlSQV---TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK11000 158 DEPLSN--------LDAALRVQMRieisrlhkrlGRTMIYVTH--DQVeamTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
30-321 |
3.84e-15 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. Moreover, 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: 349991 [Multi-domain] Cd Length: 298 Bit Score: 76.29 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDA------AKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRL 103
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 104 RESMIA----VGLG-LDQQrveKAGtaDLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAG 178
Cdd:cd18547 81 RKDLFEklqrLPLSyFDTH---SHG--DIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 179 VLYGLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLE-------NLRTRAVANGSWQAirwnlrgRFLG 251
Cdd:cd18547 156 PLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREeeaieefDEINEELYKASFKA-------QFYS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 252 NTL--VVRLLAgeAVATIGVAWTGYLLVTTDRLSVGaAATAVLVLLRLFS-PVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18547 229 GLLmpIMNFIN--NLGYVLVAVVGGLLVINGALTVG-VIQAFLQYSRQFSqPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-321 |
4.82e-15 |
|
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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 75.98 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIA 109
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 110 vglGLDQQRVE---KAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLH-----------PLFFVPVL 175
Cdd:cd18550 81 ---HLQRMSLAfftRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDwrlallslvllPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 176 LAGvlyglAIREFLRTAPPVYRAERNASTTQSqriLStIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTLV 255
Cdd:cd18550 158 RVG-----RRRRKLTREQQEKLAELNSIMQET---LS-VSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 256 VRLLAGEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18550 229 AALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-563 |
5.97e-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: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 349 QVSFGYQDGP-DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPR----QGSI--------TMTSGHARTV--- 412
Cdd:COG4172 13 SVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSIlfdgqdllGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 ---LISQE-------IHTFSGTLFDDVAL--GLAGQAedwpderVRDAVLAALERVG----ADWVEQLPHgvdtvvgrlg 476
Cdd:COG4172 93 riaMIFQEpmtslnpLHTIGKQIAEVLRLhrGLSGAA-------ARARALELLERVGipdpERRLDAYPH---------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 477 iRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALD---RAA-----AEAVR--GRTALVVAHRLSQVT-MADE 545
Cdd:COG4172 156 -QLSGGQRQRVMIAMALANEPDLLIADEPT--------TALDvtvQAQildllKDLQRelGMALLLITHDLGVVRrFADR 226
|
250
....*....|....*...
gi 488473579 546 VAVMDNGRIVEVGAPEQL 563
Cdd:COG4172 227 VAVMRQGEIVEQGPTAEL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
364-559 |
6.91e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTV----LISQEIHtfsgTLFDDVALGL-----A 434
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFgdysYRSQRIR----MIFQDPSTSLnprqrI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 435 GQAEDWP---------DERvRDAVLAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILD 503
Cdd:PRK15112 107 SQILDFPlrlntdlepEQR-EKQIIETLRQVGllPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 504 EATAEAGSSGATALDRAAAE--AVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGA 559
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLElqEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGS 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
33-314 |
7.01e-15 |
|
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: 75.29 E-value: 7.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIAVGL 112
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 113 GldqQRVE---KAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP-------LFFVPVLLAGVLYG 182
Cdd:cd18557 81 R---QEIAffdKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltlvllLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 183 LAIReflrtapPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENL----------------RTRAVANGSWQAIrwnlr 246
Cdd:cd18557 158 RYIR-------KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKeirrysealdrsyrlaRKKALANALFQGI----- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 247 GRFLGNtlvvrllageaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAA 314
Cdd:cd18557 226 TSLLIY-----------LSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
344-563 |
8.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGP----DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-----ITMTSG----HAR 410
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTvtvddITITHKtkdkYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 411 TV-----LISQ--EIHTFSGTLFDDVALGlaGQAEDWPDERVRDAVLAALERVG--ADWVEQLPhgvdtvvgrlgIRLSP 481
Cdd:PRK13646 82 PVrkrigMVFQfpESQLFEDTVEREIIFG--PKNFKMNLDEVKNYAHRLLMDLGfsRDVMSQSP-----------FQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 482 AQAQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQVT-MADEVAVMD 550
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTA--------GLDPQSKRQVmrllkslqtdENKTIILVSHDMNEVArYADEVIVMK 220
|
250
....*....|...
gi 488473579 551 NGRIVEVGAPEQL 563
Cdd:PRK13646 221 EGSIVSQTSPKEL 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
350-561 |
1.12e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDgpdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGhARTVLISQEIHTfsgtlfdDV 429
Cdd:PRK09544 12 VSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-LRIGYVPQKLYL-------DT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLAGQAEDWPDERVRDA-VLAALERVGADWVEQLPHGvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEATAE 508
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEdILPALKRVQAGHLIDAPMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 509 AGSSGATAL----DRAAAEAvrGRTALVVAHRLSQVtMA--DEVAVMdNGRIVEVGAPE 561
Cdd:PRK09544 151 VDVNGQVALydliDQLRREL--DCAVLMVSHDLHLV-MAktDEVLCL-NHHICCSGTPE 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
345-563 |
1.25e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.45 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-----TMTSGHARTV-----LI 414
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgePITKENIREVrkfvgLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQ--EIHTFSGTLFDDVALGLAGQAEDwpDERVRDAVLAALERVG-ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALAR 491
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLD--EETVAHRVSSALHMLGlEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 492 ALLADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-563 |
2.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPDV----LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGH----------- 408
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 409 ---ARTVLISQ--EIHTFSGTLFDDVALGLAGQAedWPDERVRDAVLAALERVGADwveqlphgvDTVVGRLGIRLSPAQ 483
Cdd:PRK13641 82 klrKKVSLVFQfpEAQLFENTVLKDVEFGPKNFG--FSEDEAKEKALKWLKKVGLS---------EDLISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 484 AQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR-GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPE 561
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPK 230
|
..
gi 488473579 562 QL 563
Cdd:PRK13641 231 EI 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
345-556 |
2.86e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTS------GHARTVLISQEI 418
Cdd:PRK11248 2 LQISHLYADYGGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 HTFSGTLFDDVALGLagQAEDWPDERVRDAVLAALERVGADWVEQlphgvdtvvgRLGIRLSPAQAQQVALARALLADPP 498
Cdd:PRK11248 81 LLPWRNVQDNVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAEK----------RYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 499 VIILDEATAeagssgatALDRAAAEAVR----------GRTALVVAHRLSQ-VTMADEVAVM--DNGRIVE 556
Cdd:PRK11248 149 LLLLDEPFG--------ALDAFTREQMQtlllklwqetGKQVLLITHDIEEaVFMATELVLLspGPGRVVE 211
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-565 |
3.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQ-DGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-------ITMTSGHARTVL 413
Cdd:PRK13643 2 IKFEKVNYTYQpNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdivVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEI---------HTFSGTLFDDVALGlaGQAEDWPDERVRDAVLAALERVG--ADWVEQLPhgvdtvvgrlgIRLSPA 482
Cdd:PRK13643 82 VRKKVgvvfqfpesQLFEETVLKDVAFG--PQNFGIPKEKAEKIAAEKLEMVGlaDEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 483 QAQQVALARALLADPPVIILDEATAeagssgatALD-RAAAEAVR--------GRTALVVAHRLSQVT-MADEVAVMDNG 552
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTA--------GLDpKARIEMMQlfesihqsGQTVVLVTHLMDDVAdYADYVYLLEKG 220
|
250
....*....|...
gi 488473579 553 RIVEVGAPEQLRQ 565
Cdd:PRK13643 221 HIISCGTPSDVFQ 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
365-563 |
3.50e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.68 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 365 SLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI--------TMTSGHARTVL---ISQEIHTFS----GTLFDDV 429
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiaKISDAELREVRrkkIAMVFQSFAlmphMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLagQAEDWPDERVRDAVLAALERVGadwVEQLPHGVDTvvgrlgiRLSPAQAQQVALARALLADPPVIILDEATAEA 509
Cdd:PRK10070 128 AFGM--ELAGINAEERREKALDALRQVG---LENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488473579 510 GSSGATAL--DRAAAEAVRGRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK10070 196 DPLIRTEMqdELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-535 |
1.09e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEI------ 418
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-SGHDITRLKNREVpflrrq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 --------HTF-SGTLFDDVALGL--AGQAEdwpdERVRDAVLAALERVG-ADWVEQLPhgvdtvvgrlgIRLSPAQAQQ 486
Cdd:PRK10908 81 igmifqdhHLLmDRTVYDNVAIPLiiAGASG----DDIRRRVSAALDKVGlLDKAKNFP-----------IQLSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR-GRTALVVAH 535
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
360-563 |
1.21e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.19 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMT---SGHA----------------------RTV-L 413
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyIGDKknnhelitnpyskkiknfkelrRRVsM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQ--EIHTFSGT-----LFDDVALGLagqaedwPDERVRDAVLAALERVGADwveqlphgvDTVVGRLGIRLSPAQAQQ 486
Cdd:PRK13631 121 VFQfpEYQLFKDTiekdiMFGPVALGV-------KKSEAKKLAKFYLNKMGLD---------DSYLERSPFGLSGGQKRR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 487 VALARALLADPPVIILDEATAEAGSSGATALDRAAAEA-VRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
324-562 |
1.22e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 324 VIQARHdkpaVSERYQRGPTSIHVDQVSFGYQDGPD-----VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPR 398
Cdd:COG1134 4 MIEVEN----VSKSYRLYHEPSRSLKELLLRRRRTRreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 399 QGSITmTSGHARTVLisqEIHT-------------FSGTLfddvaLGLAGQAedwPDERVRDAV-LAALERVgadwveql 464
Cdd:COG1134 80 SGRVE-VNGRVSALL---ELGAgfhpeltgreniyLNGRL-----LGLSRKE---IDEKFDEIVeFAELGDF-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 465 phgVDTVVGRL--G--IRLspaqaqqvALARALLADPPVIILDEATAeAGSSG--ATALDRAAAEAVRGRTALVVAHRLS 538
Cdd:COG1134 140 ---IDQPVKTYssGmrARL--------AFAVATAVDPDILLVDEVLA-VGDAAfqKKCLARIRELRESGRTVIFVSHSMG 207
|
250 260
....*....|....*....|....*
gi 488473579 539 QV-TMADEVAVMDNGRIVEVGAPEQ 562
Cdd:COG1134 208 AVrRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
98-537 |
1.31e-13 |
|
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: 74.18 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 98 TIITRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLA 177
Cdd:TIGR01271 955 TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPV 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 178 GVLYGLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFG----LENLRTRAVA--NGSW----QAIRWnlrg 247
Cdd:TIGR01271 1035 AVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGrqsyFETLFHKALNlhTANWflylSTLRW---- 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 248 rFLGNTLVVRLLAGEAVATIGVAWTGyllvttdrlsVGAAATAVLVLLRL--FSPVRFLLMFLNNLQAAWVCLQRVVGVI 325
Cdd:TIGR01271 1111 -FQMRIDIIFVFFFIAVTFIAIGTNQ----------DGEGEVGIILTLAMniLSTLQWAVNSSIDVDGLMRSVSRVFKFI 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 326 QARHDKPAVSER---YQRG--------------PTSIH--VDQVSFGY-QDGPDVLHTVSLDIPAGHTVVLVGESGAGKS 385
Cdd:TIGR01271 1180 DLPQEEPRPSGGggkYQLStvlvienphaqkcwPSGGQmdVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKS 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 386 TLAALVAGLLEPRQ---------GSITMTSGHARTVLISQEIHTFSGTLFDDValglaGQAEDWPDE---RVRDAVlaAL 453
Cdd:TIGR01271 1260 TLLSALLRLLSTEGeiqidgvswNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL-----DPYEQWSDEeiwKVAEEV--GL 1332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 454 ERVgadwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVV 533
Cdd:TIGR01271 1333 KSV----IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
....
gi 488473579 534 AHRL 537
Cdd:TIGR01271 1409 EHRV 1412
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-563 |
1.88e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 349 QVSFGyqdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLE----PRQGSITMTSGHA-----------RTVL 413
Cdd:PRK14247 10 KVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeARVSGEVYLDGQDifkmdvielrrRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQ---EIHTFSgtLFDDVALGLA----GQAEDWPDERVRDAvlaaLERVgadwveQLPHGVDTVVGRLGIRLSPAQAQQ 486
Cdd:PRK14247 87 VFQipnPIPNLS--IFENVALGLKlnrlVKSKKELQERVRWA----LEKA------QLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 487 VALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAArISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
364-563 |
1.99e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.66 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT--------MTSGHARTVliSQEIHT-FSG---------TL 425
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgMKDDEWRAV--RSDIQMiFQDplaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGLAGQAEDWPDERVRDAVLAALERVGAdwveqLPHgvdtVVGRLGIRLSPAQAQQVALARALLADPPVIILDEA 505
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLKVGL-----LPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 506 TaeagssgaTALDRA-AAEAVR---------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK15079 189 V--------SALDVSiQAQVVNllqqlqremGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-321 |
2.35e-13 |
|
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: 71.00 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSAL-----------LTPALVMAAAVIG----SGICNGAAQSLTPS 94
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLlglapllgpdpLALLLLAAAALVGiallRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 95 FFTTIITRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPV 174
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 175 LLAGVLYGLAIREF---LRTAPPVYRAERNASTTQSQRILSTIHgvdVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLG 251
Cdd:cd18564 161 LAVAPLLLLAARRFsrrIKEASREQRRREGALASVAQESLSAIR---VVQAFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 252 NTL--VVRLLagEAVATIGVAWTGYLLVTTDRLSVGaaatAVLV----LLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18564 238 ALLspVVDVL--VAVGTALVLWFGAWLVLAGRLTPG----DLLVflayLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-554 |
2.42e-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: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 341 GPTSIHVDQVSfgyqdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIht 420
Cdd:cd03215 1 GEPVLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-DGKPVTRRSPRDA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 fsgtlfddVALGLAGQAEDwpdeRVRDAVLaalervgadwveqLPHGVDTVVGrLGIRLSPAQAQQVALARALLADPPVI 500
Cdd:cd03215 73 --------IRAGIAYVPED----RKREGLV-------------LDLSVAENIA-LSSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 501 ILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQV-TMADEVAVMDNGRI 554
Cdd:cd03215 127 ILDEPTR--------GVDVGAKAEIyrlireladAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
345-567 |
2.56e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM-------TSGH--ARTVLI- 414
Cdd:COG4604 2 IEIKNVSKRYGGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvatTPSRelAKRLAIl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSG-TLFDDVALGlagqaeDWP---------DERVRDAVLAALErvgadwVEQLPHG-VDTvvgrlgirLSPAQ 483
Cdd:COG4604 81 RQENHINSRlTVRELVAFG------RFPyskgrltaeDREIIDEAIAYLD------LEDLADRyLDE--------LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 484 AQqvalaRALLA-----DPPVIILDEATaeagssgaTALD------------RAAAEavRGRTALVVAHRLSQV-TMADE 545
Cdd:COG4604 141 RQ-----RAFIAmvlaqDTDYVLLDEPL--------NNLDmkhsvqmmkllrRLADE--LGKTVVIVLHDINFAsCYADH 205
|
250 260
....*....|....*....|..
gi 488473579 546 VAVMDNGRIVEVGAPEQLRQSD 567
Cdd:COG4604 206 IVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-558 |
3.25e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 351 SFGyqdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVL------------ISQEI 418
Cdd:PRK09700 14 SFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI-NNINYNKLdhklaaqlgigiIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 ----------HTFSGTLFDDVALGLagQAEDWPDERVRDAVLaaLERVGadwveqLPHGVDTVVGRLGIrlspAQAQQVA 488
Cdd:PRK09700 90 svideltvleNLYIGRHLTKKVCGV--NIIDWREMRVRAAMM--LLRVG------LKVDLDEKVANLSI----SHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 489 LARALLADPPVIILDEATAEAGSSGATAL----DRAAAEavrGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLflimNQLRKE---GTAIVYISHKLAEIrRICDRYTVMKDGSSVCSG 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
357-563 |
3.40e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.78 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 357 GPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI--------TMTSGHARTVLISQeIHTFSGTLFDD 428
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidTARSLSQQKGLIRQ-LRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 VALglagqaedWPDERVRDAVLAalervGADWVEQLPHGVDTVVGR-----LGI---------RLSPAQAQQVALARALL 494
Cdd:PRK11264 94 FNL--------FPHRTVLENIIE-----GPVIVKGEPKEEATARARellakVGLagketsyprRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATaeagssgaTALD-----------RAAAEavRGRTALVVAHRLS-QVTMADEVAVMDNGRIVEVGAPEQ 562
Cdd:PRK11264 161 MRPEVILFDEPT--------SALDpelvgevlntiRQLAQ--EKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKA 230
|
.
gi 488473579 563 L 563
Cdd:PRK11264 231 L 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-551 |
3.47e-13 |
|
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: 67.56 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsGHARTVLISQEIHTFSGT 424
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-EGEDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LfddvalglagqaedwpdervRDAVLAALERVgadwveqlphgvdtvvgrlgirLSPAQAQQVALARALLADPPVIILDE 504
Cdd:cd03223 80 L--------------------REQLIYPWDDV----------------------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473579 505 ATaeagssgaTALD----RAAAEAVRGR-TALV-VAHRLSQVTMADEVAVMDN 551
Cdd:cd03223 118 AT--------SALDeeseDRLYQLLKELgITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-530 |
3.86e-13 |
|
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: 68.29 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 355 QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG--HARTVLISQEIHTFSGTLFDDVALG 432
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 433 LAGQAEDWPDERVRDAVLAALERVGADWVEQLPHGvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEATaeagss 512
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPT------ 153
|
170
....*....|....*...
gi 488473579 513 gaTALDRAAAEAVRGRTA 530
Cdd:cd03231 154 --TALDKAGVARFAEAMA 169
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
329-566 |
3.90e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 329 HDKPAVSERYQRGPTSIHVDQvsfgYQDGPDVL-HTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG 407
Cdd:PTZ00243 647 HEATPTSERSAKTPKMKTDDF----FELEPKVLlRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 408 HArtvLISQEIHTFSGTLFDDValgLAGQAEDwpDERVRDAV-LAALErvgADwVEQLPHGVDTVVGRLGIRLSPAQAQQ 486
Cdd:PTZ00243 723 IA---YVPQQAWIMNATVRGNI---LFFDEED--AARLADAVrVSQLE---AD-LAQLGGGLETEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 487 VALARALLADPPVIILDEATaeagssgaTALDRAAAE---------AVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEV 557
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPL--------SALDAHVGErvveecflgALAGKTRVLATHQVHVVPRADYVVALGDGRVEFS 862
|
....*....
gi 488473579 558 GAPEQLRQS 566
Cdd:PTZ00243 863 GSSADFMRT 871
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
360-555 |
4.61e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-------TMTSGHARTVLIsqeihtfsGTLFDDVALG 432
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvTKLPEYKRAKYI--------GRVFQDPMMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 433 LAGQ---AED--------------WP-DERVRDAVLAALERVGADwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALL 494
Cdd:COG1101 93 TAPSmtiEENlalayrrgkrrglrRGlTKKRRELFRELLATLGLG----LENRLDTKVG----LLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 495 ADPPVIILDEATAeagssgatALDRAAAEAV----------RGRTALVVAHRLSQ-VTMADEVAVMDNGRIV 555
Cdd:COG1101 165 TKPKLLLLDEHTA--------ALDPKTAALVleltekiveeNNLTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-544 |
5.06e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDG---PDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQG-------SITMTSGHARTVLI 414
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdvifngqPMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQE---IHTFSGTLFD-----DVALGL--AGQAEDWPDERVRDaVLAALervgadwveqlphGVDTVVGRLGIRLSPAQA 484
Cdd:PRK11629 86 NQKlgfIYQFHHLLPDftaleNVAMPLliGKKKPAEINSRALE-MLAAV-------------GLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 485 QQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEA-VRGRTA-LVVAH------RLS-QVTMAD 544
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAfLVVTHdlqlakRMSrQLEMRD 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-563 |
7.84e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 347 VDQVSFGYQDGPD---VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLL-----EPRQGSITMTSG---HA------ 409
Cdd:PRK15134 8 IENLSVAFRQQQTvrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGEsllHAseqtlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 410 -----RTVLISQE-------IHTFSGTLFDDVAL--GLAGQAedwpderVRDAVLAALERVG----ADWVEQLPHgvdtv 471
Cdd:PRK15134 88 gvrgnKIAMIFQEpmvslnpLHTLEKQLYEVLSLhrGMRREA-------ARGEILNCLDRVGirqaAKRLTDYPH----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 472 vgrlgiRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALDRAA--------AEAVR--GRTALVVAHRLSQV- 540
Cdd:PRK15134 156 ------QLSGGERQRVMIAMALLTRPELLIADEPT--------TALDVSVqaqilqllRELQQelNMGLLFITHNLSIVr 221
|
250 260
....*....|....*....|...
gi 488473579 541 TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK15134 222 KLADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
339-569 |
1.09e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.64 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 339 QRGPTSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI--------TMTSGHAR 410
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgenipAMSRSRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 411 TVLISQEIHTFSGTLF------DDVALGLAGQAEdWPDERVRDAVLAALERVGADWVEQLphgvdtvvgrLGIRLSPAQA 484
Cdd:PRK11831 81 TVRKRMSMLFQSGALFtdmnvfDNVAYPLREHTQ-LPAPLLHSTVMMKLEAVGLRGAAKL----------MPSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 485 QQVALARALLADPPVIILDEATAEAGSSGATALDRAAAE--AVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPE 561
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQ 229
|
....*...
gi 488473579 562 QLRQSDGP 569
Cdd:PRK11831 230 ALQANPDP 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-506 |
1.11e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 341 GPTSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsGHarTVLI---SQE 417
Cdd:COG0488 312 GKKVLELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GE--TVKIgyfDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 IHTFSgtlfddvalglagqaedwPDERVRDavlaALERVGADWVEQLPHGvdtVVGRLGirLSPAQAQQ----------- 486
Cdd:COG0488 387 QEELD------------------PDKTVLD----ELRDGAPGGTEQEVRG---YLGRFL--FSGDDAFKpvgvlsggeka 439
|
170 180
....*....|....*....|.
gi 488473579 487 -VALARALLADPPVIILDEAT 506
Cdd:COG0488 440 rLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-314 |
1.14e-12 |
|
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: 69.13 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTP---------------ALVMAAAVIGSGICNGAAQSLTPS 94
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPaslgpadprgqlwllGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 95 FFTTIITRLR----ESMIAVGLGL--DQQrvekagTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP 168
Cdd:cd18565 81 FAQRVQHDLRtdtyDHVQRLDMAFfeDRQ------TGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 169 ------LFFVPVLLAGVLYglaireFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGS----- 237
Cdd:cd18565 155 qlalvaLLPVPLIIAGTYW------FQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASeeyrd 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 238 --WQAIRwnLRGRFlgnTLVVRLLAGEA-VATIGVAwtGYLLVT-----TDRLSVGAAATAVLVLLRLFSPVRFLLMFLN 309
Cdd:cd18565 229 anWRAIR--LRAAF---FPVIRLVAGAGfVATFVVG--GYWVLDgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLID 301
|
....*
gi 488473579 310 NLQAA 314
Cdd:cd18565 302 QYQRA 306
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
364-564 |
1.51e-12 |
|
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: 67.01 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGH-----ARTV-----LISQEIHTFSG-TLFDDVAL- 431
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-AGHdvvrePREVrrrigIVFQDLSVDDElTGWENLYIh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 -GLAGQAEDWPDERVrDAVLAALERvgADWVEQLphgVDTVVGRLGIRLSpaqaqqvaLARALLADPPVIILDEATaeag 510
Cdd:cd03265 98 aRLYGVPGAERRERI-DELLDFVGL--LEAADRL---VKTYSGGMRRRLE--------IARSLVHRPEVLFLDEPT---- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 511 ssgaTALDRAAAEAV----------RGRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVGAPEQLR 564
Cdd:cd03265 160 ----IGLDPQTRAHVweyieklkeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
356-535 |
1.67e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 356 DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV--LISQEIHTFS------GTLfd 427
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrdEPHENILYLGhlpglkPEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 428 DVALGLAGQAEDWPDERVrdAVLAALERVGADWVEQLPHGvdtvvgrlgiRLSPAQAQQVALARALLADPPVIILDEATa 507
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQR--TIEDALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPT- 155
|
170 180
....*....|....*....|....*...
gi 488473579 508 eagssgaTALDRAaaeAVRGRTALVVAH 535
Cdd:TIGR01189 156 -------TALDKA---GVALLAGLLRAH 173
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
344-561 |
1.84e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVL---------I 414
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvpQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIH-TFSGTLFDDVALGLAGQAeDW---PDERVRDAVLAALERVGadwVEQLPHgvdtvvgRLGIRLSPAQAQQVALA 490
Cdd:PRK15056 86 SEEVDwSFPVLVEDVVMMGRYGHM-GWlrrAKKRDRQIVTAALARVD---MVEFRH-------RQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 491 RALLADPPVIILDEA-TAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPE 561
Cdd:PRK15056 155 RAIAQQGQVILLDEPfTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
360-536 |
2.22e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVLISQEIHtFSG---------TLFDDVA 430
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH-YLGhrnamkpalTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 431 L--GLAGQAEDWPDervrdavlAALERVGADWVEQLPHGVdtvvgrlgirLSPAQAQQVALARALLADPPVIILDEATAe 508
Cdd:PRK13539 96 FwaAFLGGEELDIA--------AALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA- 156
|
170 180
....*....|....*....|....*...
gi 488473579 509 agssgatALDRAAAEAVrgrTALVVAHR 536
Cdd:PRK13539 157 -------ALDAAAVALF---AELIRAHL 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
361-556 |
2.24e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI-----------TMTSGHARTVLISQEIHTFSG-TLFDD 428
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrfasTTAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 VALGLAGQAEDWPDER-VRDAVLAALERVGADWVEQLPhgvdtvVGRLGIrlspAQAQQVALARALLADPPVIILDEATA 507
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRlLNYEAREQLEHLGVDIDPDTP------LKYLSI----GQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473579 508 EAGSSGATALDRAAAE-AVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVE 556
Cdd:PRK11288 170 SLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
352-560 |
2.67e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 352 FGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHA-----RTVL-ISQEIHT----- 420
Cdd:PRK13638 9 FRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPldyskRGLLaLRQQVATvfqdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 ----FSGTLFDDVALGLA--GQAEDWPDERVRDavlaALERVGADWVEQLPhgvdtvvgrlgIR-LSPAQAQQVALARAL 493
Cdd:PRK13638 87 eqqiFYTDIDSDIAFSLRnlGVPEAEITRRVDE----ALTLVDAQHFRHQP-----------IQcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 494 LADPPVIILDEATA---EAGSSGATALDRAAAEavRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAP 560
Cdd:PRK13638 152 VLQARYLLLDEPTAgldPAGRTQMIAIIRRIVA--QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAP 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
364-563 |
3.73e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT------MTSGHARTVLISQEI--------------HTFSG 423
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdlLKADPEAQKLLRQKIqivfqnpygslnprKKVGQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALGLAGQAEdwpdERvRDAVLAALERVG--ADWVEQLPHgvdtvvgrlgiRLSPAQAQQVALARALLADPPVII 501
Cdd:PRK11308 114 ILEEPLLINTSLSAA----ER-REKALAMMAKVGlrPEHYDRYPH-----------MFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 502 LDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK11308 178 ADEPV--------SALDVSVQAQVlnlmmdlqqeLGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-566 |
3.94e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.04 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 357 GPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEP----RQGSITMTSGHA------------RTVLISQEIHT 420
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyRYSGDVLLGGRSifnyrdvlefrrRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSGTLFDDVALGLAGQaEDWPDERVRDAVLAALERVGAdWveqlphgvDTVVGRLG---IRLSPAQAQQVALARALLADP 497
Cdd:PRK14271 113 FPMSIMDNVLAGVRAH-KLVPRKEFRGVAQARLTEVGL-W--------DAVKDRLSdspFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 498 PVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQS 566
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAArISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
361-563 |
4.21e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALV--AGLLEPR---QGSITMtSGH------ARTVLISQEI-------HTFS 422
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVY-NGHniysprTDTVDLRKEIgmvfqqpNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 GTLFDDVALGLAGQAEDwpDERVRDAVLAALERVGADWVEQLPHGVDTVVGrlgirLSPAQAQQVALARALLADPPVIIL 502
Cdd:PRK14239 100 MSIYENVVYGLRLKGIK--DKQVLDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 503 DEATaeagssgaTALDRAAAEAVRGR--------TALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK14239 173 DEPT--------SALDPISAGKIEETllglkddyTMLLVTRSMQQASrISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
364-564 |
4.35e-12 |
|
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: 65.60 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--TSGHARTVLISQEIhtfsG------TLFDDV----AL 431
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIngYSIRTDRKAARQSL----GycpqfdALFDELtvreHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 GLAGQAEDWPDERVRDAVLAALERVGadwveqLPHGVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILDEATaeags 511
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVELLLRVLG------LTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPT----- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 512 sgaTALD--------RAAAEAVRGRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVGAPEQLR 564
Cdd:cd03263 162 ---SGLDpasrraiwDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQELK 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
359-563 |
4.40e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 359 DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTV-----------------------LIS 415
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknqlrllrtrltMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFSG-TLFDDV------ALGLAGQaedwpdeRVRDAVLAALERVGADWVEQlphgvdtvvGRLGIRLSPAQAQQVA 488
Cdd:PRK10619 99 QHFNLWSHmTVLENVmeapiqVLGLSKQ-------EARERAVKYLAKVGIDERAQ---------GKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 489 LARALLADPPVIILDEATaeagssgaTALD-RAAAEAVR--------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVG 558
Cdd:PRK10619 163 IARALAMEPEVLLFDEPT--------SALDpELVGEVLRimqqlaeeGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEG 234
|
....*
gi 488473579 559 APEQL 563
Cdd:PRK10619 235 APEQL 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
361-563 |
4.65e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEP---RQGSITMtSGHARTvliSQEIHTFSGTLF-DDVALG---- 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLL-NGMPID---AKEMRAISAYVQqDDLFIPtltv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 433 ---LAGQA-----EDWPDERVRDAVLAALERVGadwveqLPHGVDTVVGRLGIR--LSPAQAQQVALARALLADPPVIIL 502
Cdd:TIGR00955 117 rehLMFQAhlrmpRRVTKKEKRERVDEVLQALG------LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 503 DEATaeagssgaTALDRAAAEAV---------RGRTALVVAHRLSQVTMA--DEVAVMDNGRIVEVGAPEQL 563
Cdd:TIGR00955 191 DEPT--------SGLDSFMAYSVvqvlkglaqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
345-553 |
5.35e-12 |
|
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: 63.62 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmTSGHARTVLISQeihtFSGt 424
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTVKIGYFEQ----LSG- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 lfddvalGlagqaedwpdERVRdavlaalervgadwveqlphgvdtvvgrlgirlspaqaqqVALARALLADPPVIILDE 504
Cdd:cd03221 74 -------G----------EKMR----------------------------------------LALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 505 ATaeagssgaTALDRAAAEAVRG------RTALVVAH-R--LSQVtmADEVAVMDNGR 553
Cdd:cd03221 97 PT--------NHLDLESIEALEEalkeypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-567 |
1.05e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGyqdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIHTFSGTLFDDV 429
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLAGQAE--------------DWPDERVRDAVLAALERVgadwveqlphGVDTVVGRLGIRLSPAQAQQVALARALLA 495
Cdd:PRK09536 87 SLSFEFDVRqvvemgrtphrsrfDTWTETDRAAVERAMERT----------GVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 496 DPPVIILDEATAEAGSSGAT-ALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
355-554 |
1.36e-11 |
|
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: 65.26 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 355 QDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrQGSITMTSGHARTV----------LISQEIHTFSGT 424
Cdd:cd03289 14 EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVplqkwrkafgVIPQKVFIFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 LFDDvaLGLAGQaedWPDERVrdavLAALERVGADWV-EQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILD 503
Cdd:cd03289 93 FRKN--LDPYGK---WSDEEI----WKVAEEVGLKSViEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473579 504 EATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRI 554
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
360-552 |
1.88e-11 |
|
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: 64.88 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsghARTVLISQEIHTFSGTLFDDVALGLAgqaed 439
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS---GRISFSSQFSWIMPGTIKENIIFGVS----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 WPDERVRDAVLAA-LErvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARAL-------LADPPVIILDEATAEags 511
Cdd:cd03291 124 YDEYRYKSVVKACqLE----EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVykdadlyLLDSPFGYLDVFTEK--- 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488473579 512 sgaTALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNG 552
Cdd:cd03291 197 ---EIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
359-558 |
2.14e-11 |
|
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: 63.83 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 359 DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGllepRQGSITMTSGHartVLISQE---IHTFS-----GTLFDDVA 430
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG----RVEGGGTTSGQ---ILFNGQprkPDQFQkcvayVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 431 LGL---------------AGQAEDWPDERVRDAVL--AALERVGADWVEQlphgvdtvvgrlgirLSPAQAQQVALARAL 493
Cdd:cd03234 94 PGLtvretltytailrlpRKSSDAIRKKRVEDVLLrdLALTRIGGNLVKG---------------ISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 494 LADPPVIILDEATAEAGSSGATALDRAAAE-AVRGRTALVVAH--RLSQVTMADEVAVMDNGRIVEVG 558
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
345-546 |
2.69e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVsfGYQ-DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVL--------IS 415
Cdd:PRK10247 8 LQLQNV--GYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-LFEGEDISTLkpeiyrqqVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHT---FSGTLFDDVAL--GLAGQAedwPDErvrDAVLAALERVGadwveqLPhgvDTVVGRLGIRLSPAQAQQVALA 490
Cdd:PRK10247 85 YCAQTptlFGDTVYDNLIFpwQIRNQQ---PDP---AIFLDDLERFA------LP---DTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 491 RALLADPPVIILDEATaeagssgaTALDRAAAEAV----------RGRTALVVAHRLSQVTMADEV 546
Cdd:PRK10247 150 RNLQFMPKVLLLDEIT--------SALDESNKHNVneiihryvreQNIAVLWVTHDKDEINHADKV 207
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-321 |
2.98e-11 |
|
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: 64.48 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAK-AHRPTSALLTPALVMAAAVIGSGICNGAA-------------------- 88
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRiylnhvaeqkvvadlrsdly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 89 ---QSLTPSFFttiitrlresmiavglglDQQRvekagTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALAS 165
Cdd:cd18778 81 dklQRLSLRYF------------------DDRQ-----TGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 166 LHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNL 245
Cdd:cd18778 138 INPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 246 RGRFLGNTL--VVRLLAgeAVATIGVAWTGYLLVTTDRLSVGaAATAVLVLLRLF-SPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18778 218 RAMKLWAIFhpLMEFLT--SLGTVLVLGFGGRLVLAGELTIG-DLVAFLLYLGLFyEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
33-285 |
4.66e-11 |
|
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: 64.04 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLR----ESMI 108
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRkdlyRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 109 AVGLG-LDQQRVekagtADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVL-LAGVL 180
Cdd:cd18576 81 RLPLSfFHERRV-----GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltllmLATVPVVvLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 181 YGLAIREFLRtappvyraERNASTTQSQRILS-TIHGVDVVRAF---GLENLRTRAVANGSWQAIRWNLRGRFLGNTLVV 256
Cdd:cd18576 156 FGRRIRKLSK--------KVQDELAEANTIVEeTLQGIRVVKAFtreDYEIERYRKALERVVKLALKRARIRALFSSFII 227
|
250 260
....*....|....*....|....*....
gi 488473579 257 RLLAGeavATIGVAWTGYLLVTTDRLSVG 285
Cdd:cd18576 228 FLLFG---AIVAVLWYGGRLVLAGELTAG 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-566 |
5.43e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 354 YQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsghARTVLISQEIHTFSGTLFDDVALGL 433
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD---GKVLYFGKDIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 434 AGQAEDWPDERVRDAVLAALERVGADWVEQLPHGVDTVVGRLGI-------------RLSPAQAQQVALARALLADPPVI 500
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevydrlnspasQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473579 501 ILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQS 566
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
124-321 |
5.45e-11 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. 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. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 63.62 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 124 TADLVSRASDdVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRtapPVYRAER--- 200
Cdd:cd18570 98 TGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNK---PFKKKNRevm 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 201 -NASTTQSQrILSTIHGVDVVRAFGLENL-------RTRAVANGSWQAIRWNLRGRFLGNTLvvrllagEAVATIGVAWT 272
Cdd:cd18570 174 eSNAELNSY-LIESLKGIETIKSLNAEEQflkkiekKFSKLLKKSFKLGKLSNLQSSIKGLI-------SLIGSLLILWI 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473579 273 GYLLVTTDRLSVGA--AATAVLVLlrLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18570 246 GSYLVIKGQLSLGQliAFNALLGY--FLGPIENLINLQPKIQEAKVAADRL 294
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
360-573 |
7.50e-11 |
|
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: 65.32 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsghARTVLISQEIHTFSGTLFDDVALGLAgqaed 439
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS---GRISFSPQTSWIMPGTIKDNIIFGLS----- 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 WPDERVRDAVLAA-LErvgaDWVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDeataeagsSGATALD 518
Cdd:TIGR01271 513 YDEYRYTSVIKACqLE----EDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLD--------SPFTHLD 580
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 519 ---------RAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVGAPEQLRQSDGPFAAL 573
Cdd:TIGR01271 581 vvtekeifeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
100-566 |
7.77e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 100 ITRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTA-----VRdaangaLPRLVNTMIMVIVSVGALASLHP-LFFVP 173
Cdd:PRK10522 80 VYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNitiafVR------LPELVQGIILTLGSAAYLAWLSPkMLLVT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 174 VLLAGVLY---GLAIREflrtappVYRAERNASTTQS------QRILstihgvDVVRAFGLENLRTRAVANGSWQA---- 240
Cdd:PRK10522 154 AIWMAVTIwggFVLVAR-------VYKHMATLRETEDklyndyQTVL------EGRKELTLNRERAEYVFENEYEPdaqe 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 241 -----IRWNLRGRFLGNTLVVRLLAgeavaTIGVAWtgYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAW 315
Cdd:PRK10522 221 yrhhiIRADTFHLSAVNWSNIMMLG-----AIGLVF--YMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 316 VCLQRVVGVIQA--RHD--KPAVSERYQRgptsIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALV 391
Cdd:PRK10522 294 VAFNKLNKLALApyKAEfpRPQAFPDWQT----LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 392 AGLLEPRQGSI-------TMTSGHARTVLISQEIHTFSgtLFDDValgLAGQAEDWPDERVrdavlaalervgADWVEQL 464
Cdd:PRK10522 370 TGLYQPQSGEIlldgkpvTAEQPEDYRKLFSAVFTDFH--LFDQL---LGPEGKPANPALV------------EKWLERL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 465 --PHGVDTVVGRL-GIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQ 539
Cdd:PRK10522 433 kmAHKLELEDGRIsNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHY 512
|
490 500
....*....|....*....|....*..
gi 488473579 540 VTMADEVAVMDNGRIVEVGAPEQLRQS 566
Cdd:PRK10522 513 FIHADRLLEMRNGQLSELTGEERDAAS 539
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
345-560 |
7.89e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.10 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGY-QDGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSiTMTSGHA----------- 409
Cdd:PRK13645 7 IILDNVSYTYaKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAipanlkkikev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 410 ----RTV-LISQ--EIHTFSGTLFDDVALGLAGQAEDwpDERVRDAVLAALERVgadwveQLPhgvDTVVGRLGIRLSPA 482
Cdd:PRK13645 86 krlrKEIgLVFQfpEYQLFQETIEKDIAFGPVNLGEN--KQEAYKKVPELLKLV------QLP---EDYVKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 483 QAQQVALARALLADPPVIILDEATAEAGSSGA----TALDRAAAEavRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEV 557
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKE--YKKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232
|
...
gi 488473579 558 GAP 560
Cdd:PRK13645 233 GSP 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-563 |
1.49e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 318 LQRVVGVIQARHDKPAVSERYQRG-------------PTSIHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGK 384
Cdd:PRK13536 2 LTRAVAEEAPRRLELSPIERKHQGiseakasipgsmsTVAIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 385 STLAALVAGLLEPRQGSITM---------TSGHARTVLISQeihtfsgtlFDDVAlglagqaedwPDERVRDAVLA---- 451
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVlgvpvparaRLARARIGVVPQ---------FDNLD----------LEFTVRENLLVfgry 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 452 ------ALERVGADWVE--QLPHGVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALD----- 518
Cdd:PRK13536 142 fgmstrEIEAVIPSLLEfaRLESKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPT--------TGLDpharh 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488473579 519 ----RAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK13536 210 liweRLRSLLARGKTILLTTHFMEEAErLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
363-567 |
1.66e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 363 TVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSgharTVLISQEIHTF-------SGTLFDDVALglag 435
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG----RVLFDAEKGIClppekrrIGYVFQDARL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 436 qaedWPDERVRDAVLAALERVGA----DWVEQLphGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAeags 511
Cdd:PRK11144 88 ----FPHYKVRGNLRYGMAKSMVaqfdKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA---- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 512 sgatALDraaaeAVRGRTALVVAHRLSQ--------VT--------MADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:PRK11144 158 ----SLD-----LPRKRELLPYLERLAReinipilyVShsldeilrLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
344-506 |
1.74e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGyqDGPDVLHTvSLDIPAGHTVVLVGESGAGKSTLAALVAGlleprqgSITMTSGHartVLISQEI----- 418
Cdd:PRK11147 5 SIHGAWLSFS--DAPLLDNA-ELHIEDNERVCLVGRNGAGKSTLMKILNG-------EVLLDDGR---IIYEQDLivarl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 -----HTFSGTLFDDVALGLAGQAE-------------DWPDERVrdavLAALERVGAD------WveQLPHGVDTVVGR 474
Cdd:PRK11147 72 qqdppRNVEGTVYDFVAEGIEEQAEylkryhdishlveTDPSEKN----LNELAKLQEQldhhnlW--QLENRINEVLAQ 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 488473579 475 LGI-------RLSPAQAQQVALARALLADPPVIILDEAT 506
Cdd:PRK11147 146 LGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPT 184
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
354-560 |
2.06e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 354 YQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGL-----------------LEPRQGSITMtsghartvlisq 416
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLeritsgeiwiggrvvneLEPADRDIAM------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 417 eihTFSG-------TLFDDVALGL--AGQAEDWPDERVRDAVlAALErvgadwVEQLPHgvdtvvgRLGIRLSPAQAQQV 487
Cdd:PRK11650 81 ---VFQNyalyphmSVRENMAYGLkiRGMPKAEIEERVAEAA-RILE------LEPLLD-------RKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 488 ALARALLADPPVIILDEATAEagssgataLD---RAA--AEAVR-----GRTALVVAHrlSQV---TMADEVAVMDNGRI 554
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSN--------LDaklRVQmrLEIQRlhrrlKTTSLYVTH--DQVeamTLADRVVVMNGGVA 213
|
....*.
gi 488473579 555 VEVGAP 560
Cdd:PRK11650 214 EQIGTP 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-555 |
2.49e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 357 GPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtsgHARTVLIsqeihtfsGTLFDDVALGLAGQ 436
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL---DGKPVRI--------RSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 437 AED------WPDERVRD-AVLAALERVGADWVeqLPHG-----VDTVVGRLGIRL-SPAQA--------QQ-VALARALL 494
Cdd:COG1129 333 PEDrkgeglVLDLSIREnITLASLDRLSRGGL--LDRRreralAEEYIKRLRIKTpSPEQPvgnlsggnQQkVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 495 ADPPVIILDEATAeagssG----ATA-----LDRAAAEavrGRTALVVAHRLSQV-TMADEVAVMDNGRIV 555
Cdd:COG1129 411 TDPKVLILDEPTR-----GidvgAKAeiyrlIRELAAE---GKAVIVISSELPELlGLSDRILVMREGRIV 473
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
360-526 |
2.70e-10 |
|
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: 60.53 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTvlisqeihtfsgtlfdDVAlglagQAED 439
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWV----------------DLA-----QASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 440 WPDERVRDAV-------LAALERVGA-DWVEQ--LPHGVD---------TVVGRLGI-----RLSPA-----QAQQVALA 490
Cdd:COG4778 85 REILALRRRTigyvsqfLRVIPRVSAlDVVAEplLERGVDreearararELLARLNLperlwDLPPAtfsggEQQRVNIA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 488473579 491 RALLADPPVIILDEATAeagssgatALDRAAAEAVR 526
Cdd:COG4778 165 RGFIADPPLLLLDEPTA--------SLDAANRAVVV 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-563 |
3.02e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQgsITMTSGHARTV-------------------LISQEIHT 420
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE--EARVEGEVRLFgrniyspdvdpievrrevgMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSG-TLFDDVALGLA----GQAEDWPDERVRDAVLAAlervgADWveqlphgvDTVVGRLG---IRLSPAQAQQVALARA 492
Cdd:PRK14267 97 FPHlTIYDNVAIGVKlnglVKSKKELDERVEWALKKA-----ALW--------DEVKDRLNdypSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 493 LLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAArVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
356-565 |
3.22e-10 |
|
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: 59.85 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 356 DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGL--LEPRQGSItmtsghartvlisqeihtfsgtLFDDVALgl 433
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI----------------------LFKGEDI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 434 agqAEDWPDERVRDAVLAALervgadwveQLP---HGV--DTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEAtae 508
Cdd:cd03217 67 ---TDLPPEERARLGIFLAF---------QYPpeiPGVknADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP--- 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 509 agSSGataLD----RAAAEAVR-----GRTALVVAH--RLSQVTMADEVAVMDNGRIVEVGAPEQLRQ 565
Cdd:cd03217 132 --DSG---LDidalRLVAEVINklreeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
359-558 |
4.06e-10 |
|
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: 59.49 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 359 DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgsiTMTSGharTVLI---SQEIHTFSGtlfddvALGLAG 435
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTG-----LGVSG---EVLIngrPLDKRSFRK------IIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 436 QaED--WPDERVRDAVLAALErvgadwveqlphgvdtvvgrlgIR-LSPAQAQQVALARALLADPPVIILDEATaeAGSS 512
Cdd:cd03213 89 Q-DDilHPTLTVRETLMFAAK----------------------LRgLSGGERKRVSIALELVSNPSLLFLDEPT--SGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488473579 513 GATALDRAA---AEAVRGRTALVVAHRLSQVT--MADEVAVMDNGRIVEVG 558
Cdd:cd03213 144 SSSALQVMSllrRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
365-535 |
6.74e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 6.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 365 SLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvLISQEIHTFSGTLFDDVA-LG-LAG-QAEDWP 441
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL---------WQGEPIRRQRDEYHQDLLyLGhQPGiKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 442 DERVR-----------DAVLAALERVGADWVEQLPHGVdtvvgrlgirLSPAQAQQVALARALLADPPVIILDEATaeag 510
Cdd:PRK13538 92 LENLRfyqrlhgpgddEALWEALAQVGLAGFEDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPF---- 157
|
170 180
....*....|....*....|....*
gi 488473579 511 ssgaTALDRAAAEAVrgrTALVVAH 535
Cdd:PRK13538 158 ----TAIDKQGVARL---EALLAQH 175
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
30-321 |
6.83e-10 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. Moreover, 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: 349992 [Multi-domain] Cd Length: 292 Bit Score: 60.49 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQsltpsFFTTII-----TRLR 104
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAG-----YFAAKAsqgfgRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 105 ESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVLLAG 178
Cdd:cd18548 76 KDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPklalilLVAIPILALV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 179 VLYglaireFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTR--AVANGSWQAIrwNLR-GRFLGNTL- 254
Cdd:cd18548 156 VFL------IMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEErfDKANDDLTDT--SLKaGRLMALLNp 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488473579 255 VVRLLAGeaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18548 228 LMMLIMN--LAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
360-555 |
7.06e-10 |
|
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: 59.65 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM--------TSGHARTVlisqeihtfsGTLFddval 431
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwkrRKKFLRRI----------GVVF----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 glaGQAED-WPDERVRD--AVLAALERVGAD--------WVE--QLPHGVDTVVgRlgiRLSPAQAQQVALARALLADPP 498
Cdd:cd03267 101 ---GQKTQlWWDLPVIDsfYLLAAIYDLPPArfkkrldeLSEllDLEELLDTPV-R---QLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 499 VIILDEATaeagssgaTALDRAAAEAVR----------GRTALVVAHRLSQVT-MADEVAVMDNGRIV 555
Cdd:cd03267 174 ILFLDEPT--------IGLDVVAQENIRnflkeynrerGTTVLLTSHYMKDIEaLARRVLVIDKGRLL 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-563 |
9.13e-10 |
|
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: 61.36 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGL--LEPRQGSITMTSGHARTVLISqEIHTFS 422
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYV-ERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 GTLFDDVALGLAGQAED--------------------------WPDERVRDAVLAALERVGADWVEQLPHGVDTV-VGRL 475
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEVDfwnlsdklrrrirkriaimlqrtfalYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIeMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 476 GIR-------LSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGR-TALVVAHRLSQVT--MADE 545
Cdd:TIGR03269 159 SHRithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVIedLSDK 238
|
250
....*....|....*...
gi 488473579 546 VAVMDNGRIVEVGAPEQL 563
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
357-567 |
1.08e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 357 GPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHART------------VLISQEIHTFSG- 423
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI-GGNPCArltpakahqlgiYLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALGLAGQAEdwpDERVRDAVLAALErvgadwvEQLphGVDTVVGRLGIrlspAQAQQVALARALLADPPVIILD 503
Cdd:PRK15439 102 SVKENILFGLPKRQA---SMQKMKQLLAALG-------CQL--DLDSSAGSLEV----ADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 504 EATAEAGSSGATAL-DRAAAEAVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:PRK15439 166 EPTASLTPAETERLfSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
352-552 |
1.69e-09 |
|
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: 58.11 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 352 FGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI--------------TMTSGHARTVLISQE 417
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeaTRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 418 IHTFSGTLFDDVALGLagqaedwPDERVRDAVLAALERVGADwVEQLPHGVDTVVGRLGIRLSPAQAQQVALARALLADP 497
Cdd:cd03290 88 PWLLNATVEENITFGS-------PFNKQRYKAVTDACSLQPD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 498 PVIILDEATaeagssgaTALDRAAAEAVR-----------GRTALVVAHRLSQVTMADEVAVMDNG 552
Cdd:cd03290 160 NIVFLDDPF--------SALDIHLSDHLMqegilkflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
30-301 |
1.95e-09 |
|
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: 58.81 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIIDAAKAHR--PTSALLTPALVMAAAVIGSGICNGAAQSLtpsFFTT---IITRLR 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGdpETQALNVYSLALLLLGLAQFILSFLQSYL---LNHTgerLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 105 ESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLA 184
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 185 IREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLE--------NLRTRAVANGSWQAIRWNL---RGRFLGNT 253
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREeyelekydKALEEALKAGIKKAVANGLsfgITQFIGYL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488473579 254 LVVrllageavatiGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPV 301
Cdd:pfam00664 238 SYA-----------LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
362-563 |
2.66e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 362 HTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgSITMTSGHARTVLISQEIHTFSGTL-----------FDDV- 429
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA---GVRQTAGRVLLDGKPVAPCALRGRKiatimqnprsaFNPLh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 -----------ALGLAGqaedwpderVRDAVLAALERVGADwveqlphGVDTVVGRLGIRLSPAQAQQVALARALLADPP 498
Cdd:PRK10418 97 tmhtharetclALGKPA---------DDATLTAALEAVGLE-------NAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 499 VIILDEATAEAGS-SGATALDR-AAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK10418 161 FIIADEPTTDLDVvAQARILDLlESIVQKRALGMLLVTHDMGVVArLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
345-544 |
2.73e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHartvlISQEIHTFSGT 424
Cdd:PRK13540 2 LDVIELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-----IKKDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 L-FDDVALGLAgqaedwPDERVRDAVL-------AALERVGADWVEQLPHGVDTVVGrlgiRLSPAQAQQVAL------- 489
Cdd:PRK13540 76 LcFVGHRSGIN------PYLTLRENCLydihfspGAVGITELCRLFSLEHLIDYPCG----LLSSGQKRQVALlrlwmsk 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 490 ARALLADPPVIILDEATAEagssgaTALDRAAAEAVRGRTALVVAHRLSQVTMAD 544
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLL------TIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
27-286 |
2.88e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 58.68 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 27 RGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRES 106
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 107 MIAVGLGLDQQRVEKAGTADLVSRASDdVTAVRDAANGalpRLVNT---MIMVIVSVGALASLHPLFFVPVLLAGVLYGL 183
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTG---QLFGTlldATSLLVFLPVLFFYSPTLALVVLAFSALIAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 184 AIREFL----RTAPPVYRAERnasttQSQRILS-TIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLRGRFLGNTL--VV 256
Cdd:cd18783 157 IILAFLppfrRRLQALYRAEG-----ERQAFLVeTVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPqtLT 231
|
250 260 270
....*....|....*....|....*....|
gi 488473579 257 RLLagEAVATIGVAWTGYLLVTTDRLSVGA 286
Cdd:cd18783 232 GPL--EKLMTVGVIWVGAYLVFAGSLTVGA 259
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
360-558 |
4.73e-09 |
|
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: 56.77 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmTSGHARTVLisqEIHT-FSGTL--FDDVALGLA-- 434
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-VRGRVSSLL---GLGGgFNPELtgRENIYLNGRll 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 435 GQAEDWPDERVRDAV-LAALERVgadwveqlphgVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILDEATAeAGSSG 513
Cdd:cd03220 113 GLSRKEIDEKIDEIIeFSELGDF-----------IDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLA-VGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473579 514 --ATALDRAAAEAVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVG 558
Cdd:cd03220 177 fqEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-563 |
7.28e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 344 SIHVDQVSFGYqDGPDVLHTVSLDIPAGHTVVLVGESGAGKST-LAAL-----------VAGLLEPRQGSI-----TMTS 406
Cdd:PRK14258 7 AIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTfLKCLnrmnelesevrVEGRVEFFNQNIyerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 407 GHARTVLISQEIHTFSGTLFDDVALGLagQAEDW-PDERVRDAVLAALErvGADWVEQLPHGVDtvvgRLGIRLSPAQAQ 485
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGV--KIVGWrPKLEIDDIVESALK--DADLWDEIKHKIH----KSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 486 QVALARALLADPPVIILDEAtaeagssgATALDRAAA-------EAVRGRTAL---VVAHRLSQVT-MADEVAVMDN--- 551
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEP--------CFGLDPIASmkvesliQSLRLRSELtmvIVSHNLHQVSrLSDFTAFFKGnen 229
|
250
....*....|....
gi 488473579 552 --GRIVEVGAPEQL 563
Cdd:PRK14258 230 riGQLVEFGLTKKI 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-567 |
1.59e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 342 PTSIHVDQVSFGYQDgPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGH---------ARTV 412
Cdd:PRK10253 5 VARLRGEQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 413 LISQEIHTFSG--TLFDDVALGLAGQA---EDWPDERvRDAVLAALERVGAdwVEQLPHGVDTvvgrlgirLSPAQAQQV 487
Cdd:PRK10253 84 GLLAQNATTPGdiTVQELVARGRYPHQplfTRWRKED-EEAVTKAMQATGI--THLADQSVDT--------LSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 488 ALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLR 564
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEIV 232
|
...
gi 488473579 565 QSD 567
Cdd:PRK10253 233 TAE 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
364-558 |
1.67e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.94 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAA-------LVAGLLEprQGSITMtSGH-------------ARTVLISQEIHTFSG 423
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTF-HGKnlyapdvdpvevrRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 424 TLFDDVALG--LAGQAEDWpDERVRDAVlaaleRVGADWveqlphgvDTVVGRL---GIRLSPAQAQQVALARALLADPP 498
Cdd:PRK14243 106 SIYDNIAYGarINGYKGDM-DELVERSL-----RQAALW--------DEVKDKLkqsGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 499 VIILDEATAEAGSSGATALDRAAAEAVRGRTALVVAHRLSQVTMADEVAVMDNGRIVEVG 558
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
343-537 |
1.77e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYQDGpDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLE----------------PRQGSIT--M 404
Cdd:PRK09984 3 TIIRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiellgrtvQREGRLArdI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 405 TSGHARTVLISQEIHTFSG-TLFDDVALGLAGQAEDW--------PDERVRdaVLAALERVG-ADWVEQLphgVDTvvgr 474
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPFWrtcfswftREQKQR--ALQALTRVGmVHFAHQR---VST---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 475 lgirLSPAQAQQVALARALLADPPVIILDEATAEAGSSGAtaldRAAAEAVR------GRTALVVAHRL 537
Cdd:PRK09984 153 ----LSGGQQQRVAIARALMQQAKVILADEPIASLDPESA----RIVMDTLRdinqndGITVVVTLHQV 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
364-558 |
1.97e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsghartvliSQEIHTFSGTLFDDVALGLAGQAEDW--- 440
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN---------GQRIDTLSPGKLQALRRDIQFIFQDPyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 441 --PDERVRDAVLAALERVGADWVEQLPHGVDTVVGRLGIR----------LSPAQAQQVALARALLADPPVIILDEATAE 508
Cdd:PRK10261 414 ldPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpehawrypheFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488473579 509 AGSSGATALDRAAAEAVR--GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVG 558
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVErISHRVAVMYLGQIVEIG 546
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
360-504 |
2.29e-08 |
|
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: 54.86 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsghartvliSQEIHTFsgTLFDDVALG---LAGQ 436
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD---------GQDITKL--PMHKRARLGigyLPQE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 437 AEDWPDERVRDAVLAALERVG---ADWVEQLPH-----GVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDE 504
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGlskKEREEKLEElleefHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
367-550 |
2.42e-08 |
|
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: 55.11 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 367 DIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItmtsghartvlisqeihtfsGTLFDDVALGLAGQAEDWPDeRVR 446
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------------------EIELDTVSYKPQYIKADYEG-TVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 447 DAVLAALERVGAD--WVEQL--PHGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATA----EAGSSGATALD 518
Cdd:cd03237 80 DLLSSITKDFYTHpyFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAyldvEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|...
gi 488473579 519 RAAAEAvrGRTALVVAHRLSQVTM-ADEVAVMD 550
Cdd:cd03237 160 RFAENN--EKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
360-536 |
3.22e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLE--PRQGSITMTSGHartvlISQEihtfsGTLFDDValglagqa 437
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ-----FGRE-----ASLIDAI-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 438 edWPDERVRDAVlAALERVG-AD---WVEQLPHgvdtvvgrlgirLSPAQAQQVALARALLADPPVIILDEATAEAGSSG 513
Cdd:COG2401 107 --GRKGDFKDAV-ELLNAVGlSDavlWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*
gi 488473579 514 ATALDRAAAEAVR--GRTALVVAHR 536
Cdd:COG2401 172 AKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-567 |
3.61e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.20 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTS----GHARtvlisqeihtfsgtlFDDVALGLAG 435
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRAR---------------HARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 436 QAEDW-PDERVRDAVL----------AALERVGADWVE--QLPHGVDTVVGRLgirlSPAQAQQVALARALLADPPVIIL 502
Cdd:PRK13537 87 QFDNLdPDFTVRENLLvfgryfglsaAAARALVPPLLEfaKLENKADAKVGEL----SGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 503 DEATaeagssgaTALDRAAAEAV---------RGRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:PRK13537 163 DEPT--------TGLDPQARHLMwerlrsllaRGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
325-563 |
5.53e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 325 IQARHDKPAVseryQRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT- 403
Cdd:COG3845 242 VLLRVEKAPA----EPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRl 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 404 ----MTSGHARTVL------ISQEIHTF----SGTLFDDVALGLAGQAEDWPDERVRdavLAALERVGADWVEQL---PH 466
Cdd:COG3845 318 dgedITGLSPRERRrlgvayIPEDRLGRglvpDMSVAENLILGRYRRPPFSRGGFLD---RKAIRAFAEELIEEFdvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 467 GVDTVVGrlgiRLSPAQAQQVALARALLADPPVIILDEATaeAGssgataLDRAAAEAVR---------GRTALVVAHRL 537
Cdd:COG3845 395 GPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPT--RG------LDVGAIEFIHqrllelrdaGAAVLLISEDL 462
|
250 260
....*....|....*....|....*..
gi 488473579 538 SQV-TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:COG3845 463 DEIlALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-321 |
5.74e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 54.44 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLDLTVPVATGWIID----AAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLR- 104
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 105 ---ESMIAVGLG-LDQQRvekagTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPV 174
Cdd:cd18563 81 dlyEHLQRLSLSfFDKRQ-----TGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWklallvLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 175 LLAGVLYglaIREFLRtapPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTR--AVANGSWQAIRWNLRGRFLGN 252
Cdd:cd18563 156 VVWGSYF---FWKKIR---RLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKrfDEANQELLDANIRAEKLWATF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 253 TLVVRLLAGeaVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18563 230 FPLLTFLTS--LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
33-285 |
6.70e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 54.44 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTT-----IITRLRESM 107
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRiagerIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 108 IAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP-------LFFVPVLLAGVL 180
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkltlvmlLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 181 YGLAIREFlrtappvyraernasTTQSQRILST--------IHGVDVVRAFGLENL-------RTRAVANGSWQAIRWnl 245
Cdd:cd18573 161 YGRYVRKL---------------SKQVQDALADatkvaeerLSNIRTVRAFAAERKeveryakKVDEVFDLAKKEALA-- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488473579 246 RGRFLGNTlvvrLLAGEaVATIGVAWTGYLLVTTDRLSVG 285
Cdd:cd18573 224 SGLFFGST----GFSGN-LSLLSVLYYGGSLVASGELTVG 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
360-563 |
7.91e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTlAALVAGLLEPRQGSITMTSghartvlisQEIHTFS-----------GTLFDD 428
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDG---------QPLHNLNrrqllpvrhriQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 429 --------------VALGLAGQAEDWPDERVRDAVLAALERVGADwvEQLPHgvdtvvgRLGIRLSPAQAQQVALARALL 494
Cdd:PRK15134 371 pnsslnprlnvlqiIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD--PETRH-------RYPAEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 495 ADPPVIILDEATaeagssgaTALDRAA-AEAVRGRTALVVAHRLS--------QV--TMADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK15134 442 LKPSLIILDEPT--------SSLDKTVqAQILALLKSLQQKHQLAylfishdlHVvrALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
361-562 |
1.23e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLePRQGSITM-----------TSGHARTVLISQEIHTFSGTLFDDV 429
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFagqpleawsaaELARHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 ALGLagqaedwPDERVRDAVLAALERVgadwVEQLphGVDTVVGRLGIRLSPAQAQQVALARALLADPPVI-------IL 502
Cdd:PRK03695 91 TLHQ-------PDKTRTEAVASALNEV----AEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 503 DEATAEAGSSGATALDRAAAE-AVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQ 562
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDE 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-554 |
1.46e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 341 GPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItMTSGHARTVLISQEiHT 420
Cdd:PLN03073 505 GPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRMAVFSQH-HV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSGTLFDDVALGLAGQAEDWPDERVRdavlAALERVGadwveqlphgvdtVVGRLGIR----LSPAQAQQVALARALLAD 496
Cdd:PLN03073 583 DGLDLSSNPLLYMMRCFPGVPEQKLR----AHLGSFG-------------VTGNLALQpmytLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 497 PPVIILDEATAEagssgataLDRAAAEA-VRGRT-----ALVVAHRLSQVTMA-DEVAVMDNGRI 554
Cdd:PLN03073 646 PHILLLDEPSNH--------LDLDAVEAlIQGLVlfqggVLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
364-569 |
1.54e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.55 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPrqgsitmTSGHARtVL----------ISQEIhtfsGTLFddvalgl 433
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVP-------TSGEVR-VLgyvpfkrrkeFARRI----GVVF------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 434 aGQAED-WPDERVRDA--VLAALERVGADWVEQLphgVDTVVGRLGI---------RLSPAQAQQVALARALLADPPVII 501
Cdd:COG4586 102 -GQRSQlWWDLPAIDSfrLLKAIYRIPDAEYKKR---LDELVELLDLgelldtpvrQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 502 LDEATaeAGssgataLDRAAAEAVR----------GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQSDGP 569
Cdd:COG4586 178 LDEPT--IG------LDVVSKEAIReflkeynrerGTTILLTSHDMDDIEaLCDRVIVIDHGRIIYDGSLEELKERFGP 248
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
357-563 |
1.71e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.59 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 357 GPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG-------HARTV----LISQEIHTFSGTL 425
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplHARARrgigYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 426 FDDVALGLAGQAEDWPDERVRDAVLAALERVgadwveQLPHGVDTvvgrLGIRLSPAQAQQVALARALLADPPVIILDEA 505
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQREDRANELMEEF------HIEHLRDS----MGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 506 TaeAGSSGATALD-RAAAEAVR--GRTALVVAHRLSQVTMADEVA-VMDNGRIVEVGAPEQL 563
Cdd:PRK10895 165 F--AGVDPISVIDiKRIIEHLRdsGLGVLITDHNVRETLAVCERAyIVSQGHLIAHGTPTEI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
361-568 |
1.76e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT-----MTSGHAR--------------------TVLIS 415
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdMADARHRravcpriaympqglgknlypTLSVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 416 QEIHTFsGTLFddvalglaGQAEDWPDERVrDAVLAA------LERvgadwveqlPHGvdtvvgrlgiRLSPAQAQQVAL 489
Cdd:NF033858 97 ENLDFF-GRLF--------GQDAAERRRRI-DELLRAtglapfADR---------PAG----------KLSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 490 ARALLADPPVIILDEATaeagsSGATALDRAA----AEAVRGR----TALVV------AHRLsqvtmaDEVAVMDNGRIV 555
Cdd:NF033858 148 CCALIHDPDLLILDEPT-----TGVDPLSRRQfwelIDRIRAErpgmSVLVAtaymeeAERF------DWLVAMDAGRVL 216
|
250
....*....|...
gi 488473579 556 EVGAPEQLRQSDG 568
Cdd:NF033858 217 ATGTPAELLARTG 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
350-579 |
1.94e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.96 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDGP---DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGS-------ITMTSGHARTVL------ 413
Cdd:PRK10535 10 IRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdVATLDADALAQLrrehfg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 -ISQEIHTFSGTLfddvalglAGQAEDWPdervrdAVLAALERvgadwvEQLPHGVDTVVGRLGI---------RLSPAQ 483
Cdd:PRK10535 90 fIFQRYHLLSHLT--------AAQNVEVP------AVYAGLER------KQRLLRAQELLQRLGLedrveyqpsQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 484 AQQVALARALLADPPVIILDEATAeagssgatALDRAAAEAV---------RGRTALVVAHRLSQVTMADEVAVMDNGRI 554
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTG--------ALDSHSGEEVmailhqlrdRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
250 260 270
....*....|....*....|....*....|.
gi 488473579 555 VEVGAPEQLRQSDG------PFAALWRVWSN 579
Cdd:PRK10535 222 VRNPPAQEKVNVAGgtepvvNTASGWRQFVS 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
339-554 |
3.90e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 339 QRGPTSIHVDQVSfgyqdGPDVlHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITmtsghartvLISQEI 418
Cdd:PRK10762 252 APGEVRLKVDNLS-----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT---------LDGHEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 HTFSGTlfDDVALGLAGQAEDwpdeRVRDAV-----------LAALERVGADWVeQLPHG-----VDTVVGRLGIR---- 478
Cdd:PRK10762 317 VTRSPQ--DGLANGIVYISED----RKRDGLvlgmsvkenmsLTALRYFSRAGG-SLKHAdeqqaVSDFIRLFNIKtpsm 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 479 ------LSPAQAQQVALARALLADPPVIILDEATaEAGSSGATA-----LDRAAAEavrGRTALVVAHRLSQVT-MADEV 546
Cdd:PRK10762 390 eqaiglLSGGNQQKVAIARGLMTRPKVLILDEPT-RGVDVGAKKeiyqlINQFKAE---GLSIILVSSEMPEVLgMSDRI 465
|
....*...
gi 488473579 547 AVMDNGRI 554
Cdd:PRK10762 466 LVMHEGRI 473
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
3-530 |
3.92e-07 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 53.34 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 3 TPRSLPLATAAQVRQEVHRAARGVRGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSG 82
Cdd:COG3321 857 GRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALA 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 83 ICNGAAQSLTPSFFTTII--TRLRESMIAVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSV 160
Cdd:COG3321 937 AAAAALLALAAAAAAAAAalAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAA 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 161 GALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAERNASTTQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQA 240
Cdd:COG3321 1017 AAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 241 IRWNLRGRFLGNTLVVRLLAGEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQR 320
Cdd:COG3321 1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 321 VVGVIQARHDKPAVSERYQRGPTSIHVDQVSFGYQDGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQG 400
Cdd:COG3321 1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 401 SITMTSGHARTVLISQEIHTFSGTLFDDVALGLAGQAEDWPDERVRDAVLAALERVGADWVEQLPHGVDTVVGRLGIRLS 480
Cdd:COG3321 1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAA 1336
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 488473579 481 PAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAAEAVRGRTA 530
Cdd:COG3321 1337 VAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
360-506 |
4.11e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTsGH--------ARTVLISQEIhtfsGTLFDDVAL 431
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQplhqmdeeARAKLRAKHV----GFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 432 ----------GLAGQAEDWPDERVRDAVLAALERVGADwvEQLPHgvdtvvgrLGIRLSPAQAQQVALARALLADPPVII 501
Cdd:PRK10584 100 iptlnalenvELPALLRGESSRQSRNGAKALLEQLGLG--KRLDH--------LPAQLSGGEQQRVALARAFNGRPDVLF 169
|
....*
gi 488473579 502 LDEAT 506
Cdd:PRK10584 170 ADEPT 174
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
124-321 |
4.11e-07 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 52.04 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 124 TADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAERNAS 203
Cdd:cd18554 102 SGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 204 TTQSQRILSTIHGVDVVRAFGLE------------NLRTRAVANgswqaIRWNLRGRFLGNTLVvrllageAVATIGVAW 271
Cdd:cd18554 182 AEVQGFLHERIQGMSVIKSFALEkheqkqfdkrngHFLTRALKH-----TRWNAKTFSAVNTIT-------DLAPLLVIG 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473579 272 TGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18554 250 FAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
127-321 |
7.43e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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 by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 50.97 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 127 LVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAErnaSTTQ 206
Cdd:cd18580 98 ILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLE---SESR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 207 S---QRILSTIHGVDVVRAFGLE-----------NLRTRAVANgSWQAIRW-NLRGRFLGNTLVVrllageAVATIGVAw 271
Cdd:cd18580 175 SplySHFSETLSGLSTIRAFGWQerfieenlrllDASQRAFYL-LLAVQRWlGLRLDLLGALLAL------VVALLAVL- 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488473579 272 tgyllvTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18580 247 ------LRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERI 290
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
343-567 |
8.11e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 343 TSIHVDQVSFGYQdGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSItmtsghartVLISQEIHTFS 422
Cdd:PRK10575 10 TTFALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI---------LLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 GTLFDDVALGLAGQAEDWPDERVRDAVL-------AALERVGADWVEQLPHGVdTVVG------RLGIRLSPAQAQQVAL 489
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGMTVRELVAigrypwhGALGRFGAADREKVEEAI-SLVGlkplahRLVDSLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 490 ARALLADPPVIILDEATaeagssgaTALDRAAAEAVrgrtaLVVAHRLSQ------------VTMA----DEVAVMDNGR 553
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPT--------SALDIAHQVDV-----LALVHRLSQergltviavlhdINMAarycDYLVALRGGE 225
|
250
....*....|....
gi 488473579 554 IVEVGAPEQLRQSD 567
Cdd:PRK10575 226 MIAQGTPAELMRGE 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
348-555 |
8.39e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 348 DQVSFGYQDgPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGllEPR--QGSITMTSG---HARTVLISQEI---- 418
Cdd:PRK11614 9 DKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRatSGRIVFDGKditDWQTAKIMREAvaiv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 419 ----HTFSG-TLFDDVALGlaGQAEDwpdervRDAVLAALERVgadwVEQLPHGVDTVVGRLGIrLSPAQAQQVALARAL 493
Cdd:PRK11614 86 pegrRVFSRmTVEENLAMG--GFFAE------RDQFQERIKWV----YELFPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 494 LADPPVIILDEAT-AEAGSSGATALDRAAAEAVRGRTALVVAHRLSQ-VTMADEVAVMDNGRIV 555
Cdd:PRK11614 153 MSQPRLLLLDEPSlGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQaLKLADRGYVLENGHVV 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
364-562 |
1.30e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.84 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLePRQGSITMT-------SGHA----RTVLISQEIHTFSGTLFDDVALG 432
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNgrplsdwSAAElarhRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 433 LAGQAedwPDERVRDAVLAALERVGADwvEQLPHGVDTvvgrlgirLSPAQAQQVALARALL-------ADPPVIILDEA 505
Cdd:COG4138 94 QPAGA---SSEAVEQLLAQLAEALGLE--DKLSRPLTQ--------LSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 506 TAEAGSSGATALDRAAAE-AVRGRTALVVAHRLSQ-VTMADEVAVMDNGRIVEVGAPEQ 562
Cdd:COG4138 161 MNSLDVAQQAALDRLLRElCQQGITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
361-556 |
1.38e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLL-------------EPRQGSITMTSGHARTVLISQEihtfsgtlfd 427
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphgsyegeilfdgEVCRFKDIRDSEALGIVIIHQE---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 428 dvaLGLAGQ---AE--------------DWPDERVRDAVLaaLERVGadwVEQLPhgvDTVVGRLGIrlspAQAQQVALA 490
Cdd:NF040905 87 ---LALIPYlsiAEniflgnerakrgviDWNETNRRAREL--LAKVG---LDESP---DTLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 491 RALLADPPVIILDEATA---EAGSsgATALDRAAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRIVE 556
Cdd:NF040905 152 KALSKDVKLLILDEPTAalnEEDS--AALLDLLLELKAQGITSIIISHKLNEIRrVADSITVLRDGRTIE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
364-565 |
2.19e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.22 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 364 VSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMT-------SGH--AR----------------TV----LI 414
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieglPGHqiARmgvvrtfqhvrlfremTVienlLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSGTLfddvaLGLAGQAedwpdeRVRDAVLAALERvGADWVEQLphGVDTVVGRLGIRLSPAQAQQVALARALL 494
Cdd:PRK11300 104 AQHQQLKTGLF-----SGLLKTP------AFRRAESEALDR-AATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 495 ADPPVIILDEATAEAGSSGATALDRAAAEAVR--GRTALVVAHRLSQVT-MADEVAVMDNGRIVEVGAPEQLRQ 565
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
350-535 |
2.96e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHARTVLISQEIHTFSgtlfddv 429
Cdd:PRK13543 17 LAFSRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLG------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 430 alGLAGQAEDwpdervrdavLAALER------VGADWVEQLPHGVDTVVGRLGI------RLSPAQAQQVALARALLADP 497
Cdd:PRK13543 89 --HLPGLKAD----------LSTLENlhflcgLHGRRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 488473579 498 PVIILDEATAEAGSSGATALDRAAAEAVR-GRTALVVAH 535
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMISAHLRgGGAALVTTH 195
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
37-321 |
3.97e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 48.71 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 37 ITAASL----LDLTVPVATGWIIDAAKAHRPTSALLtpalVMAAAVIGSGICN------------GAAQSLTPSFFTTII 100
Cdd:cd18568 7 ILLASLllqlLGLALPLFTQIILDRVLVHKNISLLN----LILIGLLIVGIFQillsavrqylldYFANRIDLSLLSDFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 101 TRLresmiavgLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMiMVIVSVGALASLHP------LFFVPV 174
Cdd:cd18568 83 KHL--------LSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLL-MVFIYLGLMFYYNLqltlivLAFIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 175 LLAGVLYglaireflrTAPPVYRAER---NASTTQSQRILSTIHGVDVVRAFGLENLrtravangswqaIRW-------- 243
Cdd:cd18568 154 YVLLTLL---------SSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERP------------IRWrwenkfak 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 244 NLRGRFLGNTLVVRL-LAGEAVATIG---VAWTGYLLVTTDRLSVGA--AATAVLVLLRlfSPVRFLLMFLNNLQAAWVC 317
Cdd:cd18568 213 ALNTRFRGQKLSIVLqLISSLINHLGtiaVLWYGAYLVISGQLTIGQlvAFNMLFGSVI--NPLLALVGLWDELQETRIS 290
|
....
gi 488473579 318 LQRV 321
Cdd:cd18568 291 VERL 294
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
340-407 |
4.05e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 4.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488473579 340 RGPTSI-----HVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSG 407
Cdd:PRK10636 303 RAPESLpnpllKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG 374
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-567 |
4.64e-06 |
|
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: 49.44 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 356 DGPDVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLL-------------EPRQGSITMTSGHARTVLISQEIHTFS 422
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiywsgSPLKASNIRDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 423 G-TLFDDVALG----LAGQAEDWPDERVRDAVLAALERVGADwveqlphGVDTVVGRLGIrlspAQAQQVALARALLADP 497
Cdd:TIGR02633 92 ElSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDAD-------NVTRPVGDYGG----GQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488473579 498 PVIILDEATAE-AGSSGATALDRAAAEAVRGRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQLRQSD 567
Cdd:TIGR02633 161 RLLILDEPSSSlTEKETEILLDIIRDLKAHGVACVYISHKLNEVkAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
371-568 |
5.52e-06 |
|
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: 49.63 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 371 GHTVVLVGESGAGKSTLAALVAGlleprqgSITMTSGHA----RTVLIS-QEIHTFSGTL--FDDVALGLAGQAEDWPDE 443
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG-------DTTVTSGDAtvagKSILTNiSDVHQNMGYCpqFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 444 RVRDAVLAALERVgADW-VEQLphGVDTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDRAAA 522
Cdd:TIGR01257 2038 RLRGVPAEEIEKV-ANWsIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488473579 523 EAVR-GRTALVVAHRLSQV-TMADEVAVMDNGRIVEVGAPEQLRQSDG 568
Cdd:TIGR01257 2115 SIIReGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
361-562 |
6.15e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSGHartvlisqeihtfsGTLFDDVALGLAGQ---- 436
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD--------------GQLRDLYALSEAERrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 437 AEDW------PDERVRDAVLA-----------------ALERVGADWVEQlphgVDTVVGRLGIR---LSPAQAQQVALA 490
Cdd:PRK11701 88 RTEWgfvhqhPRDGLRMQVSAggnigerlmavgarhygDIRATAGDWLER----VEIDAARIDDLpttFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 491 RALLADPPVIILDEATaeAG---SSGATALD---RAAAEAvrGRTALVVAHRLSQVTM-ADEVAVMDNGRIVEVGAPEQ 562
Cdd:PRK11701 164 RNLVTHPRLVFMDEPT--GGldvSVQARLLDllrGLVREL--GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQ 238
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
27-320 |
6.74e-06 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit 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, a various type of lipids and polypeptides. 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 by alternating between inward- and outward-facing conformations. Moreover, 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 48.22 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 27 RGYFIGAIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICN----------GAA-------- 88
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNyfvtywghvmGARietdmrrd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 89 -----QSLTPSFFttiitrlresmiavglglDQQRvekagTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGAL 163
Cdd:cd18549 81 lfehlQKLSFSFF------------------DNNK-----TGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIIL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 164 ASLHP------LFFVPVLLagvLYGLAIREFLRTAppvYRAER------NAsttqsqRILSTIHGVDVVRAFGLENLRTR 231
Cdd:cd18549 138 LTINVpltlivFALLPLMI---IFTIYFNKKMKKA---FRRVRekigeiNA------QLEDSLSGIRVVKAFANEEYEIE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 232 --AVANGSWQAIR-WNLR--GRFL-GNTLVVRLLageAVATIGVawtGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLL 305
Cdd:cd18549 206 kfDEGNDRFLESKkKAYKamAYFFsGMNFFTNLL---NLVVLVA---GGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLV 279
|
330
....*....|....*
gi 488473579 306 MFLNNLQAAWVCLQR 320
Cdd:cd18549 280 NFTEQYQKGMAGFER 294
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
350-563 |
6.78e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 350 VSFGYQDGpDV--LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLePRQGSItmtSGHAR--------------TVL 413
Cdd:PRK09473 20 VTFSTPDG-DVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRI---GGSATfngreilnlpekelNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 414 ISQEIhtfsGTLFDDVALGL-------------------AGQAEDWpDERVR--DAVL--AALERVGadwveQLPHgvdt 470
Cdd:PRK09473 95 RAEQI----SMIFQDPMTSLnpymrvgeqlmevlmlhkgMSKAEAF-EESVRmlDAVKmpEARKRMK-----MYPH---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 471 vvgrlgiRLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALDRAAAEAVRG---------RTALV-VAHRLSQV 540
Cdd:PRK09473 161 -------EFSGGMRQRVMIAMALLCRPKLLIADEPT--------TALDVTVQAQIMTllnelkrefNTAIImITHDLGVV 225
|
250 260
....*....|....*....|....
gi 488473579 541 T-MADEVAVMDNGRIVEVGAPEQL 563
Cdd:PRK09473 226 AgICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
24-312 |
7.93e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.96 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 24 RGVRGYFIGAIVVItaaSLLDLTVPVATGWIIDAAKAHRPTSALLtpalVMAAAVIGSGICNGAAQSLTPSFFTTIITRL 103
Cdd:cd18566 1 RPLLPQVLLASLFI---NILALATPLFILQVYDRVIPNESIPTLQ----VLVIGVVIAILLESLLRLLRSYILAWIGARF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 104 --RESMIAVG--LGLDQQRVEKAGTADLVSRASDdVTAVRDAANGalpRLVNTMI---MVIVSVGALASLH-PLFFVPVL 175
Cdd:cd18566 74 dhRLSNAAFEhlLSLPLSFFEREPSGAHLERLNS-LEQIREFLTG---QALLALLdlpFVLIFLGLIWYLGgKLVLVPLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 176 LAGVLYGLAIReflrTAPPVYRAERNASTTQSQR---ILSTIHGVDVVRAFGLENLRTRavangswqaiRW-NLRGRFLG 251
Cdd:cd18566 150 LLGLFVLVAIL----LGPILRRALKERSRADERRqnfLIETLTGIHTIKAMAMEPQMLR----------RYeRLQANAAY 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 252 NTLVVRLLAGEA---------VATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQ 312
Cdd:cd18566 216 AGFKVAKINAVAqtlgqlfsqVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQ 285
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
371-555 |
7.98e-06 |
|
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: 45.83 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 371 GHTVVLVGESGAGKSTLAALVAGLLEPRQGSItmtsghartvlisqeihtfsgtlfddvalglagqaedwpdervrdaVL 450
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV----------------------------------------------IY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 451 AALERVGADWVEQLPHgvdTVVGRLGIRLSPAQAQQVALARALLADPPVIILDEATA------EAGSSGATALDRAAAEA 524
Cdd:smart00382 36 IDGEDILEEVLDQLLL---IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSlldaeqEALLLLLEELRLLLLLK 112
|
170 180 190
....*....|....*....|....*....|.
gi 488473579 525 VRGRTALVVAHRLSQVTMADEVAVMDNGRIV 555
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
361-540 |
9.41e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 361 LHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMtSGHARTVLISQEIhtfSGTLFDDVALGLAGQAEDW 440
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-KGSAALIAISSGL---NGQLTGIENIELKGLMMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 441 PDERVRDAVLAALERvgADWVEQLPHGVDTVVGRLGIRLSPAQAQQValarallaDPPVIILDEATAeAGSSGAT--ALD 518
Cdd:PRK13545 116 TKEKIKEIIPEIIEF--ADIGKFIYQPVKTYSSGMKSRLGFAISVHI--------NPDILVIDEALS-VGDQTFTkkCLD 184
|
170 180
....*....|....*....|..
gi 488473579 519 RAAAEAVRGRTALVVAHRLSQV 540
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQV 206
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
365-538 |
1.21e-05 |
|
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: 48.21 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 365 SLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITMTSgHARTVLISQEIHTFSGTLFDDVALglAGQAEDWPDER 444
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-KGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 445 VRDAVLAA-LERVgadwveQLPHGVDTVVGRLGIR-----LSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALD 518
Cdd:TIGR00954 549 LSDKDLEQiLDNV------QLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMY 622
|
170 180
....*....|....*....|
gi 488473579 519 RAAAEAvrGRTALVVAHRLS 538
Cdd:TIGR00954 623 RLCREF--GITLFSVSHRKS 640
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
360-504 |
2.90e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 45.79 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSIT----------MtsgHARTVL-IS---QEIHTFSG-T 424
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedithlpM---HKRARLgIGylpQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 425 lfddvalglagqaedwpderVRDAVLAALERVGADWVEQLPH--------GVDTVVGRLGIRLSPAQAQQVALARALLAD 496
Cdd:COG1137 95 --------------------VEDNILAVLELRKLSKKEREERleelleefGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
....*...
gi 488473579 497 PPVIILDE 504
Cdd:COG1137 155 PKFILLDE 162
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
33-226 |
3.94e-05 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 45.79 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIAVGL 112
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 113 GLDQQRVEKAGTADLVSRASDDVTAVRDA----ANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGV---LYGLAI 185
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSvalnANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIaqkVYNTYH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488473579 186 REFLrtappvyRAERNASTTQSQRILSTIHGVDVVRAFGLE 226
Cdd:cd18590 161 QKLS-------QAVQDSIAKAGELAREAVSSIRTVRSFKAE 194
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
127-299 |
3.98e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 45.92 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 127 LVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAErnaSTTQ 206
Cdd:cd18604 102 ILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLE---SVAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 207 S---QRILSTIHGVDVVRAFGLENL-------RTRAVANGSWqaIRWNLRgRFLGntlvVRLlagEAVATIGVAWTGYLL 276
Cdd:cd18604 179 SpilSHFGETLAGLVTIRAFGAEERfieemlrRIDRYSRAFR--YLWNLN-RWLS----VRI---DLLGALFSFATAALL 248
|
170 180 190
....*....|....*....|....*....|...
gi 488473579 277 VTTDRLSVGAAA----------TAVLVLLRLFS 299
Cdd:cd18604 249 VYGPGIDAGLAGfslsfalgfsSAILWLVRSYN 281
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
347-402 |
1.00e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 347 VDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI 402
Cdd:PRK15064 322 VENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
33-314 |
1.13e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 44.46 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGaAQSLTPSFFTTIIT-RLRESMIAVG 111
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSG-LRGGCFSYAGTRLVrRLRRDLFRSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 112 LGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVPVLLAGV-LYGLA 184
Cdd:cd18572 80 LRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltllaFITVPVIALITkVYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 185 IREFLRTAPPVYrAERNASTTQSqriLSTIHgvdVVRAFGLEN----------------LRTRAVANGSWQAIRWnlrgr 248
Cdd:cd18572 160 YRKLSKEIQDAL-AEANQVAEEA---LSNIR---TVRSFATEErearryeraldkalklSVRQALAYAGYVAVNT----- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 249 FLGNTLVVRLLageavatigvaWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAA 314
Cdd:cd18572 228 LLQNGTQVLVL-----------FYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA 282
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
33-286 |
1.30e-04 |
|
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: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.01 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIAVGL 112
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 113 GLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFFVP-VLLAGVLYGLAI 185
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltllvLLVIPlVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 186 REFLRTAppvyrAERNASTtqSQRILSTIHGVDVVRAFGLENL---RTRAVANGSWQAIRWNLRGRFLGNTLVVRLLAGe 262
Cdd:cd18575 161 RRLSRAS-----QDRLADL--SAFAEETLSAIKTVQAFTREDAerqRFATAVEAAFAAALRRIRARALLTALVIFLVFG- 232
|
250 260
....*....|....*....|....
gi 488473579 263 avATIGVAWTGYLLVTTDRLSVGA 286
Cdd:cd18575 233 --AIVFVLWLGAHDVLAGRMSAGE 254
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
49-307 |
1.31e-04 |
|
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: 44.19 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 49 VATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIAVGLGLDQQRVEKAGTADLV 128
Cdd:cd18561 17 WLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 129 SRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAERNASTTQSQ 208
Cdd:cd18561 97 TTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 209 RILSTIHGVDVVRAFGLENLRTRAVANGS---WQAIRWNLRGRFLGNTLVVRLLAGEAVATIGVAWTGYLlvtTDRLSVG 285
Cdd:cd18561 177 QFLDSLQGMTTLKAFGASKRRGNELAARAedlRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVL---GGQLTLS 253
|
250 260
....*....|....*....|..
gi 488473579 286 AAATAVLVLLRLFSPVRFLLMF 307
Cdd:cd18561 254 SLLLILFLSREFFRPLRDLGAY 275
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
360-558 |
1.44e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPR--QGSITMTSGH------ARTVLISQE----IH-TFSGTLF 426
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKptkqilKRTGFVTQDdilyPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 427 DDVALGLAGQAEDWPDERVRDAVLAALervgadwveQLPHGVDTVVGRLGIR-LSPAQAQQVALARALLADPPVIILDEA 505
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKILVAESVISEL---------GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488473579 506 TAEAGSSGATALDRA-AAEAVRGRTALVVAHRLSQ--VTMADEVAVMDNGRIVEVG 558
Cdd:PLN03211 234 TSGLDATAAYRLVLTlGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
33-286 |
3.46e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 43.01 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTS------ALLTPALVMAAAVIGSGIcngaAQSLTPSFFTT----IITR 102
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGgeealrALNQAVLILLGVVLIGSI----ATFLRSWLFTLagerVVAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 103 LR----ESMIAVGLGL-DQQRvekagTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHP------LFF 171
Cdd:cd18780 77 LRkrlfSAIIAQEIAFfDVTR-----TGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWkltlvmLSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 172 VPVLLAG-VLYGLAIREFLRTappVYRAERNASTTQSQrilsTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLR---- 246
Cdd:cd18780 152 VPPLSIGaVIYGKYVRKLSKK---FQDALAAASTVAEE----SISNIRTVRSFAKETKEVSRYSEKINESYLLGKKlara 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488473579 247 -GRFLGntlVVRLLAGEAVATigVAWTGYLLVTTDRLSVGA 286
Cdd:cd18780 225 sGGFNG---FMGAAAQLAIVL--VLWYGGRLVIDGELTTGL 260
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
127-255 |
4.54e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 42.47 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 127 LVSRASDDVtavrDAANGALPR----LVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAErna 202
Cdd:cd18603 100 ILNRFSKDI----DTVDNTLPQnirsFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLE--- 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 203 STTQSQrILS----TIHGVDVVRAFGL-------------ENLRTR---AVANgswqaiRW-NLRGRFLGNTLV 255
Cdd:cd18603 173 SVSRSP-IYShfseTLQGASTIRAYGVqerfiresdrrvdENQRAYypsIVSN------RWlAVRLEFLGNLIV 239
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
360-560 |
4.82e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.12 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLL--EPRQGSITMTSGHA-----------------RTVLISQEIHT 420
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgGGAPRGARVTGDVTlngeplaaidaprlarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 421 FSGTLFDDVALGLAGQAE--DWPDERVRDAVLAALERVGAdwveqlphgvDTVVGRLGIRLSPAQAQQVALARAL----- 493
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGA----------TALVGRDVTTLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 494 ----LADPPVIILDEATAeagssgatALDRAAA----EAVRGRT------ALVVAHRLS-QVTMADEVAVMDNGRIVEVG 558
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTA--------ALDLAHQhrllDTVRRLArdwnlgVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
..
gi 488473579 559 AP 560
Cdd:PRK13547 238 AP 239
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
32-321 |
6.76e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 41.76 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 32 GAIVVITAAS----LLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICN----GAAQSLTPSFFTTIITRL 103
Cdd:cd18779 2 GLLGQILLASlllqLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGllrsHLLLRLRTRLDTQLTLGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 104 RESMIAVGLGLDQQRvekaGTADLVSRASDdVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGL 183
Cdd:cd18779 82 LEHLLRLPYRFFQQR----STGDLLMRLSS-NATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 184 AireFLRTAPPVYRAERNASTTQSQ---RILSTIHGVDVVRAFGLENlrtRAVANGSW---QAIRWNLRGRFLGNTLVVR 257
Cdd:cd18779 157 L---LLATRRRVRELMARELAAQAEaqsYLVEALSGIETLKASGAED---RALDRWSNlfvDQLNASLRRGRLDALVDAL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488473579 258 LLAGEAVATIGVAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18779 231 LATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
376-552 |
1.12e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 376 LVGESGAGKSTLAALVAGL--------------LEPRQGSITMTSGHARTVLISQEIHTFSGTLFDDVALGLAGQAEDWP 441
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRktggyiegdirisgFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEE 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 442 DERVRDAVLAALErvgadwVEQLPhgvDTVVGRLGIR-LSPAQAQQVALARALLADPPVIILDEATaeagsSGATAldRA 520
Cdd:PLN03140 991 KMMFVDEVMELVE------LDNLK---DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPT-----SGLDA--RA 1054
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488473579 521 AA---EAVR-----GRTALVVAHRLS-QVTMA-DEVAVMDNG 552
Cdd:PLN03140 1055 AAivmRTVRntvdtGRTVVCTIHQPSiDIFEAfDELLLMKRG 1096
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
345-404 |
1.13e-03 |
|
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: 41.84 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 345 IHVDQVSFGYQDGPdVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSITM 404
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
478-554 |
1.48e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 478 RLSPAQAQQVALARALLADPPVIILDEATaeagssgaTALDRAA---------AEAVRGRTALVVAHRLSQVT-MADEVA 547
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPT--------RGIDVGAkyeiyklinQLVQQGVAIIVISSELPEVLgLSDRVL 476
|
....*..
gi 488473579 548 VMDNGRI 554
Cdd:PRK13549 477 VMHEGKL 483
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
30-169 |
1.69e-03 |
|
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: 40.47 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 30 FIGAIVVITAASLLdltvpvatGWIIDAA-KAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMI 108
Cdd:cd18584 6 LLAALLIIAQAWLL--------ARIIAGVfLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488473579 109 AVGLGLDQQRVEKAGTADLVSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPL 169
Cdd:cd18584 78 ARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWV 138
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
134-320 |
1.69e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 40.66 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 134 DVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLF-FVPVLLAGVLYGLAIREFLRTAPPvYRAERNASTTQSQRILS 212
Cdd:cd18586 104 DLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLgWVALVGAPVLVGLAWLNHRATRKP-LGEANEAQAARDALAAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 213 TIHGVDVVRAFGLE-NLRTR----AVANGSWQAIRWNLRGRFLGNTLVVRLLAgeAVATIGVawtGYLLVTTDRLSVGAA 287
Cdd:cd18586 183 TLRNAETIKALGMLgNLRRRwearHAETLELQIRASDLAGAISAIGKTLRMAL--QSLILGV---GAYLVIDGELTIGAL 257
|
170 180 190
....*....|....*....|....*....|...
gi 488473579 288 ATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQR 320
Cdd:cd18586 258 IAASILSGRALAPIDQLVGAWKQLSAARQAYER 290
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
360-561 |
2.25e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 360 VLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQgsitmTSGharTVLIS-QEIHTfsGTLFDDVALGLAGQAE 438
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRN-----ISG---TVFKDgKEVDV--STVSDAIDAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 439 D-------WPDERVRDAVLAALERVGADWV----------EQL-------PHGVDTVVGRLgirlSPAQAQQVALARALL 494
Cdd:NF040905 345 DrkgyglnLIDDIKRNITLANLGKVSRRGVideneeikvaEEYrkkmnikTPSVFQKVGNL----SGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488473579 495 ADPPVIILDEATaeAG-SSGA-----TALDRAAAEavrGRTALVVAHRLSQVT-MADEVAVMDNGRIV-EVGAPE 561
Cdd:NF040905 421 TDPDVLILDEPT--RGiDVGAkyeiyTIINELAAE---GKGVIVISSELPELLgMCDRIYVMNEGRITgELPREE 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
479-557 |
2.47e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 479 LSPAQAQQVALARALLADPPVIILDEATaEAGSSGATA----LDRAAAEavRGRTALVVAHRLSQV-TMADEVAVMDNGR 553
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPT-RGIDVGAKAeiykVMRQLAD--DGKVILMVSSELPEIiTVCDRIAVFCEGR 486
|
....
gi 488473579 554 IVEV 557
Cdd:PRK09700 487 LTQI 490
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
370-402 |
3.86e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 3.86e-03
10 20 30
....*....|....*....|....*....|...
gi 488473579 370 AGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI 402
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
368-400 |
4.58e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.74 E-value: 4.58e-03
10 20 30
....*....|....*....|....*....|....*
gi 488473579 368 IPAGHTVVLVGESGAGKSTLAA--LVAGLLEPRQG 400
Cdd:COG0467 17 LPRGSSTLLSGPPGTGKTTLALqfLAEGLRRGEKG 51
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
33-321 |
4.76e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.11 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAA--SLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGAAQSLTPSFFTTIITRLRESMIAV 110
Cdd:cd18782 5 IEVLALSFvvQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 111 GLGLDQQRVEKAGTADLVSRASdDVTAVRDAANG-ALPRLVNTMIMVIVsVGALASLHP------LFFVPVLLA-GVLYG 182
Cdd:cd18782 85 LLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGtALTTLLDVLFSVIY-IAVLFSYSPlltlvvLATVPLQLLlTFLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 183 LAIREFLRtappvyRAERNASTTQSqRILSTIHGVDVVRAFGLEnLRTRAvangSWQairwNLRGRFLGNTL---VVRLL 259
Cdd:cd18782 163 PILRRQIR------RRAEASAKTQS-YLVESLTGIQTVKAQNAE-LKARW----RWQ----NRYARSLGEGFkltVLGTT 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488473579 260 AGEAVATIG------VAWTGYLLVTTDRLSVGAAATAVLVLLRLFSPVRFLLMFLNNLQAAWVCLQRV 321
Cdd:cd18782 227 SGSLSQFLNklssllVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
371-407 |
4.86e-03 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 39.65 E-value: 4.86e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488473579 371 GHTVVLVGESGAGKSTLA-ALVAGLLEPRQGSITMTSG 407
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAkALMVKLMEMRGRPVTLLDG 429
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
33-140 |
7.03e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 38.83 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 33 AIVVITAASLLDLTVPVATGWIIDAAKAHRPTSALLTPALVMAAAVIGSGICNGaaqsLTPSFFTTIITRLR-------- 104
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAG----IRGGLFTLAMARLNirirnllf 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 488473579 105 ESMIAVGLGL-DQQRvekagTADLVSRASDDVTAVRD 140
Cdd:cd18784 77 RSIVSQEIGFfDTVK-----TGDITSRLTSDTTTMSD 108
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
120-285 |
7.83e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 38.60 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 120 EKAGTADLVSRAsDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLairefLRTAppVYRAE 199
Cdd:cd18567 94 EKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYAL-----LRLA--LYPPL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 200 RNAST-------TQSQRILSTIHGVDVVRAFGLENLRTRAVANGSWQAIRWNLR-GRF-LGNTLVVRLLAGeaVATIGVA 270
Cdd:cd18567 166 RRATEeqivasaKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRlQRLqILFSAANGLLFG--LENILVI 243
|
170
....*....|....*
gi 488473579 271 WTGYLLVTTDRLSVG 285
Cdd:cd18567 244 YLGALLVLDGEFTVG 258
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
478-554 |
9.00e-03 |
|
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: 39.04 E-value: 9.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488473579 478 RLSPAQAQQVALARALLADPPVIILDEATAEAGSSGATALDR-AAAEAVRGRTALVVAHRLSQVT-MADEVAVMDNGRI 554
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKlINQLAQEGVAIIVVSSELAEVLgLSDRVLVIGEGKL 481
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
149-242 |
9.10e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 38.46 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 149 LVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAErnaSTTQS---QRILSTIHGVDVVRAFGL 225
Cdd:cd18601 140 FLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIE---GTTRSpvfSHLSSTLQGLWTIRAYSA 216
|
90 100 110
....*....|....*....|....*....|..
gi 488473579 226 E-----------NLRTRA----VANGSWQAIR 242
Cdd:cd18601 217 QerfqeefdahqDLHSEAwflfLATSRWLAVR 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-563 |
9.64e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 38.68 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 359 DVLHTVSLDIPAGHTVVLVGESGAGKSTLAALVAGLLEPRQGSI------------------TMTSGHARTV------LI 414
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqvielsEQSAAQMRHVrgadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 415 SQEIHTFSGTLF---DDVALGLAGQAEDWPDERVRDAVlAALERVgadwveQLPHGvDTVVGRLGIRLSPAQAQQVALAR 491
Cdd:PRK10261 110 FQEPMTSLNPVFtvgEQIAESIRLHQGASREEAMVEAK-RMLDQV------RIPEA-QTILSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 492 ALLADPPVIILDEATaeagssgaTALDRAAAEAVRGRTALV----------VAHRLSQVT-MADEVAVMDNGRIVEVGAP 560
Cdd:PRK10261 182 ALSCRPAVLIADEPT--------TALDVTIQAQILQLIKVLqkemsmgvifITHDMGVVAeIADRVLVMYQGEAVETGSV 253
|
...
gi 488473579 561 EQL 563
Cdd:PRK10261 254 EQI 256
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
128-293 |
9.90e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 38.22 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 128 VSRASDDVTAVRDAANGALPRLVNTMIMVIVSVGALASLHPLFFVPVLLAGVLYGLAIREFLRTAPPVYRAErnaSTTQS 207
Cdd:cd18606 95 LNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLE---SILRS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473579 208 qRILS----TIHGVDVVRAFGLE-----------NLRTRA----VANGSWQAIRWNlrgrFLGNTLVvrLLAGeavatig 268
Cdd:cd18606 172 -FVYAnfseSLSGLSTIRAYGAQdrfikknekliDNMNRAyfltIANQRWLAIRLD----LLGSLLV--LIVA------- 237
|
170 180
....*....|....*....|....*
gi 488473579 269 vawtgyLLVTTDRLSVGAAATAVLV 293
Cdd:cd18606 238 ------LLCVTRRFSISPSSTGLVL 256
|
|
| |
