|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-576 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 600.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 1 MKAShPKKIQKKLVQDLLSKKSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQW 80
Cdd:COG1132 1 MSKS-PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 81 INPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKI 160
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 161 DLLMLFLVLFLTPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQS 240
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 241 AIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILE 320
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 321 ESSPNITGTEKLDSSTVKGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL 400
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 401 DGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQ 480
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 481 GQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHS 560
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*.
gi 1091156555 561 ELMAQKGIYYQMQNAQ 576
Cdd:COG1132 560 ELLARGGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-576 |
5.95e-141 |
|
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: 425.02 E-value: 5.95e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 2 KASHPKKIQKKLVQDLLSKKSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWI 81
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 82 NPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTtDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKID 161
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 162 LLMLFLVLFLTPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSA 241
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 242 IFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILEE 321
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 322 SSPNITGTEKLDSSTVKGQIDFKNVIFGYNK-SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL 400
Cdd:COG2274 455 PPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 401 DGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQ 480
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 481 GQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHS 560
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
570
....*....|....*.
gi 1091156555 561 ELMAQKGIYYQMQNAQ 576
Cdd:COG2274 695 ELLARKGLYAELVQQQ 710
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-567 |
1.56e-116 |
|
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: 344.98 E-value: 1.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIG 418
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRI 498
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 499 LILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKG 567
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
341-573 |
1.15e-112 |
|
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: 335.35 E-value: 1.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNK-SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQ 573
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-576 |
1.58e-112 |
|
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: 347.09 E-value: 1.58e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVgMALLGTVVQVCLTVYLPVLIGQAVD--VVLSPHSMILLLPIMwkMVAVILANTIIQWINPLLYNRLIFHYVASL 97
Cdd:TIGR02203 13 KAGLV-LAGVAMILVAATESTLAALLKPLLDdgFGGRDRSVLWWVPLV--VIGLAVLRGICSFVSTYLLSWVSNKVVRDI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 98 RKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLF 177
Cdd:TIGR02203 90 RVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 178 LARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINS 257
Cdd:TIGR02203 170 LMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 258 LIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILEESSPNITGTEKLDSstV 337
Cdd:TIGR02203 250 LALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIER--A 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 338 KGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQE 416
Cdd:TIGR02203 328 RGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQETWLKSATIHDNIAYANPK-ASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKL 495
Cdd:TIGR02203 408 VALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 496 PRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIY---YQM 572
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
....
gi 1091156555 573 QNAQ 576
Cdd:TIGR02203 568 QFRE 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-576 |
2.65e-109 |
|
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: 339.87 E-value: 2.65e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 16 DLLSKKSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWkMVA---VILANTIIQWINPLLYNRLIFH 92
Cdd:COG5265 30 PYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGL-LLAyglLRLLSVLFGELRDALFARVTQR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 93 YVASLRKAVMEKLNLLPIAY-LDKR--GIGDLISRVTTDTEQLSNglLMVFNQFFVGLLTILVTIFSMAKIDllmlflvl 169
Cdd:COG5265 109 AVRRLALEVFRHLHALSLRFhLERQtgGLSRDIERGTKGIEFLLR--FLLFNILPTLLEIALVAGILLVKYD-------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 170 fltpLSLFLARFIAKKSYHLYqNQTASRGRqTQFIEEMVSQE---------SLI-----QAFSAQEESSDHFRTINQEYA 235
Cdd:COG5265 179 ----WWFALITLVTVVLYIAF-TVVVTEWR-TKFRREMNEADseantravdSLLnyetvKYFGNEAREARRYDEALARYE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 236 -------------NFSQSAIFYSSTVnpstrfinsliygFLAGIGALRIMSGAFSVGQLiTFLN-YVNQYTKPFNDISSV 301
Cdd:COG5265 253 raavksqtslallNFGQALIIALGLT-------------AMMLMAAQGVVAGTMTVGDF-VLVNaYLIQLYIPLNFLGFV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 302 LSEMQSALACAERLYSILEESsPNIT---GTEKLDSStvKGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGA 378
Cdd:COG5265 319 YREIRQALADMERMFDLLDQP-PEVAdapDAPPLVVG--GGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 379 GKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADF 458
Cdd:COG5265 396 GKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 459 FIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLST 538
Cdd:COG5265 476 FIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLST 555
|
570 580 590
....*....|....*....|....*....|....*...
gi 1091156555 539 IQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:COG5265 556 IVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-569 |
3.25e-107 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 333.59 E-value: 3.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:TIGR02204 17 RGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLS------------NGLLmvfnqFFVGLLTILVTIFSMAKIdlLMLFLV 168
Cdd:TIGR02204 97 VFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQsvigsslsmalrNALM-----CIGGLIMMFITSPKLTSL--VLLAVP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 169 LFLTPLSLFLARFiakksyhlyqnQTASRGRQTQFIE------EMVSQESLIQAFSAQEESSDHF-RTINQEYANFSQSa 241
Cdd:TIGR02204 170 LVLLPILLFGRRV-----------RKLSRESQDRIADagsyagETLGAIRTVQAFGHEDAERSRFgGAVEKAYEAARQR- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 242 IFYSSTVnpsTRFINSLIYGFLAG---IGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSI 318
Cdd:TIGR02204 238 IRTRALL---TAIVIVLVFGAIVGvlwVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 319 LEESsPNITG--TEKLDSSTVKGQIDFKNVIFGY--NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD 394
Cdd:TIGR02204 315 LQAE-PDIKApaHPKTLPVPLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 395 GGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDA 474
Cdd:TIGR02204 394 SGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 475 GDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIV 554
Cdd:TIGR02204 474 GVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
570
....*....|....*
gi 1091156555 555 EVGNHSELMAQKGIY 569
Cdd:TIGR02204 554 AQGTHAELIAKGGLY 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
94-576 |
2.99e-101 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 318.12 E-value: 2.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 94 VASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSN-----------------GL--LMVFNQFFVGLLTILVTi 154
Cdd:PRK11176 97 VMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASsssgalitvvregasiiGLfiMMFYYSWQLSLILIVIA- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 155 fsmakidllmlflvlfltPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEY 234
Cdd:PRK11176 176 ------------------PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 235 ANFSQSAIFYSSTVNPSTRFINSLIYGF---LAGIGALR--IMSGAFSV--GQLITFLnyvnqytKPFNDISSVLSEMQS 307
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLIASLALAFvlyAASFPSVMdtLTAGTITVvfSSMIALM-------RPLKSLTNVNAQFQR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 308 ALACAERLYSILEESSPNITGTEKLDssTVKGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINL 386
Cdd:PRK11176 311 GMAACQTLFAILDLEQEKDEGKRVIE--RAKGDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 387 LMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYA-NPKASRDEVIEAAKAANADFFIKQLPN 465
Cdd:PRK11176 389 LTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDN 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 466 GYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADII 545
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
490 500 510
....*....|....*....|....*....|.
gi 1091156555 546 LVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
341-576 |
1.12e-100 |
|
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: 304.54 E-value: 1.12e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILI 500
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 501 LDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
341-576 |
1.32e-97 |
|
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: 296.76 E-value: 1.32e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKP---LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEI 417
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-567 |
1.52e-97 |
|
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: 307.84 E-value: 1.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 6 PKKIQKKLVQDL-LSKKSLVGMALLGtVVQVCLTVYLPVLIGQAVD-VVLSPHSMILLLPIMWKMVAVILANTIIQWINp 83
Cdd:COG4988 1 QKPLDKRLKRLArGARRWLALAVLLG-LLSGLLIIAQAWLLASLLAgLIIGGAPLSALLPLLGLLLAVLLLRALLAWLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 84 llyNRLIFHY----VASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGL---LTILVTIFS 156
Cdd:COG4988 79 ---ERAAFRAaarvKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAAlvpLLILVAVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 157 MAKIDLLMLFLVLFLTPLSLFLARFIAKKsyhLYQNQTASRGR-QTQFIEeMVSQESLIQAFSAQEESSDHFRTINQEya 235
Cdd:COG4988 156 LDWLSGLILLVTAPLIPLFMILVGKGAAK---ASRRQWRALARlSGHFLD-RLRGLTTLKLFGRAKAEAERIAEASED-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 236 nFSQSAI------FYSSTVnpsTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSAL 309
Cdd:COG4988 230 -FRKRTMkvlrvaFLSSAV---LEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 310 ACAERLYSILEESSPNITGTEKLDSSTVKGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMR 389
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 390 FYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDT 469
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 470 YLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMV 549
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLD 545
|
570
....*....|....*...
gi 1091156555 550 SGEIVEVGNHSELMAQKG 567
Cdd:COG4988 546 DGRIVEQGTHEELLAKNG 563
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-572 |
4.17e-97 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 310.89 E-value: 4.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 12 KLVQDLLSKKSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIF 91
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 92 HYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFL 171
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLIN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 172 TPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPS 251
Cdd:TIGR00958 311 LPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 252 TRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILEESsPNITGTEK 331
Cdd:TIGR00958 391 TSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRK-PNIPLTGT 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 332 LDSSTVKGQIDFKNVIFGY--NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYE 409
Cdd:TIGR00958 470 LAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 410 PSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIA 489
Cdd:TIGR00958 550 HHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 490 RIFLKLPRILILDEATSSIDTRTEVLVQEAfqMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIY 569
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
...
gi 1091156555 570 YQM 572
Cdd:TIGR00958 708 KHL 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
88-572 |
6.27e-95 |
|
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: 301.30 E-value: 6.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 88 RLIFHYV-----ASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDL 162
Cdd:COG4987 76 RLVSHDAtlrllADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 163 LMLFLVLFLTPLSLFLARFIA-KKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANfSQSA 241
Cdd:COG4987 156 ALALVLALGLLLAGLLLPLLAaRLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAA-AQRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 242 IFYSSTVnpsTRFINSLIYGfLAGIGALRIMSGAFSVGQL-------ITFLnyvnqytkP------FNDISSVLSEMQSA 308
Cdd:COG4987 235 LARLSAL---AQALLQLAAG-LAVVAVLWLAAPLVAAGALsgpllalLVLA--------AlalfeaLAPLPAAAQHLGRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 309 LACAERLYSILEESsPNITGTEKLDSSTVKGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLL 387
Cdd:COG4987 303 RAAARRLNELLDAP-PAVTEPAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 388 MRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGY 467
Cdd:COG4987 382 LRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 468 DTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILV 547
Cdd:COG4987 462 DTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILV 541
|
490 500
....*....|....*....|....*
gi 1091156555 548 MVSGEIVEVGNHSELMAQKGIYYQM 572
Cdd:COG4987 542 LEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
27-314 |
3.59e-91 |
|
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: 282.37 E-value: 3.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMIL------LLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLAR 180
Cdd:cd18547 84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 181 FIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIY 260
Cdd:cd18547 164 FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGY 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 261 GFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18547 244 VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
42-576 |
3.60e-84 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 276.62 E-value: 3.60e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 42 PVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDL 121
Cdd:TIGR01846 159 PLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 122 ISRVTtDTEQLSN-----GLLMVFNQFFVgLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKsyhlYQNQTAS 196
Cdd:TIGR01846 239 VARVR-ELEQIRNfltgsALTVVLDLLFV-VVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKR----VEDKFER 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 197 RGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAF 276
Cdd:TIGR01846 313 SAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 277 SVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILEESSPNiTGTEKLDSSTVKGQIDFKNVIFGYNKSKP- 355
Cdd:TIGR01846 393 SPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEP-RSAGLAALPELRGAITFENIRFRYAPDSPe 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNI 435
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 AYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVL 515
Cdd:TIGR01846 552 ALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEAL 631
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 516 VQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:TIGR01846 632 IMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-576 |
7.17e-83 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 270.44 E-value: 7.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLvGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMilllPimWKMVAVILANTI--------IQWINPLLYNRLIF 91
Cdd:PRK10790 22 RKPL-GLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNL----P--LGLVAGLAAAYVglqllaagLHYAQSLLFNRAAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 92 HYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFF-----VGllTILVTIFS----MAKIdl 162
Cdd:PRK10790 95 GVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLrsaalIG--AMLVAMFSldwrMALV-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 163 lmlflvlfltPLSLFLARFIAKKSYHLYQNQTASRGRQ-----TQFIEEMVSQESLIQAFSAQEESSDHFRTINQE-YAN 236
Cdd:PRK10790 171 ----------AIMIFPAVLVVMVIYQRYSTPIVRRVRAyladiNDGFNEVINGMSVIQQFRQQARFGERMGEASRShYMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 237 FSQSAIFYSSTVNPSTRFINSLI-------YGFLAgigalrimSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSAL 309
Cdd:PRK10790 241 RMQTLRLDGFLLRPLLSLFSALIlcgllmlFGFSA--------SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 310 ACAERLYSILEESSPNITGTEKLDSStvkGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMR 389
Cdd:PRK10790 313 VAGERVFELMDGPRQQYGNDDRPLQS---GRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 390 FYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPkASRDEVIEAAKAANADFFIKQLPNGYDT 469
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 470 YLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMV 549
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLH 548
|
570 580
....*....|....*....|....*..
gi 1091156555 550 SGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:PRK10790 549 RGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-576 |
2.98e-81 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 266.06 E-value: 2.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 17 LLSKKSLVGMALLGTVVQVCLTVYLPVLIGQAVDVvLSPHSMILLLPIMWkmVAVILANTIIQWINPLLYNRLIFHYVAS 96
Cdd:PRK13657 14 LGAEKRLGILLAVANVLLAAATFAEPILFGRIIDA-ISGKGDIFPLLAAW--AGFGLFNIIAGVLVARHADRLAHRRRLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 97 LRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSL 176
Cdd:PRK13657 91 VLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSLVLVVLGIVYT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 177 FLARFIAKKSYHL------YQNQTASRgrqtqfIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNP 250
Cdd:PRK13657 171 LITTLVMRKTKDGqaaveeHYHDLFAH------VSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 251 STRFINSL-IYGFLAgIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSiLEESSPNITGT 329
Cdd:PRK13657 245 LNRAASTItMLAILV-LGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFE-VEDAVPDVRDP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 330 EKL-DSSTVKGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDY 408
Cdd:PRK13657 323 PGAiDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 409 EPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTI 488
Cdd:PRK13657 403 TRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 489 ARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGI 568
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGR 562
|
....*...
gi 1091156555 569 YYQMQNAQ 576
Cdd:PRK13657 563 FAALLRAQ 570
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-576 |
1.09e-75 |
|
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: 240.08 E-value: 1.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL-LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:cd03252 1 ITFEHVRFRYKPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQ 576
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
339-558 |
1.03e-70 |
|
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: 226.61 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNK-SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEI 417
Cdd:cd03244 1 GDIEFKNVSLRYRPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANpKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGN 558
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-548 |
1.85e-68 |
|
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: 218.79 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIHDNIayanpkasrdevieaakaanadffikqlpngydtyledagdsLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVM 548
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
14-572 |
2.27e-66 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 228.69 E-value: 2.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 14 VQDLLSkksLVGMALLGTVvqvcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHY 93
Cdd:TIGR03797 135 RRDLLA---ILAMGLLGTL----LGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 94 VASLRKAVMEKLNLLPIAYLDKRGIGDLISR---VTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLF 170
Cdd:TIGR03797 208 DASLQAAVWDRLLRLPVSFFRQYSTGDLASRamgISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 171 LTPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMvsqeSLIQAFSAQEESsdhFRTINQEYAnfSQSAIFYSstvnp 250
Cdd:TIGR03797 288 AIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGI----SKLRVAGAENRA---FARWAKLFS--RQRKLELS----- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 251 sTRFINSLIYGFLAGIGALRIM-----------SGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSIL 319
Cdd:TIGR03797 354 -AQRIENLLTVFNAVLPVLTSAalfaaaisllgGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPIL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 320 EeSSPNITGtEKLDSSTVKGQIDFKNVIFGYNKSKPL-LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:TIGR03797 433 E-ALPEVDE-AKTDPGKLSGAIEVDRVTFRYRPDGPLiLDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 399 LLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPkASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSL 478
Cdd:TIGR03797 511 FYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTL 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 479 SQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLmkGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGN 558
Cdd:TIGR03797 590 SGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGT 667
|
570
....*....|....
gi 1091156555 559 HSELMAQKGIYYQM 572
Cdd:TIGR03797 668 YDELMAREGLFAQL 681
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-548 |
2.81e-66 |
|
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: 224.86 E-value: 2.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVGMALLGtVVQVCLTVYLPVLIGQAVDVVLSP-HSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLR 98
Cdd:TIGR02857 2 RRALALLALLG-VLGALLIIAQAWLLARVVDGLISAgEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 99 KAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNgllmVFNQFFVGL-------LTILVTIFSmakIDLLMLFLVLFL 171
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDG----YFARYLPQLvlavivpLAILAAVFP---QDWISGLILLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 172 TPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIfysstvnpS 251
Cdd:TIGR02857 154 APLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVL--------R 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 252 TRFINSLIYGFLAGIG--------ALRIMSG--AFSVGQLITFLnyVNQYTKPFNDISSVLSEMQSALACAERLYSILEE 321
Cdd:TIGR02857 226 IAFLSSAVLELFATLSvalvavyiGFRLLAGdlDLATGLFVLLL--APEFYLPLRQLGAQYHARADGVAAAEALFAVLDA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 322 SSPNITGTEKLDSsTVKGQIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLD 401
Cdd:TIGR02857 304 APRPLAGKAPVTA-APASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 402 GKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQG 481
Cdd:TIGR02857 383 GVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 482 QCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVM 548
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-554 |
3.65e-66 |
|
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: 214.76 E-value: 3.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKSK-PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEI 417
Cdd:cd03245 1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIV 554
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
336-553 |
4.36e-66 |
|
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: 214.64 E-value: 4.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 336 TVKGQIDFKNVIFGYNK--SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL 413
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFL 493
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEI 553
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-572 |
1.30e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.84 E-value: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 309 LACAERLYSILEESsPNITGTEKLDSSTVKGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLL 387
Cdd:PRK11160 308 IASARRINEITEQK-PEVTFPTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 388 MRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQlPNGY 467
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 468 DTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILV 547
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
250 260
....*....|....*....|....*
gi 1091156555 548 MVSGEIVEVGNHSELMAQKGIYYQM 572
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
308-577 |
8.00e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 200.84 E-value: 8.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 308 ALACAERLYSILEESSPNITGTEKLDSSTVKGQIDFKN-VIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINL 386
Cdd:PRK11174 317 AVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDlEILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 387 LMRF--YEvdgGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLP 464
Cdd:PRK11174 396 LLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 465 NGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADI 544
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQ 552
|
250 260 270
....*....|....*....|....*....|...
gi 1091156555 545 ILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQK 577
Cdd:PRK11174 553 IWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
42-577 |
2.02e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 193.78 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 42 PVLIGQAVDVVlSPHSMILLLPIMWkmVAVILANTIIQWINPLLYNRLIF----HYVASLRKAVMEKLNL-LPIAYLDKR 116
Cdd:PRK10789 15 PKVVGIIVDGV-TEQHMTTGQILMW--IGTMVLIAVVVYLLRYVWRVLLFgasyQLAVELREDFYRQLSRqHPEFYLRHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 117 gIGDLISRVTTDTEQL----SNGLLMVFNQFFVGLLTILVtifsMAkidllmLFLVLFLTPLSL----FLARFIAKKSYH 188
Cdd:PRK10789 92 -TGDLMARATNDVDRVvfaaGEGVLTLVDSLVMGCAVLIV----MS------TQISWQLTLLALlpmpVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 189 LYQN----QTA--SRGRQTQfieEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPsTRFINSLIYGF 262
Cdd:PRK10789 161 LHERfklaQAAfsSLNDRTQ---ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP-TIYIAIGMANL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 263 LA-GIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSILEESSPNITGTEKLDSSTVKGQI 341
Cdd:PRK10789 237 LAiGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 342 DFKNviFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:PRK10789 317 NIRQ--FTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILI 500
Cdd:PRK10789 395 SQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 501 LDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQMQNAQK 577
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQ 551
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
88-536 |
1.77e-52 |
|
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: 187.57 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 88 RLIFHYVA-----SLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDL 162
Cdd:TIGR02868 74 RLVGHDAAlrslgALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 163 LMLFLVLFLTPLSLFLARFI---AKKSYHlyQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQ 239
Cdd:TIGR02868 154 PAALILAAGLLLAGFVAPLVslrAARAAE--QALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 240 SAifysSTVNPSTRFINSLIYGfLAGIGALRIMSGAFSVGQL----ITFLNYVN-QYTKPFNDISSVLSEMQSALACAER 314
Cdd:TIGR02868 232 RA----AAATALGAALTLLAAG-LAVLGALWAGGPAVADGRLapvtLAVLVLLPlAAFEAFAALPAAAQQLTRVRAAAER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 315 LYSILEESSPNITGTEKLDSSTVKG--QIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYE 392
Cdd:TIGR02868 307 IVEVLDAAGPVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 393 VDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLE 472
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLG 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 473 DAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRL 536
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
109-572 |
6.69e-51 |
|
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: 189.39 E-value: 6.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 109 PIAYLDKRGIGDLISRVTTDT----EQLSNGLLMVFNQFFVGLLTILVTIFSMAkidllmlFLVLFLTPLSL---FLARF 181
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELdtvdSMIPPVIKMFMGSLFNVIGALIVILLATP-------IAAVIIPPLGLlyfFVQRF 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 182 IAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEEssdhFRTINQEYANFSQSAIFYSSTVNP----STRFINS 257
Cdd:TIGR00957 1125 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQER----FIHQSDLKVDENQKAYYPSIVANRwlavRLECVGN 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 258 LIYGFLAGIGAlrIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL--YSILEESSP-NITGTEKLDS 334
Cdd:TIGR00957 1201 CIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPwQIQETAPPSG 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 335 STVKGQIDFKNVIFGYNKSKPL-LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL 413
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYREDLDLvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQETWLKSATIHDNIayaNP--KASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARI 491
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 492 FLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQ 571
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
.
gi 1091156555 572 M 572
Cdd:TIGR00957 1516 M 1516
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
305-565 |
2.89e-50 |
|
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: 182.26 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 305 MQSALACAERLYSILEESSPNitgTEKLDSSTVKGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTL 383
Cdd:COG4618 298 FVSARQAYRRLNELLAAVPAE---PERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 384 INLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYAnPKASRDEVIEAAKAANADFFIKQL 463
Cdd:COG4618 375 ARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARF-GDADPEKVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 464 PNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML-MKGRTSFIIAHRLSTIQTA 542
Cdd:COG4618 454 PDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAV 533
|
250 260
....*....|....*....|...
gi 1091156555 543 DIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG4618 534 DKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-565 |
7.90e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 175.23 E-value: 7.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 19 SKKSLVGMALLGTVVQVcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLR 98
Cdd:TIGR01842 4 VKRTFIIVGLFSFVINI-LMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 99 KAVMEKLNLLPIAYLDKRGigdliSRVTTDTEQL-----SNGLLMVFN--------------QFFVGLLTILVTIFSMAk 159
Cdd:TIGR01842 83 QPIFAASFSATLRRGSGDG-----LQALRDLDQLrqfltGPGLFAFFDapwmpiyllvcfllHPWIGILALGGAVVLVG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 160 idllmlflvlfltpLSLFLARFIAKKsyhlYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQ 239
Cdd:TIGR01842 157 --------------LALLNNRATKKP----LKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 240 SAIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERLYSIL 319
Cdd:TIGR01842 219 AASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 320 EESSPNitgTEKLDSSTVKGQIDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:TIGR01842 299 ANYPSR---DPAMPLPEPEGHLSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 399 LLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSL 478
Cdd:TIGR01842 376 RLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 479 SQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTIQTADIILVMVSGEIVEVG 557
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
....*...
gi 1091156555 558 NHSELMAQ 565
Cdd:TIGR01842 536 ERDEVLAK 543
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
27-315 |
5.22e-47 |
|
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: 166.57 E-value: 5.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKS 186
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 187 YHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGI 266
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1091156555 267 GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd07346 244 GGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
341-566 |
5.52e-45 |
|
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: 159.03 E-value: 5.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFfikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIflkL- 495
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEALELV-------GLEHLADRPPHELSGGQKQRVAIAGV---La 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 496 --PRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA-HRLSTI-QTADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:COG1122 151 mePEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
339-557 |
9.44e-45 |
|
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: 157.57 E-value: 9.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYN-KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEI 417
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANpKASRDEVIEAAKAAnadffikqlpngydtyleDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVG 557
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
230-569 |
4.46e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 169.05 E-value: 4.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 230 INQEYANFSQSAIFysstvnpstrFINSLIYGFlagiGALRIMSGAFSVG----QLITFLnYVNQYTkpfNDISSVLSEM 305
Cdd:PTZ00265 1065 VNSMLWGFSQSAQL----------FINSFAYWF----GSFLIRRGTILVDdfmkSLFTFL-FTGSYA---GKLMSLKGDS 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 306 QSALACAERLYSILEESSpNIT-----GTEKLDSSTVKGQIDFKNVIFGY--NKSKPLLNGINLHIPAGAKVAIVGPTGA 378
Cdd:PTZ00265 1127 ENAKLSFEKYYPLIIRKS-NIDvrdngGIRIKNKNDIKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGS 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 379 GKSTLINLLMRFYEV------------------------------------------------------DGGNILLDGKP 404
Cdd:PTZ00265 1206 GKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVD 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 405 ITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQ 484
Cdd:PTZ00265 1286 ICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQ 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 485 LLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQTADIILVM----VSGEIVEV-G 557
Cdd:PTZ00265 1366 RIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAhG 1445
|
410
....*....|...
gi 1091156555 558 NHSELM-AQKGIY 569
Cdd:PTZ00265 1446 THEELLsVQDGVY 1458
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-314 |
7.46e-44 |
|
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: 157.93 E-value: 7.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMIL--LLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEK 104
Cdd:cd18544 4 ALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLqgLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 105 LNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAK 184
Cdd:cd18544 84 IQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 185 KSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLA 264
Cdd:cd18544 164 KSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1091156555 265 GIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18544 244 WYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-553 |
5.02e-43 |
|
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: 151.60 E-value: 5.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIHDNIayanpkasrdevieaakaanadffikqlpngydtyledagdsLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQML-MKGRTSFIIAHRLSTIQTADIILVMVSGEI 553
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-567 |
1.37e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 164.38 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 28 LLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIM-WKMVAVILANTIiqWinpLLYNRLifHYVASLRKAVMEKLN 106
Cdd:PLN03232 922 LTTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLgFGQVAVTFTNSF--W---LISSSL--HAAKRLHDAMLNSIL 994
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTifsMAKIDLLMLFLVLFLTPL-SLFLARFIAKK 185
Cdd:PLN03232 995 RAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLST---FALIGTVSTISLWAIMPLlILFYAAYLYYQ 1071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 186 SYHLYQNQTASRGRQTQFIE--EMVSQESLIQAFSAQeessDHFRTINQEYANfsqSAIFYSSTVNPSTRFINSLiygfL 263
Cdd:PLN03232 1072 STSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAY----DRMAKINGKSMD---NNIRFTLANTSSNRWLTIR----L 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 264 AGIGALRI-MSGAFSVGQ-------------LITFLNYVNQYTKPFNDISSVLSEMQSALACAERL--YSILEESSPNIT 327
Cdd:PLN03232 1141 ETLGGVMIwLTATFAVLRngnaenqagfastMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVgnYIDLPSEATAII 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 328 GTEKLDSS-TVKGQIDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPI 405
Cdd:PLN03232 1221 ENNRPVSGwPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV 1300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 406 TDYEPSQLRQEIGMVLQETWLKSATIHDNIayaNPKASRDE--VIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQC 483
Cdd:PLN03232 1301 AKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDadLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQR 1377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 484 QLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PLN03232 1378 QLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
....
gi 1091156555 564 AQKG 567
Cdd:PLN03232 1458 SRDT 1461
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
317-566 |
4.05e-41 |
|
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: 149.29 E-value: 4.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 317 SILEESSPNITGtekldsstVKGQIDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG 395
Cdd:cd03288 4 SISGSSNSGLVG--------LGGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 396 GNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIayaNP--KASRDEVIEAAKAANADFFIKQLPNGYDTYLED 473
Cdd:cd03288 76 GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 474 AGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEI 553
Cdd:cd03288 153 GGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
250
....*....|...
gi 1091156555 554 VEVGNHSELMAQK 566
Cdd:cd03288 233 VECDTPENLLAQE 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-567 |
2.28e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 154.51 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEI 417
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANPKASRDeVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEHNDAD-LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKG 567
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
357-506 |
1.05e-38 |
|
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: 138.93 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSA-TIHDNI 435
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 436 AYAnpkASRDEVIEAAKAANADFFIKQLPNGY--DTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATS 506
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
26-314 |
3.96e-38 |
|
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: 142.22 E-value: 3.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 26 MALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKL 105
Cdd:cd18545 4 LALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 106 NLLPIAYLDKRGIGDLISRVTTDTEQL----SNGLLMVFNQFFvgllTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARF 181
Cdd:cd18545 84 QKLSFSFFDSRPVGKILSRVINDVNSLsdllSNGLINLIPDLL----TLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 182 IAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYG 261
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 262 FLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18545 240 LVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
341-562 |
4.42e-37 |
|
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: 137.31 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEV-----DGGNILLDGKPIT--DYEPSQL 413
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYdlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQETWLKSATIHDNIAYA------NPKASRDEVIEAA--KAANADFFIKQLpngydtyledAGDSLSQGQCQL 485
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrKAALWDEVKDRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 486 LTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVGNHSEL 562
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-552 |
7.17e-37 |
|
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: 136.06 E-value: 7.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 343 FKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVL 421
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 422 Q--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFFIKQLPNgYDTYledagdSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-RSPF------TLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA-HRLSTI-QTADIILVMVSGE 552
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-552 |
2.22e-35 |
|
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: 130.06 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 343 FKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQ 422
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 etwlksatihdniayanpkasrdevieaakaanadffikqlpngydtyledagdsLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 503 EATSSIDTRTEVLVQEAF-QMLMKGRTSFIIAHRLSTIQTA-DIILVMVSGE 552
Cdd:cd00267 106 EPTSGLDPASRERLLELLrELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
24-315 |
2.30e-35 |
|
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: 134.48 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 24 VGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLpimWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVME 103
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 104 KLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIA 183
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 184 KKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFL 263
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 264 AGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
27-315 |
6.34e-35 |
|
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: 133.32 E-value: 6.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLS--PHSMILLLPIMwkMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEK 104
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLDDIFVekDLEALLLVPLA--IIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 105 LNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAK 184
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 185 KSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLA 264
Cdd:cd18552 162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 265 GIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18552 242 WYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-314 |
1.33e-34 |
|
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: 132.28 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 24 VGMALLGTVVQVcltvYLPVLIGQAVD-VVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVM 102
Cdd:cd18778 5 LLCALLSTLLGL----VPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 103 EKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFI 182
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 183 AKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGF 262
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 263 LAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-565 |
2.23e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.57 E-value: 2.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG---GNILLDGKPITDYEPSQLRQE 416
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQE--TWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFfikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIF 492
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAV-------GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
308-565 |
2.50e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.57 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 308 ALACAERLYSILEESSPNITGTEKLdsstvkgqIDFKNVIFGYNKSKP----LLNGINLHIPAGAKVAIVGPTGAGKSTL 383
Cdd:COG1123 236 ALAAVPRLGAARGRAAPAAAAAEPL--------LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 384 INLLMRFYEVDGGNILLDGKPITDY---EPSQLRQEIGMVLQ-------ETWlksaTIHDNIAYA---NPKASRDEVIEA 450
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQdpysslnPRM----TVGDIIAEPlrlHGLLSRAERRER 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 451 AKAANADFfikQLPngydtylEDAGD----SLSQGQCQLLTIARIFLKLPRILILDEATSSID--TRTEVL-----VQEA 519
Cdd:COG1123 384 VAELLERV---GLP-------PDLADryphELSGGQRQRVAIARALALEPKLLILDEPTSALDvsVQAQILnllrdLQRE 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1091156555 520 FqmlmkGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG1123 454 L-----GLTYLFISHDLAVVrYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
182-577 |
4.56e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 138.62 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 182 IAKKSYHLYQNQTASrgrqtqFIEEMVSQESLIQAFSAQeessdhfRTINQEyanFSQSAIFYSSTVNPSTrFINSLIYG 261
Cdd:PTZ00265 223 INKKTSLLYNNNTMS------IIEEALVGIRTVVSYCGE-------KTILKK---FNLSEKLYSKYILKAN-FMESLHIG 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 262 FLAGIgALRIMSGAFSVGQLITFLNYVNQYtkPFNDI--SSVLSEMQSALACAERLYSILeessPNIT-------GTEKL 332
Cdd:PTZ00265 286 MINGF-ILASYAFGFWYGTRIIISDLSNQQ--PNNDFhgGSVISILLGVLISMFMLTIIL----PNITeymksleATNSL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 333 --------------DSSTVKG--QIDFKNVIFGYNKSK--PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD 394
Cdd:PTZ00265 359 yeiinrkplvenndDGKKLKDikKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 395 GGNILL-DGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIAYA----------------NPKASRD------------ 445
Cdd:PTZ00265 439 EGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakc 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 446 -----------------------------EVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLP 496
Cdd:PTZ00265 519 agdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 497 RILILDEATSSIDTRTEVLVQEAFQMLmKG---RTSFIIAHRLSTIQTADIILVMVSGE--------------------- 552
Cdd:PTZ00265 599 KILILDEATSSLDNKSEYLVQKTINNL-KGnenRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnken 677
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 553 --------------------------IVEVGNHSELMAQK-GIYYQMQNAQK 577
Cdd:PTZ00265 678 nnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQK 729
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
23-314 |
4.58e-34 |
|
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: 131.09 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 23 LVGMALLgTVVQVCLTVYLPVLIGQAVDVVLSP----HSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLR 98
Cdd:cd18563 1 LILGFLL-MLLGTALGLVPPYLTKILIDDVLIQlgpgGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 99 KAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFL 178
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 179 ARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSL 258
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 259 IYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18563 240 GTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
353-557 |
1.36e-33 |
|
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: 127.25 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSqlRQEIGMVLQE----TWLks 428
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDyalfPHL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 aTIHDNIAYA-----NPKASRDE-VIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:cd03259 88 -TVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 503 EATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-557 |
2.66e-33 |
|
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: 125.12 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEpSQLRQEIGM 419
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIHDNIayanpkasrdevieaakaanadffikqlpngydtyledaGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVG 557
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
341-565 |
1.11e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 125.18 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyEPSQLRQEIGMV 420
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWL-KSATIHDNI-----AYANPKASRDEVIEAAkaanADFFikqlpnGydtyLEDAGD----SLSQGQCQLLTIAR 490
Cdd:COG1131 79 PQEPALyPDLTVRENLrffarLYGLPRKEARERIDEL----LELF------G----LTDAADrkvgTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 491 IFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
341-564 |
1.39e-32 |
|
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: 125.49 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWL-KSATIHDNIAYAnPKASRDEviEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:cd03295 81 IQQIGLfPHMTVEENIALV-PKLLKWP--KEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRL-STIQTADIILVMVSGEIVEVGNHSELMA 564
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
345-557 |
1.46e-32 |
|
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: 124.93 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFG-YNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---RQEIGMV 420
Cdd:cd03257 8 SVSFPtGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQE-------TWlksaTIHDNIAYANPKASRDEVIEAAKAANADFFIK-QLPngyDTYLEDAGDSLSQGQCQLLTIARIF 492
Cdd:cd03257 88 FQDpmsslnpRM----TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLP---EEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVLVQEAFQML--MKGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
88-575 |
1.56e-32 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 133.75 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 88 RLIFHYVA------SLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVF----NQFFVGLLTILVTIFSM 157
Cdd:PTZ00243 1018 RFFLSYEAmrrgsrNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYlyllQCLFSICSSILVTSASQ 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 158 akidllmlflvlfltPLSLFLARFIAKKSYHLYQNQTASRgrqtqfiEEMVSQESLIQA--FSAQEESSDHFRTINQeYA 235
Cdd:PTZ00243 1098 ---------------PFVLVALVPCGYLYYRLMQFYNSAN-------REIRRIKSVAKSpvFTLLEEALQGSATITA-YG 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 236 NFS---QSA-----IFYSSTV--NPSTR-------FINSLIYGFLAGIGALRIMSGAFS--VGQLITFLNYVNQYTKPFN 296
Cdd:PTZ00243 1155 KAHlvmQEAlrrldVVYSCSYleNVANRwlgvrveFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLN 1234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 297 DISSVLSEMQSALACAER-LYSILE---ESSPNI----------TGTEKLDSSTV----------------KGQIDFKNV 346
Cdd:PTZ00243 1235 WLVRQVATVEADMNSVERlLYYTDEvphEDMPELdeevdalerrTGMAADVTGTVviepasptsaaphpvqAGSLVFEGV 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 347 IFGYNKSKPL-LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETW 425
Cdd:PTZ00243 1315 QMRYREGLPLvLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPV 1394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 426 LKSATIHDNIayaNP--KASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILIL-D 502
Cdd:PTZ00243 1395 LFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmD 1471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 503 EATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSEL-MAQKGIYYQMQNA 575
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEA 1545
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
341-552 |
3.57e-32 |
|
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: 122.96 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNK----SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKpitdyepsqlrqe 416
Cdd:cd03250 1 ISVEDASFTWDSgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQETWLKSATIHDNIAYANP--KASRDEVIEAAkAANADffIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLK 494
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKAC-ALEPD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 495 LPRILILDEATSSIDTRTEV-LVQEAFQ-MLMKGRTSFIIAHRLSTIQTADIILVMVSGE 552
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRhIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
341-567 |
5.61e-32 |
|
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: 123.81 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdYEPSQLRQEIGMV 420
Cdd:COG4555 2 IEVENLSKKYGK-VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWL-KSATIHDNIAYANpkASRDEVIEAAKAAnADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:COG4555 80 PDERGLyDRLTVRENIRYFA--ELYGLFDEELKKR-IEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA-HRLSTI-QTADIILVMVSGEIVEVGNHSELMAQKG 567
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-315 |
1.16e-31 |
|
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: 124.08 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKS 186
Cdd:cd18542 84 RLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 187 YHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGI 266
Cdd:cd18542 164 RPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1091156555 267 GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18542 244 GGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
341-565 |
3.06e-31 |
|
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: 121.15 E-value: 3.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV--IFGYNKSK-PLLNGINLHIPAGAKVAIVGPTGAGKSTL---INLLMRFyevDGGNILLDGKPITDYEPSQL- 413
Cdd:cd03258 2 IELKNVskVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERP---TSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 --RQEIGMVLQE-TWLKSATIHDNIAYA-----NPKASRDEVIEA-----AKAANADFFIKQlpngydtyledagdsLSQ 480
Cdd:cd03258 79 kaRRRIGMIFQHfNLLSSRTVFENVALPleiagVPKAEIEERVLEllelvGLEDKADAYPAQ---------------LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 481 GQCQLLTIARIFLKLPRILILDEATSSIDTRTevlVQEAFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSGEIV 554
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVkRICDRVAVMEKGEVV 220
|
250
....*....|.
gi 1091156555 555 EVGNHSELMAQ 565
Cdd:cd03258 221 EEGTVEEVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
341-552 |
5.76e-31 |
|
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: 118.83 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYE--PSQLRQEIG 418
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWLKS-ATIHDNIAYAnpkasrdevieaakaanadffikqlpngydtyledagdsLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03229 80 MVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 498 ILILDEATSSID--TRTEV--LVQEAFQMLmkGRTSFIIAHRLSTIQT-ADIILVMVSGE 552
Cdd:cd03229 121 VLLLDEPTSALDpiTRREVraLLKSLQAQL--GITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
341-563 |
4.48e-30 |
|
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: 118.61 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:COG1120 2 LEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETwlkSA----TIHDNIAY---------ANPKASRDEVIEAAkaanadffikqlpngydtyLEDAG---------DSL 478
Cdd:COG1120 81 PQEP---PApfglTVRELVALgryphlglfGRPSAEDREAVEEA-------------------LERTGlehladrpvDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 479 SQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML--MKGRTSFIIAHRLS-TIQTADIILVMVSGEIVE 555
Cdd:COG1120 139 SGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVA 218
|
....*...
gi 1091156555 556 VGNHSELM 563
Cdd:COG1120 219 QGPPEEVL 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
341-557 |
4.57e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ---LRQEI 417
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWL-KSATIHDNIAYA------NPKASRDEVIEA-------AKAanadffiKQLPngydtyledagDSLSQGQC 483
Cdd:COG2884 82 GVVFQDFRLlPDRTVYENVALPlrvtgkSRKEIRRRVREVldlvglsDKA-------KALP-----------HELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 484 QLLTIARIFLKLPRILILDEATSSIDTRT--EVLvqEAFQMLMKGRTSFIIA-HRLSTIQTADI-ILVMVSGEIVEVG 557
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETswEIM--ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-564 |
5.36e-30 |
|
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: 118.37 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQE 423
Cdd:COG1124 8 SVSYGQgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 twlksatihdniAYA--NPKASRDEVI-EAAKAANadffIKQLPNGYDTYLEDAG----------DSLSQGQCQLLTIAR 490
Cdd:COG1124 88 ------------PYAslHPRHTVDRILaEPLRIHG----LPDREERIAELLEQVGlppsfldrypHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 491 IFLKLPRILILDEATSSID--TRTEVLvqEAFQMLMK--GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMA 564
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvsVQAEIL--NLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
341-565 |
1.09e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKL 495
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGleNIGVPREEMVERVDQA-----LRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 496 PRILILDEATSSIDT--RTEVLvqEAFQML--MKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK13635 159 PDIIILDEATSMLDPrgRREVL--ETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
344-557 |
1.37e-29 |
|
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: 114.84 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQe 423
Cdd:cd03214 3 ENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 twlksatihdniayanpkasrdeVIEAAKAAN-ADFFIkqlpngydtyledagDSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:cd03214 81 -----------------------ALELLGLAHlADRPF---------------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 503 EATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLS-TIQTADIILVMVSGEIVEVG 557
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
23-315 |
1.59e-29 |
|
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: 118.28 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 23 LVGMALLgtVVQVCLTVYLPVLIGQAVDVVLSP-HSMILLLPIMWKMVAVILANTIIQWinplLYNRLIFhyVAS----- 96
Cdd:cd18541 2 LLGILFL--ILVDLLQLLIPRIIGRAIDALTAGtLTASQLLRYALLILLLALLIGIFRF----LWRYLIF--GASrriey 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 97 -LRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSN----GLLMVFNqffvGLLTILVTIFSMAKIDLLMLFLVLFL 171
Cdd:cd18541 74 dLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMalgpGILYLVD----ALFLGVLVLVMMFTISPKLTLIALLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 172 TPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPS 251
Cdd:cd18541 150 LPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 252 TRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18541 230 IGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
23-315 |
7.02e-29 |
|
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: 116.43 E-value: 7.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 23 LVGMALLgtVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVM 102
Cdd:cd18546 2 ALALLLV--VVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 103 EKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFI 182
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 183 AKKSYHLYqnqTASRGRqtqfIEEMVS--QESL-----IQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFI 255
Cdd:cd18546 160 RRRSSRAY---RRARER----IAAVNAdlQETLagirvVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 256 NSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18546 233 GNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
341-556 |
1.68e-28 |
|
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: 113.34 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY---NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPsqlrqEI 417
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQET----WLksaTIHDNIAYAnPKASRdeVIEAAKAANADFFIKQLPngydtyLEDAGDS----LSQGQCQLLTIA 489
Cdd:cd03293 76 GYVFQQDallpWL---TVLDNVALG-LELQG--VPKAEARERAEELLELVG------LSGFENAyphqLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 490 RIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLS-TIQTADIILVM--VSGEIVEV 556
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-564 |
1.79e-28 |
|
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: 113.30 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKSkPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMVLQ 422
Cdd:cd03224 4 ENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 ETWL-KSATIHDNI---AYANPKASRDEVIEAAKaanaDFF--IKQLpngydtyLEDAGDSLSQGQCQLLTIARIFLKLP 496
Cdd:cd03224 83 GRRIfPELTVEENLllgAYARRRAKRKARLERVY----ELFprLKER-------RKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 497 RILILDEATSSIdtrTEVLVQEAFQMLMK----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:cd03224 152 KLLLLDEPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-568 |
2.55e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQ--ETWLKSATIHDNIAYA------NPKASRDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARI 491
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 492 FLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA--HRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGI 568
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
357-561 |
2.99e-28 |
|
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: 112.81 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSqlRQEIGMVLQETWL-KSATIHDNI 435
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALfPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 AYA-----NPKASRDE-VIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFLKLPRILILDEATSSID 509
Cdd:cd03299 93 AYGlkkrkVDKKEIERkVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 510 TRT-EVLVQEAFQMLMKGRTSFI-IAHRLSTIQT-ADIILVMVSGEIVEVGNHSE 561
Cdd:cd03299 162 VRTkEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
24-295 |
4.93e-28 |
|
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: 113.51 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 24 VGMALLGTVVQVCLTVYLPVLIGQAVDVVL---SPHSMILLLPIMWkMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdgDPETQALNVYSLA-LLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLAR 180
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 181 FIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIY 260
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1091156555 261 GFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPF 295
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
341-555 |
6.90e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 111.67 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSK---PLLNGINLHIPAGAKVAIVGPTGAGKSTLINL---LMRfyeVDGGNILLDGKPITDYEPSQL- 413
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 ---RQEIGMVLQE-TWLKSATIHDNIAYA------NPKASRDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQC 483
Cdd:COG1136 82 rlrRRHIGFVFQFfNLLPELTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 484 QLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQTADIILVMVSGEIVE 555
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
27-315 |
1.20e-27 |
|
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: 112.65 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKS 186
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 187 YHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFinsLIYGFLAGI 266
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSL---LIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 267 ---GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18557 238 lwyGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
20-314 |
1.32e-27 |
|
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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 112.57 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVGMALLGTVVQVCLTVYlPVLIGQAVDVVLSPHSMILLlpimWKMVAVILANTIIQWINPLLYNRL---IFHYVAS 96
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVF-PLLTKYAIDHFITPGTLDGL----TGFILLYLGLILIQALSVFLFIRLagkIEMGVSY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 97 -LRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLS 175
Cdd:cd18540 76 dLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 176 LFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFI 255
Cdd:cd18540 156 AVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 256 NSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18540 236 GSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
341-553 |
1.88e-27 |
|
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: 108.64 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyEPSQLRQEIGMV 420
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQEtwlksatihdniayanpkasrdevieaakaanaDFFIKQLpNGYDtYLEdagdsLSQGQCQLLTIARIFLKLPRILI 500
Cdd:cd03230 79 PEE---------------------------------PSLYENL-TVRE-NLK-----LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 501 LDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTIQT-ADIILVMVSGEI 553
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-533 |
6.78e-27 |
|
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: 108.65 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ---LRQEI 417
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSA-TIHDNIAYA------NPKASRDEVIEAAKAANADFFIKQLPNGydtyledagdsLSQGQCQLLTIAR 490
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1091156555 491 IFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA 533
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-314 |
2.05e-26 |
|
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: 109.03 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18548 4 APLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKS 186
Cdd:cd18548 84 SFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 187 YHLYQNQtasrgrQTQfIEEM--VSQESL-----IQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLI 259
Cdd:cd18548 164 IPLFKKV------QKK-LDRLnrVVRENLtgirvIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 260 YGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18548 237 IVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKR 291
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
357-565 |
9.61e-26 |
|
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: 107.83 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYE---VDGGNILLDGKPITDYEPSQLRQ----EIGMVLQE------ 423
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 -TWlksaTIHDNIA-------YANPKASRDEVIEAAKA---ANADFFIKQLPNgydtyledagdSLSQGQCQLLTIAR-I 491
Cdd:COG0444 101 pVM----TVGDQIAeplrihgGLSKAEARERAIELLERvglPDPERRLDRYPH-----------ELSGGMRQRVMIARaL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 492 FLKlPRILILDEATSSIDtrteVLVQ----EAFQMLMKGR-TSFI-IAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:COG0444 166 ALE-PKLLIADEPTTALD----VTIQaqilNLLKDLQRELgLAILfITHDLGVVaEIADRVAVMYAGRIVEEGPVEELFE 240
|
.
gi 1091156555 565 Q 565
Cdd:COG0444 241 N 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
344-554 |
9.78e-26 |
|
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: 105.03 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdyePSQLRQEIGMVLQE 423
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 T--WLKSATIHDNIAYANPKASRDEviEAAKAANADFFIkqlpngyDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILIL 501
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDAGN--EQAETVLKDLDL-------YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 502 DEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTIQ-TADIILVMVSGEIV 554
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAkVCDRVLLLANGAIV 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
294-569 |
1.73e-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: 111.96 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 294 PFNDISSVLSEMQSALACAERLYSIL--EESSPNiTGTEKLDSSTVKGQIDFKNVIFGYNKSKP-LLNGINLHIPAGAKV 370
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLshEELEPD-SIERRTIKPGEGNSITVHNATFTWARDLPpTLNGITFSIPEGALV 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 371 AIVGPTGAGKSTLINLLMRFYEVDGGNILLDGkpitdyepsqlrqEIGMVLQETWLKSATIHDNIAYA---NPKASRdEV 447
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGkalNEKYYQ-QV 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 448 IEAAkAANADFFIkqLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAF---QMLM 524
Cdd:TIGR00957 734 LEAC-ALLPDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVL 810
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1091156555 525 KGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIY 569
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
357-564 |
2.03e-25 |
|
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: 104.83 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-RQEIGMVLQETWL-KSATIHDN 434
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IA---------YANPKASRDEVIEAAKAANA--DFFikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDE 503
Cdd:cd03219 96 VMvaaqartgsGLLLARARREEREARERAEEllERV------GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 504 ATSSIdtrTEVLVQEAFQMLMK----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:cd03219 170 PAAGL---NPEETEELAELIRElrerGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-556 |
2.28e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.56 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 335 STVKGQIDFKNVIFGY---NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdyeps 411
Cdd:COG1116 2 SAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 412 QLRQEIGMVLQET----WLksaTIHDNIAYA-----NPKASRDEVIEAAkaanadffIKQLpnGydtyLEDAGDS----L 478
Cdd:COG1116 77 GPGPDRGVVFQEPallpWL---TVLDNVALGlelrgVPKAERRERAREL--------LELV--G----LAGFEDAyphqL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 479 SQGQCQLLTIARIFLKLPRILILDEATSSID--TRtEVLVQEAFQMLMK-GRTSFIIAH------RLstiqtADIILVMV 549
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDalTR-ERLQDELLRLWQEtGKTVLFVTHdvdeavFL-----ADRVVVLS 213
|
....*....
gi 1091156555 550 S--GEIVEV 556
Cdd:COG1116 214 ArpGRIVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
341-564 |
2.63e-25 |
|
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: 104.51 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---RQEI 417
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWL-KSATIHDNIAY------ANPKAS-RDEVIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIA 489
Cdd:cd03261 80 GMLFQSGALfDSLTVFENVAFplrehtRLSEEEiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 490 R-IFLKlPRILILDEATSSID-TRTEVLV------QEAFQMlmkgrTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHS 560
Cdd:cd03261 149 RaLALD-PELLLYDEPTAGLDpIASGVIDdlirslKKELGL-----TSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPE 222
|
....
gi 1091156555 561 ELMA 564
Cdd:cd03261 223 ELRA 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
341-565 |
7.20e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.63 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPitdyePSQLRQEIGMV 420
Cdd:COG1121 7 IELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQET---WLKSATIHDNIA---YAN-------PKASRDEVIEAAKAAN-ADFFIKQLpngydtyledagDSLSQGQCQLL 486
Cdd:COG1121 81 PQRAevdWDFPITVRDVVLmgrYGRrglfrrpSRADREAVDEALERVGlEDLADRPI------------GELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 487 TIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML-MKGRTSFIIAHRLSTIQT-ADIILVMvSGEIVEVGNHSELMA 564
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPPEEVLT 227
|
.
gi 1091156555 565 Q 565
Cdd:COG1121 228 P 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
341-558 |
7.31e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.93 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV--IFGYNKSK-PLLNGINLHIPAGAKVAIVGPTGAGKSTL---INLLMRFyevDGGNILLDGKPITDYEPSQL- 413
Cdd:COG1135 2 IELENLskTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERP---TSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 --RQEIGMVLQE-TWLKSATIHDNIAY----AN-PKASR----DEVIE----AAKAanadffiKQLPngydtyledagDS 477
Cdd:COG1135 79 aaRRKIGMIFQHfNLLSSRTVAENVALpleiAGvPKAEIrkrvAELLElvglSDKA-------DAYP-----------SQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 478 LSQGQCQLLTIARiflKL---PRILILDEATSSIDTRT--EVLvqeafQMLMK-----GRTSFIIAHRLSTIQT-ADIIL 546
Cdd:COG1135 141 LSGGQKQRVGIAR---ALannPKVLLCDEATSALDPETtrSIL-----DLLKDinrelGLTIVLITHEMDVVRRiCDRVA 212
|
250
....*....|..
gi 1091156555 547 VMVSGEIVEVGN 558
Cdd:COG1135 213 VLENGRIVEQGP 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
27-315 |
8.19e-25 |
|
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: 104.49 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPL----SLFLARFI 182
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVvvlvAVLFGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 183 AKKSYHLYQNQTASRGRqtqfIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPstrFINSLIYGF 262
Cdd:cd18576 161 RKLSKKVQDELAEANTI----VEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS---FIIFLLFGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 263 LAGI---GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18576 234 IVAVlwyGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-563 |
1.61e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVI--FGynkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPS--QLRQE 416
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQETWL-KSATIHDNIAYAnP----KASRDEVIEAAKAANADFFIKQLPNGYDTyledagdSLSQGQCQLLTIARI 491
Cdd:PRK09493 79 AGMVFQQFYLfPHLTALENVMFG-PlrvrGASKEEAEKQARELLAKVGLAERAHHYPS-------ELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 492 FLKLPRILILDEATSSIDT--RTEVLvqEAFQMLM-KGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPelRHEVL--KVMQDLAeEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
341-553 |
2.24e-24 |
|
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: 101.41 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYN---KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---- 413
Cdd:cd03255 1 IELKNLSKTYGgggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQETWL-KSATIHDNIAYA-----NPKASRDEVIEAAkaanadffIKQLpnGYDTYLEDAGDSLSQGQCQLLT 487
Cdd:cd03255 81 RRHIGFVFQSFNLlPDLTALENVELPlllagVPKKERRERAEEL--------LERV--GLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQTADIILVMVSGEI 553
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-553 |
2.44e-24 |
|
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: 101.07 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVifgyNKS---KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITD--YEPSQLRQ 415
Cdd:cd03262 1 IEIKNL----HKSfgdFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 416 EIGMVLQETWL-KSATIHDNIAYAnP----KASRDEVIEAAKAanadffikqlpngydtYLEDAG---------DSLSQG 481
Cdd:cd03262 77 KVGMVFQQFNLfPHLTVLENITLA-PikvkGMSKAEAEERALE----------------LLEKVGladkadaypAQLSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 482 QCQLLTIARIFLKLPRILILDEATSSIDTRtevLVQEAFQmLMK-----GRTSFIIAHRLSTIQ-TADIILVMVSGEI 553
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
340-545 |
2.69e-24 |
|
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: 100.63 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyEPSQLRQEIGM 419
Cdd:COG4133 2 MLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSA-TIHDNIAYA----NPKASRDEVIEAAKAANadffikqlpngydtyLEDAGD----SLSQGQCQLLTIAR 490
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWaalyGLRADREAIDEALEAVG---------------LAGLADlpvrQLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 491 IFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA-HRLSTIQTADII 545
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
341-565 |
3.76e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY--NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIG 418
Cdd:PRK13650 5 IEVKNLTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffiKQLPnGYDTYLEDAGDSLSQGQCQLLTIARIFLK 494
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGleNKGIPHEEMKERVNEA------LELV-GMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 495 LPRILILDEATSSIDT--RTEVL-----VQEAFQMlmkgrTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK13650 158 RPKIIILDEATSMLDPegRLELIktikgIRDDYQM-----TVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-548 |
7.34e-24 |
|
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: 99.92 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 343 FKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPitdyePSQLRQEIGMVLQ 422
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 -------------ETWLKSATIHDNIAYANPKASRDEVIEAAKAAN-ADFFIKQLpngydtyledagDSLSQGQCQLLTI 488
Cdd:cd03235 76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGlSELADRQI------------GELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 489 ARIFLKLPRILILDEATSSIDTRTEVLVQEAF-QMLMKGRTSFIIAHRLSTIQT-ADIILVM 548
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLrELRREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
351-557 |
1.15e-23 |
|
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: 99.65 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 351 NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG---GNILLDGKPItdyEPSQLRQEIGMVLQ-ETWL 426
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCVAYVRQdDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 KSATIHDNIAYANPKASRDEVIEAAKAA-NADFFIKQLPNGY--DTYLEdagdSLSQGQCQLLTIARIFLKLPRILILDE 503
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSDAIRKKrVEDVLLRDLALTRigGNLVK----GISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 504 ATSSIDTRT-----EVLVQEAfqmlMKGRTSFIIAH--RLSTIQTADIILVMVSGEIVEVG 557
Cdd:cd03234 170 PTSGLDSFTalnlvSTLSQLA----RRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
341-557 |
1.67e-23 |
|
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: 98.01 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFG-----YNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLM--RFYEVDGGNILLDGKPItdyEPSQL 413
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQETWL-KSATIHDNIAYanpkasrdevieAAKaanadffIKqlpngydtyledagdSLSQGQCQLLTIARIF 492
Cdd:cd03213 81 RKIIGYVPQDDILhPTLTVRETLMF------------AAK-------LR---------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLST--IQTADIILVMVSGEIVEVG 557
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-561 |
2.74e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEP--SQLR 414
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 415 QEIGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffIKQLPNGYDTYLEDAGDSLSQGQCQLLTIAR 490
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 491 IFLKLPRILILDEATSSID--TRTEVL-----VQEAFQMlmkgrTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSE 561
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDpkGRDEILnkikeLHKEYNM-----TIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
48-315 |
3.69e-23 |
|
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: 100.28 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 48 AVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTT 127
Cdd:cd18564 40 GLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 128 DTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSyhlyqnQTASRgRQTQFIEEM 207
Cdd:cd18564 120 DVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRI------KEASR-EQRRREGAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 208 VS--QESL-----IQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQ 280
Cdd:cd18564 193 ASvaQESLsairvVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGD 272
|
250 260 270
....*....|....*....|....*....|....*
gi 1091156555 281 LITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18564 273 LLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
352-557 |
4.04e-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: 97.71 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVLQETWL-KSAT 430
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALyPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 431 IHDNIAYA-----NPKASRDE-VIEAAKaanadffIKQLpngyDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEA 504
Cdd:cd03301 89 VYDNIAFGlklrkVPKDEIDErVREVAE-------LLQI----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 505 TSSIDTRTEV-LVQEAFQMLMKGRTSFI-IAH-RLSTIQTADIILVMVSGEIVEVG 557
Cdd:cd03301 158 LSNLDAKLRVqMRAELKRLQQRLGTTTIyVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-562 |
4.77e-23 |
|
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: 98.08 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlRQeIGMV 420
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-RP-VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWL-KSATIHDNIAYA------NPKASRDEVIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFL 493
Cdd:cd03300 78 FQNYALfPHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSEL 562
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
341-557 |
5.58e-23 |
|
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: 97.26 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKpLLNGINLHIPAGAkVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYePSQLRQEIGMV 420
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQE-TWLKSATIHDNIAYA------NPKASRDEVIEAAKAANadffikqlpngydtyLEDAGD----SLSQGQCQLLTIA 489
Cdd:cd03264 78 PQEfGVYPNFTVREFLDYIawlkgiPSKEVKARVDEVLELVN---------------LGDRAKkkigSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 490 RIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-566 |
5.72e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPSQL---RQEI 417
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFL 493
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA-----LKAV--GMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 494 KLPRILILDEATSSIDTR-TEVLVQEAFQMLMKGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
341-565 |
6.17e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 100.26 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV--IF-GYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---R 414
Cdd:PRK11153 2 IELKNIskVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 415 QEIGMVLQE-TWLKSATIHDNIAYAnpkasrdevIEAAKAANADffIKQLPN------GydtyLEDAGDS----LSQGQC 483
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALP---------LELAGTPKAE--IKARVTellelvG----LSDKADRypaqLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 484 QLLTIARIFLKLPRILILDEATSSIDTRTevlVQEAFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVG 557
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
....*...
gi 1091156555 558 NHSELMAQ 565
Cdd:PRK11153 224 TVSEVFSH 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
341-564 |
6.92e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.63 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL--LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIG 418
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQ--ETWLKSATIHDNIAYA--NPKASRDEVI----EAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIAR 490
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIkrvdEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 491 IFLKLPRILILDEATSSIDT--RTEVL-----VQEAFQMlmkgrTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPtgRQEIMrviheIKEKYQL-----TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
.
gi 1091156555 564 A 564
Cdd:PRK13642 229 A 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-554 |
7.04e-23 |
|
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: 95.19 E-value: 7.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMVLQetwlksatihdni 435
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 ayanpkasrdevieaakaanadffikqlpngydtyledagdsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTevl 515
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE--- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091156555 516 VQEAFQMLMK----GRTSFIIAHRLSTI-QTADIILVMVSGEIV 554
Cdd:cd03216 118 VERLFKVIRRlraqGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
360-565 |
9.40e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.13 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 360 INLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVLQETWL-KSATIHDNIAYA 438
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLfPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 439 -NPK-----ASRDEVIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFL-KLPrILILDEATSSIDT- 510
Cdd:COG3840 96 lRPGlkltaEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPa 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 511 -RTEV--LVQEAFQMLmkGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG3840 164 lRQEMldLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-562 |
1.15e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMVLQET----WLksaTI 431
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELnlvpNL---SV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIAYANPKAS-----RDEVIEAAKAANADFfikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATS 506
Cdd:COG1129 97 AENIFLGREPRRgglidWRAMRRRARELLARL-------GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 507 SIDTR-TEVLvqeaFQMLM----KGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSEL 562
Cdd:COG1129 170 SLTEReVERL----FRIIRrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
357-557 |
1.16e-22 |
|
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: 97.42 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-RQEIGMVLQETWL-KSATIHDN 434
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLfPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 I--------------AYANPKASRDEVIEAAKAANA--DFFikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRI 498
Cdd:COG0411 100 VlvaaharlgrgllaALLRLPRARREEREARERAEEllERV------GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 499 LILDEATSSIdtrTEVLVQEAFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVG 557
Cdd:COG0411 174 LLLDEPAAGL---NPEETEELAELIRRlrderGITILLIEHDMDLVmGLADRIVVLDFGRVIAEG 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
341-562 |
1.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL-LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFfikqlpNGYDtYLEDAGDSLSQGQCQLLTIARIFLKL 495
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEALKQV------DMLE-RADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 496 PRILILDEATSSID--TRTEV--LVQEAFQmlMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK13648 161 PSVIILDEATSMLDpdARQNLldLVRKVKS--EHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
339-557 |
2.38e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlRQeIG 418
Cdd:COG3839 2 ASLELENVSKSYGG-VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQetwlkS-A-----TIHDNIAYA-----NPKASRDE-VIEAAKaanadffIKQLpngyDTYLEDAGDSLSQGQCQLL 486
Cdd:COG3839 79 MVFQ-----SyAlyphmTVYENIAFPlklrkVPKAEIDRrVREAAE-------LLGL----EDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 487 TIARIFLKLPRILILDEATSSID------TRTEvlVQEAFQMLmkgRTSFIIA-HRlstiQT-----ADIILVMVSGEIV 554
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAE--IKRLHRRL---GTTTIYVtHD----QVeamtlADRIAVMNDGRIQ 213
|
...
gi 1091156555 555 EVG 557
Cdd:COG3839 214 QVG 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
341-554 |
2.77e-22 |
|
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: 96.10 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPS---QLRQEI 417
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWL-KSATIHDNI-----AYANPKAS-----RDEVIEAAKAANADFfikqlpnGYDTYLEDAGDSLSQGQCQLL 486
Cdd:cd03256 81 GMIFQQFNLiERLSVLENVlsgrlGRRSTWRSlfglfPKEEKQRALAALERV-------GLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 487 TIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML--MKGRTSFIIAHRLSTIQT-ADIILVMVSGEIV 554
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-563 |
3.42e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSA-TI 431
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPfTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIA-----YANPKASRDEVIEAAKAAnADffIKQLPNGYdtYLEdagdsLSQGQCQLLTIARIFLKL------PRILI 500
Cdd:PRK13548 94 EEVVAmgrapHGLSRAEDDALVAAALAQ-VD--LAHLAGRD--YPQ-----LSGGEQQRVQLARVLAQLwepdgpPRWLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 501 LDEATSSIDTR-TEVLVQEAFQMLMKGRTSFI-IAHRLS-TIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK13548 164 LDEPTSALDLAhQHHVLRLARQLAHERGLAVIvVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-566 |
3.51e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.84 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPS---QLRQEI 417
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFFIKQLPNgydtyleDAGDSLSQGQCQLLTIARIFL 493
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-562 |
3.88e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.47 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 350 YNKSKPL--LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---RQEIGMVLQET 424
Cdd:PRK15079 28 WQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 wLKS----ATIHDNIAYA----NPKASRDEVIEAAKAANADffIKQLPNGYDTYLEDagdsLSQGQCQLLTIARIFLKLP 496
Cdd:PRK15079 108 -LASlnprMTIGEIIAEPlrtyHPKLSRQEVKDRVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 497 RILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-562 |
4.78e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 347 IFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLD------GKPITDYEPSQLRQEIGMV 420
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQE-TWLKSATIHDNIAYANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:PRK14246 96 FQQpNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-554 |
4.81e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT---DYEPSQLrqeIGMVLQETWLKSA- 429
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpEYKRAKY---IGRVFQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 --TIHDNIAYANPKASRDEVIEAAKAANADFF---IKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEA 504
Cdd:COG1101 96 smTIEENLALAYRRGKRRGLRRGLTKKRRELFrelLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 505 TSSIDTRTEVLVQEAFQMLMKGR--TSFIIAHRLS-TIQTADIILVMVSGEIV 554
Cdd:COG1101 176 TAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-557 |
7.31e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.29 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFGYNKskpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG-----GNILLDGKPI--TDYEPSQLRQEI 417
Cdd:PRK14267 11 RVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQ-ETWLKSATIHDNIA-------YANPKASRDEVIEAA--KAAnadffikqLPNGYDTYLEDAGDSLSQGQCQLLT 487
Cdd:PRK14267 88 GMVFQyPNPFPHLTIYDNVAigvklngLVKSKKELDERVEWAlkKAA--------LWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHrlSTIQTA---DIILVMVSGEIVEVG 557
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
344-564 |
8.03e-22 |
|
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: 94.66 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKSkPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-RQEIGMVLQ 422
Cdd:COG0410 7 ENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 ETWL-KSATIHDNI---AYANP-KASRDEVIEAAkaanADFF------IKQLpngydtyledAGdSLSQGQCQLLTIARI 491
Cdd:COG0410 86 GRRIfPSLTVEENLllgAYARRdRAEVRADLERV----YELFprlkerRRQR----------AG-TLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 492 FLKLPRILILDEAtssidtrTE----VLVQEAFQMLMK----GRTSFII---AHRLSTIqtADIILVMVSGEIVEVGNHS 560
Cdd:COG0410 151 LMSRPKLLLLDEP-------SLglapLIVEEIFEIIRRlnreGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAA 221
|
....
gi 1091156555 561 ELMA 564
Cdd:COG0410 222 ELLA 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
24-315 |
3.06e-21 |
|
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: 94.09 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 24 VGMALLGTVvqvcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVME 103
Cdd:cd18543 5 LLAALLATL----AGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 104 KLNLLPIAYLDKRGIGDLISRVTTDTEQLsNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIA 183
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 184 KKSY---HLYQNQTASrgrQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIY 260
Cdd:cd18543 160 RRYFpasRRAQDQAGD---LATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 261 GFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18543 237 AAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-562 |
3.32e-21 |
|
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: 92.79 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV--IFGynkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPsQLRQeIG 418
Cdd:cd03296 3 IEVRNVskRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV-QERN-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWL-KSATIHDNIAY---ANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDagdsLSQGQCQLLTIARIFLK 494
Cdd:cd03296 78 FVFQHYALfRHMTVFDNVAFglrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ----LSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 495 LPRILILDEATSSIDTRtevlVQEAFQMLMK------GRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:cd03296 154 EPKVLLLDEPFGALDAK----VRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
341-563 |
3.96e-21 |
|
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: 92.84 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRF-YEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 V---LQETWLKSATIHDNIA---------YANPKasrDEVIEAAKAANADFFIKQLpngydtyledAG---DSLSQGQCQ 484
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVLsgffdsiglYREPT---DEQRERARELLELLGLAHL----------ADrpfGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 485 LLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFI-IAHRLStiqtaDII------LVMVSGEIVEV 556
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVE-----EIPpgithvLLLKDGRVVAA 224
|
....*..
gi 1091156555 557 GNHSELM 563
Cdd:COG1119 225 GPKEEVL 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
350-562 |
5.21e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 350 YNKSKPLlNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD-----GGNILLDGKPItdYEPS----QLRQEIGMV 420
Cdd:PRK14239 15 YNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNI--YSPRtdtvDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATIHDNIAYA------NPKASRDEVIEAA-KAANADFFIKQlpngydtYLEDAGDSLSQGQCQLLTIARIFL 493
Cdd:PRK14239 92 FQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-571 |
7.05e-21 |
|
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: 92.61 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGgNILLDGKPITDYEPSQLRQEI 417
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAyANPKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQ 571
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
21-314 |
7.26e-21 |
|
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: 93.28 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWInpllynrliFHYV------ 94
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYF---------VTYWghvmga 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 95 ---ASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNgllMVF---NQFFVGLLTILVTIFSMAKIDLLMLFLV 168
Cdd:cd18549 72 rieTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE---LAHhgpEDLFISIITIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 169 LFLTPLSLFLARFIAKKsyhLYQNQTASRGRQTQF---IEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYS 245
Cdd:cd18549 149 FALLPLMIIFTIYFNKK---MKKAFRRVREKIGEInaqLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAM 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 246 STVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18549 226 AYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
252-549 |
9.17e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.03 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 252 TRFINSLIYGFLAGIGALRIMSGAFSVGQLITflnyvnqytkpfndISSVLSEMQSAL--------------ACAERLYS 317
Cdd:COG4178 272 TTGYGQLAVIFPILVAAPRYFAGEITLGGLMQ--------------AASAFGQVQGALswfvdnyqslaewrATVDRLAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 318 ---ILEESSPNITGTEKLDSSTVkGQIDFKNV-IFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTL---INLLMRF 390
Cdd:COG4178 338 feeALEAADALPEAASRIETSED-GALALEDLtLRTPD-GRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraIAGLWPY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 391 YEvdgGNILLdgkpitdyePSQLRQeigMVL-QETWLKSATIHDNIAYANP--KASRDEVIEAAKAANADFFIKQLpngy 467
Cdd:COG4178 416 GS---GRIAR---------PAGARV---LFLpQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERL---- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 468 DTyLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGrTSFI-IAHRLSTIQTADIIL 546
Cdd:COG4178 477 DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVL 554
|
...
gi 1091156555 547 VMV 549
Cdd:COG4178 555 ELT 557
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-557 |
1.03e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGM 419
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQ--ETWLKSATIHDNIAYAnPKASRDEVIEAAKaaNADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFG-PENLCLPPIEIRK--RVDRALAEI--GLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLM-KGRTSFIIAHRLSTIQTADIILVMVSGEIVEVG 557
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
341-568 |
1.12e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSK-PLLNGINLHIPAGAKVAIVGPTGAGKST---LINLLMRFYEVDGGNILLDGKPITDYEPSQLRQE 416
Cdd:PRK13640 6 VEFKHVSFTYPDSKkPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFfikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIF 492
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADV-------GMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 493 LKLPRILILDEATSSIDT--RTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEI------VEVGNHSELMA 564
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPagKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIFSKVEMLK 238
|
....
gi 1091156555 565 QKGI 568
Cdd:PRK13640 239 EIGL 242
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
109-571 |
1.94e-20 |
|
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: 96.13 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 109 PIAYLDKRGIGDLISRVTTDTEQLSNGL-LMVFNqfFVGLltILVTIFSMAKIDLLMLFLVLFLTPLSLFlarFIAKKSY 187
Cdd:TIGR01271 972 PMAVLNTMKAGRILNRFTKDMAIIDDMLpLTLFD--FIQL--TLIVLGAIFVVSVLQPYIFIAAIPVAVI---FIMLRAY 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 188 HLYQNQT----ASRGRQTQFIEEMVSQESL--IQAFSAQEessdHFRTINQEYANFSQSAIF-YSSTVNPSTRFINSLIY 260
Cdd:TIGR01271 1045 FLRTSQQlkqlESEARSPIFSHLITSLKGLwtIRAFGRQS----YFETLFHKALNLHTANWFlYLSTLRWFQMRIDIIFV 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 261 GFLAGIGALRIMS---GAFSVGQLITF-LNYVNQYTKPFNDISSVLSEMQSAlacaERLYSIL----EESSPNiTGTEKL 332
Cdd:TIGR01271 1121 FFFIAVTFIAIGTnqdGEGEVGIILTLaMNILSTLQWAVNSSIDVDGLMRSV----SRVFKFIdlpqEEPRPS-GGGGKY 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 333 DSSTV--------------KGQIDFKNVIFGYNKS-KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGgN 397
Cdd:TIGR01271 1196 QLSTVlvienphaqkcwpsGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEG-E 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 398 ILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIHDNIayaNPKA--SRDEVIEAAKAANADFFIKQLPNGYDTYLEDAG 475
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG 1351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 476 DSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVE 555
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
490
....*....|....*.
gi 1091156555 556 VGNHSELMAQKGIYYQ 571
Cdd:TIGR01271 1432 YDSIQKLLNETSLFKQ 1447
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
329-536 |
3.54e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 3.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 329 TEKLDSSTVKGQIDFKNVIFGYNKSkplLNGINLHIPAGAKVAIVGPTGAGKSTLI------NLLMRFYEVDGgNILLDG 402
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLA---VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEG-KVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 403 KPI--TDYEPSQLRQEIGMVLQETWLKSATIHDNIAYA----NPKASRDEVIEAA--KAAnadffikqLPNGYDTYLEDA 474
Cdd:PRK14243 77 KNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGarinGYKGDMDELVERSlrQAA--------LWDEVKDKLKQS 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 475 GDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRL 536
Cdd:PRK14243 149 GLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
361-566 |
3.68e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.64 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 361 NLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVLQETWLKS-ATIHDNIAYA- 438
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 439 NP-----KASRDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIFLKLPRILILDEATSSIDT--R 511
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPalR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 512 TEVLV-------QEAFQMLMkgrtsfiIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:PRK10771 166 QEMLTlvsqvcqERQLTLLM-------VSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
354-557 |
4.93e-20 |
|
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: 88.35 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRF--YEVDGGNILLDGKPITDYEPSQlRQEIGMVLqetwlksati 431
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIFL---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 hdniAYANPKAsrdevIEAAKaaNADFfikqlpngydtyLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSID-T 510
Cdd:cd03217 82 ----AFQYPPE-----IPGVK--NADF------------LRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDiD 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091156555 511 RTEVLVQEAFQMLMKGRTSFIIAH--RLSTIQTADIILVMVSGEIVEVG 557
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-562 |
5.14e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.70 E-value: 5.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlRQeIGMV 420
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQEtwlkSA-----TIHDNIAYA-----NPKASRDE-VIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIA 489
Cdd:COG3842 83 FQD----YAlfphlTVAENVAFGlrmrgVPKAEIRArVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 490 RIFLKLPRILILDEATSSIDTRT-EVLVQEAFQMLMKGRTSFIIA-HRLS---TIqtADIILVMVSGEIVEVGNHSEL 562
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLrEEMREELRRLQRELGITFIYVtHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
341-562 |
6.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffiKQLPNGYDtYLEDAGDSLSQGQCQLLTIARIFLKLP 496
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEA------LKAVRMWD-FRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 497 RILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA-HRLS-TIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
347-555 |
6.79e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 6.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 347 IFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ---LRQEIGMVLQe 423
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 twlksatihDNIAYANPKASRDEVI-----------EAAKAANADFFIKQ--LPngyDTYLEDAGDSLSQGQCQLLTIAR 490
Cdd:PRK10419 97 ---------DSISAVNPRKTVREIIreplrhllsldKAERLARASEMLRAvdLD---DSVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 491 IFLKLPRILILDEATSSIDTrteVLVQEAFQMLMKGRTSF-----IIAHRLSTIQT-ADIILVMVSGEIVE 555
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKLQQQFgtaclFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-562 |
7.28e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKSKpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD-----GGNILLDGKPITDYEPSQLR 414
Cdd:PRK14247 3 KIEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 415 QEIGMVLQ-ETWLKSATIHDNIAYAnPK-----ASRDEVIEAAKAANADffiKQLPNGYDTYLEDAGDSLSQGQCQLLTI 488
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALG-LKlnrlvKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 489 ARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAH-RLSTIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
353-563 |
2.26e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 87.86 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSA-TI 431
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFPfTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIA-----YANPKASRDEVIEAAKAAnadffikqlpngydTYLEDAGD----SLSQGQCQLLTIARIFLKL------- 495
Cdd:COG4559 93 EEVVAlgrapHGSSAAQDRQIVREALAL--------------VGLAHLAGrsyqTLSGGEQQRVQLARVLAQLwepvdgg 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 496 PRILILDEATSSIDTRTEVLV-QEAFQMLMKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVlRLARQLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-566 |
4.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.53 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT----DYEPSQ 412
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 413 LRQEIGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADF-FIKQLpngydtyLEDAGDSLSQGQCQLLT 487
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYAHRLLMDLgFSRDV-------MSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLM--KGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 1091156555 565 QK 566
Cdd:PRK13646 236 DK 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
357-553 |
4.90e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 4.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItdyepSQLRQEIGMVLQET----WLKsatIH 432
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQDArllpWKK---VI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYANPKASRDEVIEAAKAANadffikqlpngydtyLED-AGD---SLSQGQCQLLTIARIFLKLPRILILDEATSSI 508
Cdd:PRK11247 100 DNVGLGLKGQWRDAALQALAAVG---------------LADrANEwpaALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091156555 509 DTRTEVLVQEAFQMLMK--GRTSFIIAHRLS-TIQTADIILVMVSGEI 553
Cdd:PRK11247 165 DALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
341-565 |
6.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMV 420
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQ--ETWLKSATIHDNIAYANPKASRDEVIEAAKAANAdffIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRI 498
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSA---LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 499 LILDEATSSIDTRTevlVQEAFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK13652 159 LVLDEPTAGLDPQG---VKELIDFLNDlpetyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
357-561 |
6.54e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMVLQETWL-KSATIHDN 434
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLvPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IAYANPKaSRDEVIEAAKAANAdffIKQLPNGY------DTYLEDagdsLSQGQCQLLTIARIFLKLPRILILDEATSsi 508
Cdd:COG3845 101 IVLGLEP-TKGGRLDRKAARAR---IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA-- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 509 dtrteVLV-QEA---FQML--MK--GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSE 561
Cdd:COG3845 171 -----VLTpQEAdelFEILrrLAaeGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
199-577 |
7.48e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 91.19 E-value: 7.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 199 RQTQFIEEMVSQESLIQAFSAQEESSDHFRTI-NQEYANFSQSAI---FYSSTVNPSTRFINSLIYGFLAGIGALRIMSG 274
Cdd:PLN03232 477 KRVGIINEILASMDTVKCYAWEKSFESRIQGIrNEELSWFRKAQLlsaFNSFILNSIPVVVTLVSFGVFVLLGGDLTPAR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 275 AFSVGQLITFLNYvnqytkPFNDISSVLSEMQSALACAERLYSILEESSPNITGTEKLDSSTvkGQIDFKNVIFGYNK-- 352
Cdd:PLN03232 557 AFTSLSLFAVLRS------PLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGA--PAISIKNGYFSWDSkt 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMrfyevdgGNIlldgkPITDYEPSQLRQEIGMVLQETWLKSATIH 432
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL-----SHAETSSVVIRGSVAYVPQVSWIFNATVR 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYANpKASRDEVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRt 512
Cdd:PLN03232 697 ENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH- 774
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 513 evLVQEAFQMLMK----GRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELmAQKGIYYQ--MQNAQK 577
Cdd:PLN03232 775 --VAHQVFDSCMKdelkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKklMENAGK 842
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
352-557 |
7.77e-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: 84.96 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSqlRQEIGMVLQETWLKSA-T 430
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALIEAPGFYPNlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 431 IHDNIAYAN-----PKASRDEVIEAAKaanadffikqlpngydtyLEDAGD----SLSQGQCQLLTIARIFLKLPRILIL 501
Cdd:cd03268 89 ARENLRLLArllgiRKKRIDEVLDVVG------------------LKDSAKkkvkGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 502 DEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIQkVADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
345-551 |
8.08e-19 |
|
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: 85.46 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKST-LINLLMRFYEVDGG---NILLDGKPITDYEPSQLRQEIGMV 420
Cdd:cd03290 5 NGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEMQTLEGKvhwSNKNESEPSFEATRSRNRYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATIHDNIAYANP--KASRDEVIEAAkAANADffIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRI 498
Cdd:cd03290 85 AQKPWLLNATVEENITFGSPfnKQRYKAVTDAC-SLQPD--IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 499 LILDEATSSIDTR-TEVLVQEAFQMLMKG--RTSFIIAHRLSTIQTADIILVMVSG 551
Cdd:cd03290 162 VFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-564 |
8.84e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYE-VDG----GNILLDGKPITDYEPS-QLRQEIG 418
Cdd:PRK14271 26 NLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSGyrysGDVLLGGRSIFNYRDVlEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWLKSATIHDNI---AYANPKASRDEVIEAAKAANADFfikQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKL 495
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVlagVRAHKLVPRKEFRGVAQARLTEV---GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 496 PRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMA 564
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-568 |
1.31e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT------DYEP 410
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 411 sqLRQEIGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAAnadffIKQ--LPngyDTYLEDAGDSLSQGQCQ 484
Cdd:PRK13634 83 --LRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQKAREM-----IELvgLP---EELLARSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 485 LLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLM--KGRTSFIIAHRLSTI-QTADIILVMVSGEIV------E 555
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFlqgtprE 232
|
250
....*....|...
gi 1091156555 556 VGNHSELMAQKGI 568
Cdd:PRK13634 233 IFADPDELEAIGL 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
341-557 |
1.77e-18 |
|
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: 84.25 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV--IFGynkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyepsQLRQEIG 418
Cdd:cd03269 1 LEVENVtkRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWL-KSATIHDNIAYAnpkASRDEVIEAAKAANADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03269 74 YLPEERGLyPKMKVIDQLVYL---AQLKGLKKEEARRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 498 ILILDEATSSID-TRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:cd03269 149 LLILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-539 |
2.36e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.09 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG-----GNILLDGKPItdYEP----S 411
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERrvnlN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 412 QLRQEIGMVLQETWLKSATIHDNIAYA------NPKASRDEVIEAA-KAAnadffikQLPNGYDTYLEDAGDSLSQGQCQ 484
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDA-------DLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 485 LLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQ--MLMKGRTSFIIAHRLSTI 539
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
353-518 |
2.48e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSATIH 432
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYanPKASRDEVIEAAKAAnADFFIKQLPngyDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRT 512
Cdd:PRK10247 99 DNLIF--PWQIRNQQPDPAIFL-DDLERFALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
....*.
gi 1091156555 513 EVLVQE 518
Cdd:PRK10247 173 KHNVNE 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
345-557 |
2.88e-18 |
|
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: 83.70 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 345 NVIFGYNKSKPLlnGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSqlRQEIGMVLQET 424
Cdd:cd03298 4 DKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 WLKS-ATIHDNIAYA-NPK-----ASRDEVIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFLKLPR 497
Cdd:cd03298 80 NLFAhLTVEQNVGLGlSPGlkltaEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 498 ILILDEATSSIDTrteVLVQEAFQMLMK-----GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:cd03298 149 VLLLDEPFAALDP---ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
89-314 |
7.36e-18 |
|
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: 84.13 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 89 LIFHYVAS-----LRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLL 163
Cdd:cd18572 58 GCFSYAGTrlvrrLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 164 MLFLVLFLTPLSLFLARF---IAKKSYHLYQNQTAsrgRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFS-Q 239
Cdd:cd18572 138 LTLLAFITVPVIALITKVygrYYRKLSKEIQDALA---EANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSvR 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 240 SAIFYSSTvNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18572 215 QALAYAGY-VAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
341-564 |
8.27e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.26 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG-----GNILLDG-KPITDYEP--SQ 412
Cdd:PRK11264 4 IEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTaRSLSQQKGliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 413 LRQEIGMVLQETWL-KSATIHDNIaYANP----KASRDEVIEAAKAANADFFIKQLPNGYDTyledagdSLSQGQCQLLT 487
Cdd:PRK11264 83 LRQHVGFVFQNFNLfPHRTVLENI-IEGPvivkGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRtevLVQEAF----QMLMKGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPE---LVGEVLntirQLAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKAL 231
|
..
gi 1091156555 563 MA 564
Cdd:PRK11264 232 FA 233
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-315 |
9.52e-18 |
|
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: 84.07 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 24 VGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVME 103
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 104 KLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIA 183
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 184 KKSYHLYQNQTASRGRQTQFIEEM--VSQESLIQAFSAQEESSDHFRTINQEYAN----FSQSAIFYSSTVNPSTRFINS 257
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDlgvrQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 258 LIYGFlagiGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18550 241 LVYWV----GGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
341-562 |
1.26e-17 |
|
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: 82.03 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLlNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyEPSQLRQEIGMV 420
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSA-TIHDNIA-----YANPKASRDEVIEAAkaanADFFikqlpngydtYLEDAGDSL----SQGQCQLLTIAR 490
Cdd:cd03265 79 FQDLSVDDElTGWENLYiharlYGVPGAERRERIDEL----LDFV----------GLLEAADRLvktySGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 491 IFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSEL 562
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
341-560 |
1.99e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNgINLHIPAGAKVAIVGPTGAGKSTLI---NLLmrfyEV-DGGNILLDG------KPITDYEP 410
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLrvlNLL----EMpRSGTLNIAGnhfdfsKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 411 SQLRQEIGMVLQETWL-KSATIHDNIAYANPKA---SRDEVIEAAKAanadfFIKQLpngydtYLEDAGDS----LSQGQ 482
Cdd:PRK11124 78 RELRRNVGMVFQQYNLwPHLTVQQNLIEAPCRVlglSKDQALARAEK-----LLERL------RLKPYADRfplhLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 483 CQLLTIARIFLKLPRILILDEATSSID---TRTEV-LVQEAFQMlmkGRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVsIIRELAET---GITQVIVTHEVEVARkTASRVVYMENGHIVEQG 223
|
...
gi 1091156555 558 NHS 560
Cdd:PRK11124 224 DAS 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-415 |
3.78e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.46 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 12 KLVQDLL--SKKSLVGMALLGTVVQVClTVYLPVLIGQAVDVVLSPHSMILLLPIMwKMVAVILANTIIQWINpllyNRL 89
Cdd:COG4615 2 NLLRLLLreSRWLLLLALLLGLLSGLA-NAGLIALINQALNATGAALARLLLLFAG-LLVLLLLSRLASQLLL----TRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 90 IFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNqFFVGLLTILVTIFSMAKIDLLMLFLVL 169
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 170 FLTPLSLFLARFIAKKSYHLYQnqtASRGRQTQFIEEMvsqESLI-------------QAFSAQE--ESSDHFRTINqey 234
Cdd:COG4615 155 VLLGLGVAGYRLLVRRARRHLR---RAREAEDRLFKHF---RALLegfkelklnrrrrRAFFDEDlqPTAERYRDLR--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 235 anfSQSAIFYSSTVNpstrFINSLIYGFLAGIGALRIMSGAFSVGQLITF---LNYVnqyTKPFNDISSVLSEMQSALAC 311
Cdd:COG4615 226 ---IRADTIFALANN----WGNLLFFALIGLILFLLPALGWADPAVLSGFvlvLLFL---RGPLSQLVGALPTLSRANVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 312 AERLYSI---LEESSPNITGTEKLDSSTVKGQIDFKNVIFGYNKSK--------PllngINLHIPAGAKVAIVGPTGAGK 380
Cdd:COG4615 296 LRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegftlgP----IDLTIRRGELVFIVGGNGSGK 371
|
410 420 430
....*....|....*....|....*....|....*
gi 1091156555 381 STLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ 415
Cdd:COG4615 372 STLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-564 |
3.90e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.60 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 353 SKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDgkpitdyepsqlrQEIGMVLQETWLKSATIH 432
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYANPKASRDeVIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRT 512
Cdd:PTZ00243 739 GNILFFDEEDAAR-LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 513 -EVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMA 564
Cdd:PTZ00243 818 gERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
352-564 |
5.82e-17 |
|
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: 80.28 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMVLQE-TWLKSA 429
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEaSIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 TIHDNI--AYANPKASRDEVIEAAKAANADFFIKQLPNGYdtyledaGDSLSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:cd03218 91 TVEENIlaVLEIRGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 508 IDTRTEVLVQEAFQMLM-KGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMA 564
Cdd:cd03218 164 VDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
357-555 |
6.52e-17 |
|
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: 80.17 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT--DYEP-SQLR-QEIGMVLQ-ETWLKSATI 431
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFalDEDArARLRaRHVGFVFQsFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIAYANPKASRDEVIEAAKAA--------NADFFIKQlpngydtyledagdsLSQGQCQLLTIARIFLKLPRILILDE 503
Cdd:COG4181 108 LENVMLPLELAGRRDARARARALlervglghRLDHYPAQ---------------LSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 504 ATSSIDTRTEVLVQEafqmLM------KGRTSFIIAHRLSTIQTADIILVMVSGEIVE 555
Cdd:COG4181 173 PTGNLDAATGEQIID----LLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
341-557 |
7.80e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlRQeIGMV 420
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWL-KSATIHDNIAYA-----NPKAS-RDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIFL 493
Cdd:PRK09452 92 FQSYALfPHMTVFENVAFGlrmqkTPAAEiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAH-RLSTIQTADIILVMVSGEIVEVG 557
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
341-577 |
8.31e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKS--KPLLNGINLHIPAGAKVAIVGPTGAGKSTLIN-LLMRFYEVDGGNILLDGKpitdyepsqlrqeI 417
Cdd:PLN03130 615 ISIKNGYFSWDSKaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQETWLKSATIHDNIAYANP-KASRDEviEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLP 496
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 497 RILILDEATSSIDTRtevLVQEAFQMLMK----GRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQKGIYYQ- 571
Cdd:PLN03130 760 DVYIFDDPLSALDAH---VGRQVFDKCIKdelrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKl 836
|
....*.
gi 1091156555 572 MQNAQK 577
Cdd:PLN03130 837 MENAGK 842
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
361-563 |
8.34e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 361 NLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ----EIGMVLQE-TWLKSATIHDNI 435
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 AYANPKASRDEVIEAAKAANAdffIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVL 515
Cdd:PRK10070 128 AFGMELAGINAEERREKALDA---LRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 516 VQEAFQMLMKG--RTSFIIAHRL-STIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK10070 203 MQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
357-557 |
8.45e-17 |
|
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: 79.33 E-value: 8.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPiTDYEPSQLRQEIGMVLQETWL-KSATIHDNI 435
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARRRLGFVSDSTGLyDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 AY---------ANPKASRDEVIEaakaanadffikQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATS 506
Cdd:cd03266 100 EYfaglyglkgDELTARLEELAD------------RL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 507 SID-TRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:cd03266 166 GLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
341-563 |
1.27e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.74 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-------L 413
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRElakrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVLQetwlksATIHDNIAYA-------NPKASRDEVIEAAkaanADFFikQLPNGYDTYLedagDSLSQGQCQLL 486
Cdd:COG4604 81 RQENHINSR------LTVRELVAFGrfpyskgRLTAEDREIIDEA----IAYL--DLEDLADRYL----DELSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 487 TIARIFLKLPRILILDEATSSIDTRTEVlvqeafQMlMK---------GRTSFIIAHRLS-TIQTADIILVMVSGEIVEV 556
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSV------QM-MKllrrladelGKTVVIVLHDINfASCYADHIVAMKDGRVVAQ 217
|
....*..
gi 1091156555 557 GNHSELM 563
Cdd:COG4604 218 GTPEEII 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
341-565 |
1.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGY-----NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPS-QLR 414
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 415 QEIGMVLQ--ETWLKSATIHDNIAYA------NPKASRDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLL 486
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 487 TIARIFLKLPRILILDEATSSIDT--RTEVLvqEAFQMLMK--GRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPsgRREVV--NTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 1091156555 563 MAQ 565
Cdd:PRK13633 232 FKE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
355-562 |
2.36e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 355 PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ-EIGMVLQETWL-KSATIH 432
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYANPKASRDEVIEAAKaanadffIKQLPNGYDtyLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSID-TR 511
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQL-------LAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 512 TEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-555 |
3.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ---- 412
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 413 LRQEIGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAanadfFIKQLpnGYDTYLEDAGD-SLSQGQCQLLT 487
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKALK-----WLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTI-QTADIILVMVSGEIVE 555
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
354-534 |
3.54e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyePSQLRqeiGMVLQ-ETWLKSATIH 432
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAER---GVVFQnEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAY-----ANPKASRDEVIEA--AKAANADF---FIKQlpngydtyledagdsLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:PRK11248 89 DNVAFglqlaGVEKMQRLEIAHQmlKKVGLEGAekrYIWQ---------------LSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091156555 503 EATSSIDTRTEVLVQEafqMLMK-----GRTSFIIAH 534
Cdd:PRK11248 154 EPFGALDAFTREQMQT---LLLKlwqetGKQVLLITH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-562 |
3.95e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 360 INLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVLQETWL-KSATIHDNIAYA 438
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALyPHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 439 NPKASRDEvIEAAKAANADFFIKQLpngyDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQE 518
Cdd:PRK11000 100 LKLAGAKK-EEINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091156555 519 AFQMLMK--GRTSFIIAH-RLSTIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK11000 175 EISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
344-565 |
4.58e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVI--FGYNKskpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVL 421
Cdd:PRK11432 10 KNITkrFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 422 QETWL-KSATIHDNIAYA-----NPKASRDE-VIEAAKAANADFFikqlpngYDTYLedagDSLSQGQCQLLTIARIFLK 494
Cdd:PRK11432 85 QSYALfPHMSLGENVGYGlkmlgVPKEERKQrVKEALELVDLAGF-------EDRYV----DQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 495 LPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
357-565 |
5.45e-16 |
|
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: 80.88 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEvDGGNILLDGKPITDYEPSQ---LRQEIGMVLQETWlkSA---- 429
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF--GSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 -TIHDNIAYA----NPKASRDEVIEAAKAAnadffikqlpngydtyLEDAG---DSL-------SQGQCQLLTIAR-IFL 493
Cdd:COG4172 379 mTVGQIIAEGlrvhGPGLSAAERRARVAEA----------------LEEVGldpAARhryphefSGGQRQRIAIARaLIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 494 KlPRILILDEATSSID--TRTEVL-----VQEAFQMlmkgrtSFI-IAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMA 564
Cdd:COG4172 443 E-PKLLVLDEPTSALDvsVQAQILdllrdLQREHGL------AYLfISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
.
gi 1091156555 565 Q 565
Cdd:COG4172 516 A 516
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-549 |
7.36e-16 |
|
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: 75.27 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNIlldGKPitdyepsqLRQEIGMV 420
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP--------EGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATIHDNIAYAnpkasrdevieaakaanadffikqlpngydtyledAGDSLSQGQCQLLTIARIFLKLPRILI 500
Cdd:cd03223 70 PQRPYLPLGTLREQLIYP-----------------------------------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091156555 501 LDEATSSIDTRTEvlvQEAFQMLMKGRTSFI-IAHRLSTIQTADIILVMV 549
Cdd:cd03223 115 LDEATSALDEESE---DRLYQLLKELGITVIsVGHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-573 |
8.38e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 339 GQIDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLlmrfyeVDGGNILLDGKPIT-DY----- 408
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQL------TNGLIISETGQTIVgDYaipan 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 409 -----EPSQLRQEIGMVLQ--ETWLKSATIHDNIAYANPKASRDEViEAAKAANADFFIKQLPngyDTYLEDAGDSLSQG 481
Cdd:PRK13645 79 lkkikEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLP---EDYVKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 482 QCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGN 558
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
250
....*....|....*
gi 1091156555 559 HSELMAQKGIYYQMQ 573
Cdd:PRK13645 235 PFEIFSNQELLTKIE 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
338-568 |
8.62e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 338 KGQIDFKNVIFGYNKSKpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQE 416
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 417 IGMVLQETWLKS-ATIHDNIAYANPKASRDEVIEAAKAANADFfikqlPNGYDTYLEDAGdSLSQGQCQLLTIARIFLKL 495
Cdd:PRK11614 82 VAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWVYELF-----PRLHERRIQRAG-TMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 496 PRILILDEATSSIdtrTEVLVQEAF----QMLMKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMAQKGI 568
Cdd:PRK11614 156 PRLLLLDEPSLGL---APIIIQQIFdtieQLREQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
42-314 |
1.21e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 77.99 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 42 PVLIGQAVD-VVLSPHSMILLLPIMWK--------------MVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18565 19 PLLIGVAIDaVFNGEASFLPLVPASLGpadprgqlwllgglTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFfVGLLTILVTIFS-MAKIDLLMLFLVLFLTPLSLFLARFIAKK 185
Cdd:cd18565 99 RLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSI-IRVVVTVLGIGAiLFYLNWQLALVALLPVPLIIAGTYWFQRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 186 SYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAG 265
Cdd:cd18565 178 IEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFV 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 266 IGALRIMSGAF------SVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18565 258 VGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKR 312
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
113-566 |
2.48e-15 |
|
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: 79.95 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 113 LDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLArFIAKKSYHLYQN 192
Cdd:TIGR01271 173 LDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQA-CLGQKMMPYRDK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 193 QTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYAN----------FSQSAIFYSSTVnpsTRFINSLIYGF 262
Cdd:TIGR01271 252 RAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKltrkiaylryFYSSAFFFSGFF---VVFLSVVPYAL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 263 LAGIGALRIMSGA-FSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAErlYSILEEsspNITGTE-KLDSSTV--- 337
Cdd:TIGR01271 329 IKGIILRRIFTTIsYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEE--YKTLEY---NLTTTEvEMVNVTAswd 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 338 ----------------KGQIDFKNVIFGYNKS---KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:TIGR01271 404 egigelfekikqnnkaRKQPNGDDGLFFSNFSlyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 399 LLDGKpitdyepsqlrqeIGMVLQETWLKSATIHDNIAYAnpkASRDEV--IEAAKAANADFFIKQLPNGYDTYLEDAGD 476
Cdd:TIGR01271 484 KHSGR-------------ISFSPQTSWIMPGTIKDNIIFG---LSYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGI 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 477 SLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEvlvQEAFQ----MLMKGRTSFIIAHRLSTIQTADIILVMVSGE 552
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE---KEIFEsclcKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
490
....*....|....
gi 1091156555 553 IVEVGNHSELMAQK 566
Cdd:TIGR01271 625 CYFYGTFSELQAKR 638
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
372-569 |
2.80e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.20 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 372 IVGPTGAGKSTLI---NLLMR----------FY-----EVDGGNILLDGKPITDYEpsQLRQEIGMVLQ--ETWLKSATI 431
Cdd:PRK13631 57 IIGNSGSGKSTLVthfNGLIKskygtiqvgdIYigdkkNNHELITNPYSKKIKNFK--ELRRRVSMVFQfpEYQLFKDTI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIAYAnPKASRDEVIEAAKAANadFFIKQLPNGYDtYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTR 511
Cdd:PRK13631 135 EKDIMFG-PVALGVKKSEAKKLAK--FYLNKMGLDDS-YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 512 TEvlvQEAFQMLM----KGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQKGIY 569
Cdd:PRK13631 211 GE---HEMMQLILdakaNNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
370-557 |
2.92e-15 |
|
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: 75.02 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 370 VAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYE-----PSQLRQeIGMVLQETWL-KSATIHDNIAYANPKAS 443
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlPPQQRK-IGLVFQQYALfPHLNVRENLAFGLKRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 444 RDEVIEAAKAANADFFIKQLPNGYDtyledagDSLSQGQCQLLTIARIFLKLPRILILDEATSSID--TRTEVL-----V 516
Cdd:cd03297 105 NREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDraLRLQLLpelkqI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091156555 517 QEAFQMlmkgrTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:cd03297 178 KKNLNI-----PVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
27-315 |
3.48e-15 |
|
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: 76.37 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQL----SNGLLMVFNQF--FVGLLTILV------TIFSMAKIdllmlflvlfltPL 174
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIqtvvGSSLSIALRNLllLIGGLVMLFitspklTLLVLLVI------------PL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 175 SLFLARFIAKKSYHLyqnqtaSRGRQ------TQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTV 248
Cdd:cd18575 149 VVLPIILFGRRVRRL------SRASQdrladlSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 249 npsTRFINSLIYGFLAGI---GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18575 223 ---TALVIFLVFGAIVFVlwlGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-534 |
3.55e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.18 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItdyePSQL---RQEI 417
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARArlaRARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQ-ETWLKSATIHDN-IAYANPKASRDEVIEAAKAANADFfiKQLPNGYDTYLEDagdsLSQGQCQLLTIARIFLKL 495
Cdd:PRK13536 117 GVVPQfDNLDLEFTVRENlLVFGRYFGMSTREIEAVIPSLLEF--ARLESKADARVSD----LSGGMKRRLTLARALIND 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1091156555 496 PRILILDEATSSIDTRTEVLVQEAFQ-MLMKGRTSFIIAH 534
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRsLLARGKTILLTTH 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
341-557 |
3.84e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT----DYEPSQ 412
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 413 LRQEIGMVLQ--ETWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFFIKqlpngyDTYLEDAGDSLSQGQCQLLTI 488
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 489 ARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML-MKGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
21-315 |
3.88e-15 |
|
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: 76.33 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVTtDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLAr 180
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 181 FIAKKSYHLYQNQTASRG--RQTQFIEEMVSQESlIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSL 258
Cdd:cd18570 159 LLFNKPFKKKNREVMESNaeLNSYLIESLKGIET-IKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 259 IYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18570 238 GSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
355-566 |
4.57e-15 |
|
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: 75.66 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 355 PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKpitdyepsqlrqeIGMVLQETWLKSATIHDN 434
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IAYAnpkASRDE--VIEAAKAANADFFIKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRT 512
Cdd:cd03291 118 IIFG---VSYDEyrYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 513 EvlvQEAFQ----MLMKGRTSFIIAHRLSTIQTADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:cd03291 195 E---KEIFEscvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
357-565 |
5.21e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.16 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPS---QLRQEIGMVLQETW------LK 427
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQNPYgslnprKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 428 SATIHDNIAYANPKASRDEVIEAAKAANADFFIKqlPNGYDTYLEdagdSLSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMMAKVGLR--PEHYDRYPH----MFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 508 IDT--RTEVL-----VQEAFQmlmkgrTSFI-IAHRLSTIQ-TADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK11308 185 LDVsvQAQVLnlmmdLQQELG------LSYVfISHDLSVVEhIADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
344-566 |
5.49e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQE 423
Cdd:PRK11231 6 ENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 -TWLKSATIHDNIAYA-NP------KASRDEVIEAAKAANAdffikqlpNGYDTYLEDAGDSLSQGQCQLLTIARIFLKL 495
Cdd:PRK11231 85 hLTPEGITVRELVAYGrSPwlslwgRLSAEDNARVNQAMEQ--------TRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 496 PRILILDEATSSIDTRTEV-LVQEAFQMLMKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELMAQK 566
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVeLMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
354-562 |
8.00e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGMVLQETWL-KSATIH 432
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALfPHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYA--NPKASRDE----VIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIFLKLPRILILDEATS 506
Cdd:PRK11607 110 QNIAFGlkQDKLPKAEiasrVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 507 SIDTRTEVLVQ-EAFQMLMK-GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK11607 179 ALDKKLRDRMQlEVVDILERvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
355-519 |
9.66e-15 |
|
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: 73.62 E-value: 9.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 355 PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL--DGKPI--TDYEPSQL----RQEIGMVLQetWL 426
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPREIlalrRRTIGYVSQ--FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 KsatihdniayANPKAS-RDEVIEAAKAANADffikqlpngYDTYLEDAGDSLSQ-----------------GQCQLLTI 488
Cdd:COG4778 103 R----------VIPRVSaLDVVAEPLLERGVD---------REEARARARELLARlnlperlwdlppatfsgGEQQRVNI 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1091156555 489 ARIFLKLPRILILDEATSSID--TRTEV--LVQEA 519
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDaaNRAVVveLIEEA 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
354-521 |
9.69e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGmvlQETWLKSA-TIH 432
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG---HRNAMKPAlTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAY-ANPKASRDEVIEAAkaanADFF----IKQLPNGYdtyledagdsLSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:PRK13539 92 ENLEFwAAFLGGEELDIAAA----LEAVglapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....
gi 1091156555 508 IDTRTEVLVQEAFQ 521
Cdd:PRK13539 158 LDAAAVALFAELIR 171
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-565 |
1.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDY----EPSQ 412
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 413 LRQEIGMVLQ--ETWLKSATIHDNIAYAnPKASRDEVIEAAKAANADFFIKQLPNgydTYLEDAGDSLSQGQCQLLTIAR 490
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKLEMVGLAD---EFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 491 IFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
344-562 |
1.09e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 73.71 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKSkPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-RQEIGMVLQ 422
Cdd:TIGR03410 4 SNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 ETWLKSA-TIHDNI---AYANPKASRdEVIEaakaanadfFIKQL-PngydtYLED-----AGDsLSQGQCQLLTIARIF 492
Cdd:TIGR03410 83 GREIFPRlTVEENLltgLAALPRRSR-KIPD---------EIYELfP-----VLKEmlgrrGGD-LSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVLVQEAFQML--MKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
357-574 |
2.42e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.50 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLrqeigMVLQE----TWLksaTIH 432
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNysllPWL---TVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAYA-------NPKASRDEVIEAAKAanadffIKQLPNGYDTYLedagDSLSQGQCQLLTIARIFLKLPRILILDEAT 505
Cdd:TIGR01184 73 ENIALAvdrvlpdLSKSERRAIVEEHIA------LVGLTEAADKRP----GQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 506 SSIDTRTEVLVQEAfqmLMK-----GRTSFIIAHRL-STIQTADIILVMVS------GEIVEVG----NHSELMAQKGIY 569
Cdd:TIGR01184 143 GALDALTRGNLQEE---LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEVPfprpRDRLEVVEDPSY 219
|
....*
gi 1091156555 570 YQMQN 574
Cdd:TIGR01184 220 YDLRN 224
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
21-315 |
2.54e-14 |
|
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: 73.75 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVT-TDTEQ--LSNGLLmvfnQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLF 177
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQeNQKIRrfLTRSAL----TTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 178 LARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHF-----RTINQEYanfsqSAIFYSSTVNPST 252
Cdd:cd18568 157 LTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWenkfaKALNTRF-----RGQKLSIVLQLIS 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 253 RFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18568 232 SLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
20-315 |
2.58e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents 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: 349999 [Multi-domain] Cd Length: 294 Bit Score: 73.70 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVGMALLGTVVQVcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRK 99
Cdd:cd18555 1 KKLLISILLLSLLLQL-LTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 100 AVMEKLNLLPIAYLDKRGIGDLISRVTTDT---EQLSNGLLMVFnqffVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSL 176
Cdd:cd18555 80 DFFEHLLKLPYSFFENRSSGDLLFRANSNVyirQILSNQVISLI----IDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 177 FLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFIN 256
Cdd:cd18555 156 LLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 257 SLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18555 236 FIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
340-562 |
2.79e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 74.49 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlrQEIGM 419
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWL-KSATIHDNIAYA-----NPKASRDE-VIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIF 492
Cdd:PRK11650 81 VFQNYALyPHMSVRENMAYGlkirgMPKAEIEErVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVlvqeafQM---LMK-----GRTSFIIAH-RLSTIQTADIILVMVSGEIVEVGNHSEL 562
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRV------QMrleIQRlhrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
356-563 |
2.94e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITD-----------YEPSQLRQEIGMVLQE- 423
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafarkvaYLPQQLPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 ------TWlksatiHDNIAYANpKASRDEVIEAAKAANADFFIKQLPngydtyledagDSLSQGQCQLLTIARIFLKLPR 497
Cdd:PRK10575 106 vaigryPW------HGALGRFG-AADREKVEEAISLVGLKPLAHRLV-----------DSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIAhRLSTIQTA----DIILVMVSGEIVEVGNHSELM 563
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-563 |
3.36e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 344 KNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQE 423
Cdd:PRK10253 11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 -TWLKSATIHDNIAYA----NP------KASRDEVIEAAKAANADFFIKQlpngydtyledAGDSLSQGQCQLLTIARIF 492
Cdd:PRK10253 90 aTTPGDITVQELVARGryphQPlftrwrKEDEEAVTKAMQATGITHLADQ-----------SVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 493 LKLPRILILDEATSSIDTRTEVLVQEAFQML--MKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
351-562 |
3.88e-14 |
|
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: 71.77 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 351 NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdYEPSQLRQEIGMVLQE-TWLKSA 429
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFdALFDEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 TIHDNIA-YANPKASRDEVIEaakaANADFFIKQLPngydtyLEDAGDS----LSQGQCQLLTIARIFLKLPRILILDEA 504
Cdd:cd03263 91 TVREHLRfYARLKGLPKSEIK----EEVELLLRVLG------LTDKANKrartLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 505 TSSIDTRTEVLVQEAFQMLMKGRTSFIIAHrlsTIQTADI----ILVMVSGEIVEVGNHSEL 562
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-557 |
4.12e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKskpLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItdyepSQL----RQ 415
Cdd:PRK10851 4 EIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLhardRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 416 eIGMVLQETWL-KSATIHDNIAYAN---PKASRDEVIEAAKAANADFFIKQLPNGYDTYledaGDSLSQGQCQLLTIARI 491
Cdd:PRK10851 76 -VGFVFQHYALfRHMTVFDNIAFGLtvlPRRERPNAAAIKAKVTQLLEMVQLAHLADRY----PAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 492 FLKLPRILILDEATSSIDT--RTEV---LVQ--EAFQMlmkgrTSFIIAH-RLSTIQTADIILVMVSGEIVEVG 557
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAqvRKELrrwLRQlhEELKF-----TSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
357-565 |
8.29e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.06 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDyepsQLRQEIGMVLQETWL-KSATIHDNI 435
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYLPEERGLyPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 436 AY------ANPKASRdevieaakaANADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSID 509
Cdd:COG4152 93 VYlarlkgLSKAEAK---------RRADEWLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 510 -TRTEVLVQEAFQMLMKGRTsfII--AHRLSTIQT-ADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG4152 162 pVNVELLKDVIRELAAKGTT--VIfsSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
354-565 |
8.73e-14 |
|
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: 73.95 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKS----TLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ----EIGMVLQE-- 423
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 TWLKSA-TIHDNIAYA-------NPKASRDEVIEAAKA---ANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIF 492
Cdd:COG4172 103 TSLNPLhTIGKQIAEVlrlhrglSGAAARARALELLERvgiPDPERRLDAYPH-----------QLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 493 LKLPRILILDEATSSID--TRTEVL-----VQEAFQMLMkgrtsFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:COG4172 172 ANEPDLLIADEPTTALDvtVQAQILdllkdLQRELGMAL-----LLITHDLGVVrRFADRVAVMRQGEIVEQGPTAELFA 246
|
.
gi 1091156555 565 Q 565
Cdd:COG4172 247 A 247
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
340-555 |
1.26e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGM 419
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 VLQETWLKSATIhdniayaNPKAsrdeviEAAKAANADFFIKQLPNGYDTYLED---AGDSLSQGQCQLLTIARIFLKLP 496
Cdd:PRK10522 402 VFTDFHLFDQLL-------GPEG------KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 497 RILILDEATSSIDTrteVLVQEAFQMLM-----KGRTSFIIAHRLSTIQTADIILVMVSGEIVE 555
Cdd:PRK10522 469 DILLLDEWAADQDP---HFRREFYQVLLpllqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
357-557 |
1.52e-13 |
|
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: 70.25 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItdyepSQLrqEIGMVLQEtwlkSATIHDNIA 436
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLL--GLGGGFNP----ELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 437 -----YANPKASRDEVIEaakaanadfFIKQLpngydTYLEDAGDS----LSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:cd03220 107 lngrlLGLSRKEIDEKID---------EIIEF-----SELGDFIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 508 IDTRTEVLVQEAFQ-MLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVG 557
Cdd:cd03220 173 GDAAFQEKCQRRLReLLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-551 |
1.59e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 358 NGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYePSQLRQEIGMV--LQETWL-KSATIHDN 434
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVrtFQHVRLfREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IAYANPKASRDEVI------------EAAKAANADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:PRK11300 101 LLVAQHQQLKTGLFsgllktpafrraESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 503 EATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQ-TADIILVMVSG 551
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMgISDRIYVVNQG 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
341-557 |
1.68e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKN--VIFGynkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIG 418
Cdd:PRK09536 4 IDVSDlsVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 419 MVLQETWLK-----------SATIHDNIAYANPKASRDEVIEAAKAANADFFIKQlpngydtyledAGDSLSQGQCQLLT 487
Cdd:PRK09536 81 SVPQDTSLSfefdvrqvvemGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADR-----------PVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRLS-TIQTADIILVMVSGEIVEVG 557
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
340-558 |
2.17e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGYNKSKPL----LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI---LLDGKPITDYEP-- 410
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 411 -------------------SQLRQEIGMVLQ--ETWLKSATIHDNIA-----YANPKAsrdeviEAAKAANADFFIKQLP 464
Cdd:PRK13651 82 kvleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIfgpvsMGVSKE------EAKKRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 465 ngyDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK-GRTSFIIAHRL-STIQTA 542
Cdd:PRK13651 156 ---ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWT 232
|
250
....*....|....*.
gi 1091156555 543 DIILVMVSGEIVEVGN 558
Cdd:PRK13651 233 KRTIFFKDGKIIKDGD 248
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
41-315 |
3.25e-13 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 70.19 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 41 LPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGD 120
Cdd:cd18589 15 IPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 121 LISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSYHLYQNQTASRGRQ 200
Cdd:cd18589 95 IVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 201 TQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQ-SAIFYssTVNPSTRFINSLIY--GFLAgIGALRIMSGAFS 277
Cdd:cd18589 175 NQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKkEAAAY--AVSMWTSSFSGLALkvGILY-YGGQLVTAGTVS 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 1091156555 278 VGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18589 252 SGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-520 |
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 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSqLRQEIGMVLQETWLKSA-TIHDN 434
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IAYANPKASRDEVIEAAKAANAdffikqlpNGYdtylED-AGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTE 513
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGL--------NGF----EDrPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*..
gi 1091156555 514 VLVQEAF 520
Cdd:cd03231 162 ARFAEAM 168
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
27-315 |
3.86e-13 |
|
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: 70.24 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVIL---------ANTIIQWINPLLYNRLifhyVASL 97
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALlgvfvvgaaANFGRVYLLRIAGERI----VARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 98 RKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTP---- 173
Cdd:cd18573 77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPpiav 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 174 LSLFLARFIAKKSyHLYQNQTASrgrQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQ-----SAIFYSSTv 248
Cdd:cd18573 157 GAVFYGRYVRKLS-KQVQDALAD---ATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKkealaSGLFFGST- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 249 npsTRFINSLIYGFLAgIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18573 232 ---GFSGNLSLLSVLY-YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
20-315 |
4.01e-13 |
|
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: 70.31 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVGMALLGTVVQVcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRK 99
Cdd:cd18782 1 RRALIEVLALSFVVQL-LGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 100 AVMEKLNLLPIAYLDKRGIGDLISRVTtDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLA 179
Cdd:cd18782 80 TIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 180 RFIAKKSYHLYQNQTASRGR-QTQFIEEMvsqeSLIQAFSAQEESSDHFRTINQEYANFSQS---AIFYSSTVNPSTRFI 255
Cdd:cd18782 159 FLFGPILRRQIRRRAEASAKtQSYLVESL----TGIQTVKAQNAELKARWRWQNRYARSLGEgfkLTVLGTTSGSLSQFL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 256 NSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18782 235 NKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-517 |
1.00e-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: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLdGKPItdyEPSQLRQEigmv 420
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---KIGYFDQH---- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 lQETWLKSATIHDNIAYANPKASRDEVIeaakaanadffikqlpngydTYLED---AGD-------SLSQGQ---CQLlt 487
Cdd:COG0488 387 -QEELDPDKTVLDELRDGAPGGTEQEVR--------------------GYLGRflfSGDdafkpvgVLSGGEkarLAL-- 443
|
170 180 190
....*....|....*....|....*....|..
gi 1091156555 488 iARIFLKLPRILILDEATS--SIDTRtEVLVQ 517
Cdd:COG0488 444 -AKLLLSPPNVLLLDEPTNhlDIETL-EALEE 473
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
357-563 |
1.73e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLL--MRFYEvdgGNILLDGKPITDYEPSQLRQEIGMVLQETWLKSA-TIHD 433
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMagLLPGQ---GEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAmPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 434 NIAYANPKASRDEVIEAAKAANADFFikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKL-------PRILILDEATS 506
Cdd:COG4138 89 YLALHQPAGASSEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQVwptinpeGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 507 SIDTRTEVLVQeafQMLMK----GRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:COG4138 163 SLDVAQQAALD---RLLRElcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
352-558 |
2.01e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRF--YEVDGGNILLDGKPITDYEPSQlRQEIGMVLqetwlksa 429
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHLGIFL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 tihdniAYANPkasrdevIEAAKAANADF------------------------FIKQ---LPNGYDTYLE-DAGDSLSQG 481
Cdd:CHL00131 89 ------AFQYP-------IEIPGVSNADFlrlaynskrkfqglpeldplefleIINEklkLVGMDPSFLSrNVNEGFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 482 QCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFI-IAH--RLSTIQTADIILVMVSGEIVEVGN 558
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
341-534 |
2.84e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPsQLRQEIGMV 420
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLK-SATIHDNI---------AYANPKASRDEVIEAAKaanadffikqlpngydtyLEDAGDS----LSQGQCQLL 486
Cdd:PRK13537 86 PQFDNLDpDFTVRENLlvfgryfglSAAAARALVPPLLEFAK------------------LENKADAkvgeLSGGMKRRL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091156555 487 TIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLM-KGRTSFIIAH 534
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTH 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-552 |
3.11e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 349 GYNKSKP---LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQlRQE--IGMVLQE 423
Cdd:PRK10762 9 GIDKAFPgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS-SQEagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 -TWLKSATIHDNIAYANPKASRDEVIEAAKA-ANADFFIKQLPNGYDTYlEDAGDsLSQGQCQLLTIARIFLKLPRILIL 501
Cdd:PRK10762 88 lNLIPQLTIAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSD-KLVGE-LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 502 DEATSSI-DTRTEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGE 552
Cdd:PRK10762 166 DEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
354-505 |
3.26e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLdgkpitdyePSQLRqeIGMVLQETWL-KSATIH 432
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQEPPLdDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNI----------------AYANPKASRDEVIEAAK-----------AANADffIKQLPNG---YDTYLEDAGDSLSQGQ 482
Cdd:COG0488 80 DTVldgdaelraleaeleeLEAKLAEPDEDLERLAElqeefealggwEAEAR--AEEILSGlgfPEEDLDRPVSELSGGW 157
|
170 180
....*....|....*....|...
gi 1091156555 483 CQLLTIARIFLKLPRILILDEAT 505
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPT 180
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-568 |
3.80e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.95 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 348 FGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPS---QLRQEIGMVLQ-- 422
Cdd:PRK13638 9 FRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVFQdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 ETWLKSATIHDNIAYA--NPKASRDEVI----EAAKAANADFFiKQLPNgydtyledagDSLSQGQCQLLTIARIFLKLP 496
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-RHQPI----------QCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 497 RILILDEATSSIDTRTEV-LVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIV------EVGNHSELMAQKGI 568
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTqMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILthgapgEVFACTEAMEQAGL 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
354-562 |
4.51e-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: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMrFYEVDG----GNILLDGKPItdyEPSQLRQEIGMVLQ-ETWLKS 428
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI---DAKEMRAISAYVQQdDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATI------------HDNIAYANPKASRDEVIEA---AKAANadffikqlpngydTYLEDAGD--SLSQGQCQLLTIARI 491
Cdd:TIGR00955 114 LTVrehlmfqahlrmPRRVTKKEKRERVDEVLQAlglRKCAN-------------TRIGVPGRvkGLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 492 FLKLPRILILDEATSSID-TRTEVLVQEAFQMLMKGRTSFIIAHRLST--IQTADIILVMVSGEIVEVGNHSEL 562
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
349-554 |
4.97e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 349 GYNKSKP---LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPSQ--LRQEIGMVLQE 423
Cdd:PRK10982 3 NISKSFPgvkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKeaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 TWL-KSATIHDNIAYAN-PK----ASRDEVIEAAKAANADFFIKQLPNgydtyleDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:PRK10982 82 LNLvLQRSVMDNMWLGRyPTkgmfVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 498 ILILDEATSSIdtrTEVLVQEAFQMLMK----GRTSFIIAHRLSTI-QTADIILVMVSGEIV 554
Cdd:PRK10982 155 IVIMDEPTSSL---TEKEVNHLFTIIRKlkerGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
27-294 |
1.27e-11 |
|
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: 65.90 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMIL------LLPIMWKMVAVIL---------ANTIIQWI-NPLLYNrli 90
Cdd:cd18554 4 TIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLdekvykLFTIIGIMFFIFLilrppveyyRQYFAQWIaNKILYD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 91 fhyvasLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLF 170
Cdd:cd18554 81 ------IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 171 LTPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEY---ANFSQSAIFYS-S 246
Cdd:cd18554 155 IFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFltrALKHTRWNAKTfS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1091156555 247 TVNPSTRFINSLIygflAGIGALRIMSGAFSVGQLITFLNYVNQYTKP 294
Cdd:cd18554 235 AVNTITDLAPLLV----IGFAAYLVIEGNLTVGTLVAFVGYMERMYSP 278
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
341-509 |
1.45e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ---LRQEI 417
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 418 GMVLQE-TWLKSATIHDNIAYA--NPKASRDEVIEAAKAANADFFIKQLPNGYDTyledagdSLSQGQCQLLTIARIFLK 494
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIPliIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170
....*....|....*
gi 1091156555 495 LPRILILDEATSSID 509
Cdd:PRK10908 155 KPAVLLADEPTGNLD 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
352-564 |
1.97e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG--GNILLDGKPITdyepSQLRQEIGMVLQETWL-KS 428
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILyPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHDNIAYAN----PKA-SRDEVIEAAKAANADFFIKQLPNGY--DTYLEdagdSLSQGQCQLLTIARIFLKLPRILIL 501
Cdd:PLN03211 155 LTVRETLVFCSllrlPKSlTKQEKILVAESVISELGLTKCENTIigNSFIR----GISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 502 DEATSSID-TRTEVLVQEAFQMLMKGRTSFIIAHRLST--IQTADIILVMVSGEIVEVGNHSELMA 564
Cdd:PLN03211 231 DEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
357-554 |
2.34e-11 |
|
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: 66.39 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDG--GNILLDGKP-----ITDYEpsqlRQEIGMVLQE-TWLKS 428
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlkasnIRDTE----RAGIVIIHQElTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHDNIAYAN------PKASRDEVIEAAKAANADFFIKQLPNGydtylEDAGDsLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:TIGR02633 93 LSVAENIFLGNeitlpgGRMAYNAMYLRAKNLLRELQLDADNVT-----RPVGD-YGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1091156555 503 EATSSI-DTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQT-ADIILVMVSGEIV 554
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
341-403 |
2.71e-11 |
|
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: 61.70 E-value: 2.71e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 341 IDFKNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGK 403
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
341-551 |
3.43e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.65 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNV---IFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYE--VDGGNILLDGKPITDYepsqLRQ 415
Cdd:cd03232 4 LTWKNLnytVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN----FQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 416 EIGMVLQEtwlksaTIHdniayaNPKASrdeVIEAAKaanadffikqlpngYDTYLEDagdsLSQGQCQLLTIARIFLKL 495
Cdd:cd03232 80 STGYVEQQ------DVH------SPNLT---VREALR--------------FSALLRG----LSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 496 PRILILDEATSSIDTRTEVLVQEAFQML-MKGRTSFIIAHRLS--TIQTADIILVMVSG 551
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
370-564 |
7.09e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 370 VAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLQetwlksatihDNIAYANPKASRDEVIE 449
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQ----------DPSTSLNPRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 450 AAKAANADFFIKQLPNGYDTYLEDAG----------DSLSQGQCQLLTIARIFLKLPRILILDEATSSID--TRTEvLVQ 517
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIETLRQVGllpdhasyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDmsMRSQ-LIN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1091156555 518 EAFQMLMKGRTSFI-IAHRLSTIQ-TADIILVMVSGEIVEVGNHSELMA 564
Cdd:PRK15112 191 LMLELQEKQGISYIyVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLA 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-564 |
8.20e-11 |
|
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: 64.44 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLL--MRFYEVDGGNIL----------------LDG 402
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 403 KP-----------------ITDYEPSQLRQEIGMVLQETW--LKSATIHDNIAYANPKASRDEVIEAAKAANadfFIKQL 463
Cdd:TIGR03269 80 EPcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFalYGDDTVLDNVLEALEEIGYEGKEAVGRAVD---LIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 464 PNGYD-TYLedAGDsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMK--GRTSFIIAHRLSTIQ 540
Cdd:TIGR03269 157 QLSHRiTHI--ARD-LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 1091156555 541 -TADIILVMVSGEIVEVGNHSELMA 564
Cdd:TIGR03269 234 dLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
357-558 |
9.18e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.41 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGK---PItdyepsqlrqEIGMVLQEtwlkSATIHD 433
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLL----------ELGAGFHP----ELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 434 NIaYAN----------PKASRDEVIEAAKaanadffikqlpngydtyLEDAGD----SLSQGQcqlltIAR------IFL 493
Cdd:COG1134 108 NI-YLNgrllglsrkeIDEKFDEIVEFAE------------------LGDFIDqpvkTYSSGM-----RARlafavaTAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 494 KlPRILILDEATSSIDtrtevlvqEAFQ---------MLMKGRTSFIIAHRLSTIQT-ADIILVMVSGEIVEVGN 558
Cdd:COG1134 164 D-PDILLVDEVLAVGD--------AAFQkkclarireLRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
357-552 |
9.72e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD--GGNILLDGKP-----ITDYEpsqlRQEIGMVLQE-TWLKS 428
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEElqasnIRDTE----RAGIAIIHQElALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHDNIAYANpKASRDEVIE-AAKAANADFFIKQLPNGYDTYLEdAGDsLSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:PRK13549 97 LSVLENIFLGN-EITPGGIMDyDAMYLRAQKLLAQLKLDINPATP-VGN-LGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091156555 508 I-DTRTEVLVQEAFQMLMKGRTSFIIAHRLSTIQT-ADIILVMVSGE 552
Cdd:PRK13549 174 LtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
354-560 |
1.43e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLM--RFYEVDGGNILLDGKPITDYEPS-----------QLRQEIGMV 420
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEdragegifmafQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLKSATihdniayaNPKASRDEVIEAAKAANADFF---IKQLPNGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPR 497
Cdd:PRK09580 94 SNQFFLQTAL--------NAVRSYRGQEPLDRFDFQDLMeekIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 498 ILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFIIA---HRLSTIQTADIILVMVSGEIVEVGNHS 560
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
357-555 |
3.05e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRF-----YEvdgGNILLDGKP-----ITDYEpsqlrqEIGMVL--QET 424
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsYE---GEILFDGEVcrfkdIRDSE------ALGIVIihQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 WLKSA-TIHDNIAYANPKASR-----DEVIEAAKAANADFFIKQLPngyDTYLEDAGdslsQGQCQLLTIARIFLKLPRI 498
Cdd:NF040905 88 ALIPYlSIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESP---DTLVTDIG----VGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 499 LILDEATSSI-DTRTEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVE 555
Cdd:NF040905 161 LILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
357-565 |
3.34e-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: 62.51 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL----DGKPITDYEP---SQLRQEIGMVLQETWL-KS 428
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPdgrGRAKRYIGILHQEYDLyPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHDN----IAYANPK--ASRDEVIEAAKAANADFFIKQLPNGYDtyledagDSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:TIGR03269 380 RTVLDNlteaIGLELPDelARMKAVITLKMVGFDEEKAEEILDKYP-------DELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 503 EATSSIDTRTEVLVQEAfqmLMKGR-----TSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHS---ILKAReemeqTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
357-565 |
6.58e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 60.69 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKS----TLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ----EIGMVLQE--TWL 426
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEpsSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 K-SATIHDNIAYANP------------KASRDEVIEAAKAANadffIKQlpngYDTYLEDAGDSLSQGQCQLLTIARIFL 493
Cdd:COG4170 103 DpSAKIGDQLIEAIPswtfkgkwwqrfKWRKKRAIELLHRVG----IKD----HKDIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 494 KLPRILILDEATSSIDTRTEVLVqeaFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQI---FRLLARlnqlqGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
357-554 |
7.03e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL----RQEIGMVLQETWLKS-ATI 431
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLShLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNI----AYANpkASRDEVIEAAKAanadfFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSS 507
Cdd:PRK10535 104 AQNVevpaVYAG--LERKQRLLRAQE-----LLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091156555 508 IDTRTEVLVQEAF-QMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIV 554
Cdd:PRK10535 175 LDSHSGEEVMAILhQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
356-565 |
8.39e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTL---INLLMRFYE----VDGGNILL----DGK-PITDYEPSQ-LRQEIGMVLQ 422
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLEKPSEgsivVNGQTINLvrdkDGQlKVADKNQLRlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 ETWLKS-ATIHDNIAYANPkasrdEVIEAAKAANADFFIKQLPN-GYDTYLEDAGDS-LSQGQCQLLTIARIFLKLPRIL 499
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPI-----QVLGLSKQEARERAVKYLAKvGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 500 ILDEATSSIDTRtevLVQEAFQMLMK----GRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK10619 175 LFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
270-548 |
1.09e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 270 RIMSGAFSVGQLITFLNYVNQytkpfndISSVLSEMQSALACAERLYSILEESSPNITGTEKLDSSTVKGQ---IDFKNV 346
Cdd:TIGR00954 385 RLMLAGRDMTRLAGFTARVDT-------LLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQdngIKFENI 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 347 IFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGnilldgkpiTDYEPSqlRQEIGMVLQETWL 426
Cdd:TIGR00954 458 PLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---------RLTKPA--KGKLFYVPQRPYM 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 KSATIHDNIAYANP------KASRDEVIEAAKAANADFFIKQLPNGYDTyLEDAGDSLSQGQCQLLTIARIFLKLPRILI 500
Cdd:TIGR00954 527 TLGTLRDQIIYPDSsedmkrRGLSDKDLEQILDNVQLTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1091156555 501 LDEATSSIDTRTEvlvQEAFQMLMKGRTSFI-IAHRLSTIQTADIILVM 548
Cdd:TIGR00954 606 LDECTSAVSVDVE---GYMYRLCREFGITLFsVSHRKSLWKYHEYLLYM 651
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
354-535 |
1.18e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRfyevdggniLLDGKPITDyepsqlrqeIGMVLQETWLKSATIHD 433
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------ALKGTPVAG---------CVDVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 434 NIAYANPKASRDEVIEAAKAANADFFIKQLPNgydtyledagdsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTE 513
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....
gi 1091156555 514 VLVQEAFQMLM-KGRTSFIIA-HR 535
Cdd:COG2401 173 KRVARNLQKLArRAGITLVVAtHH 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
357-557 |
1.25e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGnILLDGKPITDYEPSQL---RQEIGMVLQetwlksatihD 433
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGE-IWFDGQPLHNLNRRQLlpvRHRIQVVFQ----------D 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 434 NIAYANPKASRDEVI-EAAKAANADFFIKQLPNGYDTYLEDAG----------DSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:PRK15134 371 PNSSLNPRLNVLQIIeEGLRVHQPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 503 EATSSIDtRTevlVQEAFQMLMKG-----RTSFI-IAHRLSTIQT-ADIILVMVSGEIVEVG 557
Cdd:PRK15134 451 EPTSSLD-KT---VQAQILALLKSlqqkhQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
20-292 |
1.27e-09 |
|
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: 59.40 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 20 KKSLVGMALLGTVVQVcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQ----WINPLLYNRLIFHYVA 95
Cdd:cd18567 1 KRALLQILLLSLALEL-FALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSalrsWLVLYLSTSLNLQWTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 96 SLrkavMEKLNLLPIAYLDKRGIGDLISR----------VTTD-TEQLSNGLL------MVFnqFFVGLLTILVTIFSMA 158
Cdd:cd18567 80 NL----FRHLLRLPLSYFEKRHLGDIVSRfgsldeiqqtLTTGfVEALLDGLMailtlvMMF--LYSPKLALIVLAAVAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 159 kidllmlflvlfltplsLFLARFIAKKSYHLYQNQ--TASRGRQTQFIEEMVSQESlIQAFSAQEESSDHFRTINQEYAN 236
Cdd:cd18567 154 -----------------YALLRLALYPPLRRATEEqiVASAKEQSHFLETIRGIQT-IKLFGREAEREARWLNLLVDAIN 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 237 fsqsAIFYSSTVNPSTRFINSLIYGFLA----GIGALRIMSGAFSVGQLITFLNYVNQYT 292
Cdd:cd18567 216 ----ADIRLQRLQILFSAANGLLFGLENilviYLGALLVLDGEFTVGMLFAFLAYKDQFS 271
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
341-543 |
3.36e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYnKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPSQLRQEIGMV 420
Cdd:PRK13540 2 LDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 421 LQETWLK-SATIHDNIAYanpkasrdEVIEAAKAANADFFIKQLPNGYdtYLEDAGDSLSQGQCQLLTIARIFLKLPRIL 499
Cdd:PRK13540 80 GHRSGINpYLTLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1091156555 500 ILDEATSSIDTRT-EVLVQEAFQMLMKGRTSFIIAHRLSTIQTAD 543
Cdd:PRK13540 150 LLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
49-315 |
3.99e-09 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 57.87 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 49 VDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLISRVTTd 128
Cdd:cd18569 29 IDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 129 TEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIeemV 208
Cdd:cd18569 108 NDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTT---M 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 209 SQESLIQAFSAQEESSDHFRTINQEYA---NFSQSAIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFL 285
Cdd:cd18569 185 SGLQMIETLKASGAESDFFSRWAGYQAkvlNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQ 264
|
250 260 270
....*....|....*....|....*....|
gi 1091156555 286 NYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18569 265 SLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-544 |
4.89e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL-------DGKPITDyepsqL 413
Cdd:PRK10938 261 IVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTlfgrrrgSGETIWD-----I 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 414 RQEIGMVlqetwlkSATIHdnIAYANPKASRDEVIEAakaanadFF------------IKQLPN------GYDTYLEDAG 475
Cdd:PRK10938 335 KKHIGYV-------SSSLH--LDYRVSTSVRNVILSG-------FFdsigiyqavsdrQQKLAQqwldilGIDKRTADAP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 476 -DSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEaF--QMLMKGRTSFI------------IAHRLSTIQ 540
Cdd:PRK10938 399 fHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRR-FvdVLISEGETQLLfvshhaedapacITHRLEFVP 477
|
....
gi 1091156555 541 TADI 544
Cdd:PRK10938 478 DGDI 481
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-565 |
6.14e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFY-----EVDGGNILLDGKPITDYEPSQLRQ----EIGMVLQET 424
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 WLKSATIHdNIAYA-----------NPKASRDEVIEAAKAANadffIKQLPNgydtYLEDAGDSLSQGQCQLLTIARIFL 493
Cdd:PRK15134 102 MVSLNPLH-TLEKQlyevlslhrgmRREAARGEILNCLDRVG----IRQAAK----RLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 494 KLPRILILDEATSSIDtrteVLVQEAFQMLMK------GRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMAQ 565
Cdd:PRK15134 173 TRPELLIADEPTTALD----VSVQAQILQLLRelqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
352-568 |
8.34e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYE-PSQLRQEIGMVLQE-TWLKSA 429
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEaSIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 TIHDNIAYAnpKASRDEVIEAAKAANADFFIKQLpngYDTYLEDA-GDSLSQGQCQLLTIARIFLKLPRILILDEATSSI 508
Cdd:PRK10895 94 SVYDNLMAV--LQIRDDLSAEQREDRANELMEEF---HIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 509 DTRTEVLVQEAFQMLM-KGRTSFIIAHRL-STIQTADIILVMVSGEIVEVGNHSELMAQKGI 568
Cdd:PRK10895 169 DPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
356-512 |
9.93e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPIT---DYEPSQLR-QEIGMVLQETWL-KSAT 430
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRaKHVGFVFQSFMLiPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 431 IHDNIAYanPKASRDEViEAAKAANADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDT 510
Cdd:PRK10584 105 ALENVEL--PALLRGES-SRQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
..
gi 1091156555 511 RT 512
Cdd:PRK10584 180 QT 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
357-539 |
1.04e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPitdyepsqlrqeigMVLQETwlkSATIHDNIA 436
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------------MRFAST---TAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 437 yanpkasrdeVI--------EAAKAANadFFIKQLPNGYD------------TYLEDAGD---------SLSQGQCQLLT 487
Cdd:PRK11288 83 ----------IIyqelhlvpEMTVAEN--LYLGQLPHKGGivnrrllnyearEQLEHLGVdidpdtplkYLSIGQRQMVE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 488 IARIFLKLPRILILDEATSSIDTR-TEVLVQEAFQMLMKGRTSFIIAHRLSTI 539
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-537 |
1.36e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPS---QLR-QEIGMVLQ-ETWLKSAT 430
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 431 IHDNIAY------ANPKASRDEVIEAAKAANADFFIKQLPNgydtyledagdSLSQGQCQLLTIARIFLKLPRILILDEA 504
Cdd:PRK11629 104 ALENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRPS-----------ELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1091156555 505 TSSIDTRTevlVQEAFQML----MKGRTSFII-------AHRLS 537
Cdd:PRK11629 173 TGNLDARN---ADSIFQLLgelnRLQGTAFLVvthdlqlAKRMS 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
364-557 |
2.10e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.66 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 364 IPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdyepSQLRQE-IGMVLQET---WLKSATIHDNIAYAN 439
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSEevdWSFPVLVEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 440 ---------PKASRDEVIEAAKA--ANADFFIKQLpngydtyledagDSLSQGQCQLLTIARIFLKLPRILILDEATSSI 508
Cdd:PRK15056 106 yghmgwlrrAKKRDRQIVTAALArvDMVEFRHRQI------------GELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091156555 509 DTRTEVLVQEAFQMLM-KGRTSFIIAHRLSTIQTADIILVMVSGEIVEVG 557
Cdd:PRK15056 174 DVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
27-283 |
2.18e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 55.94 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDV--------VLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLR 98
Cdd:cd18577 4 GLLAAIAAGAALPLMTIVFGDLFDAftdfgsgeSSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 99 KAVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGL-----LMVFN--QFFVGL---------LTiLVTIFSMakidl 162
Cdd:cd18577 84 KRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIgeklgLLIQSlsTFIAGFiiafiyswkLT-LVLLATL----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 163 lmlflvlfltPLSLFLARFIAKKSYHLYQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAI 242
Cdd:cd18577 158 ----------PLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1091156555 243 FYSSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLIT 283
Cdd:cd18577 228 LVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLT 268
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-554 |
2.24e-08 |
|
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: 53.53 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 367 GAKVAIVGPTGAGKSTLINLLMRFYEVDGGN-ILLDGKPITDYEPSQLRQEigmvlqetwlksatihdniayanpkasrd 445
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 446 evieaakaanadffikqlpngydtYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEA------ 519
Cdd:smart00382 53 ------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrll 108
|
170 180 190
....*....|....*....|....*....|....*
gi 1091156555 520 FQMLMKGRTSFIIAHRLSTIQTADIILVMVSGEIV 554
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
334-437 |
2.50e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 334 SSTVKGQIDFKNVIFGyNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL 413
Cdd:PRK11831 1 EQSVANLVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100
....*....|....*....|....*...
gi 1091156555 414 ---RQEIGMVLQETWL-KSATIHDNIAY 437
Cdd:PRK11831 80 ytvRKRMSMLFQSGALfTDMNVFDNVAY 107
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
344-398 |
2.76e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.76e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 344 KNVIFGYNKsKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:PRK15064 323 ENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
44-315 |
3.03e-08 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 55.20 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 44 LIGQAV-DVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLNLLPIAYLDKRGIGDLI 122
Cdd:cd18588 23 LFFQVIiDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 123 SRVttdtEQLSNgllmvFNQFFVG--------LLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSYHLYQNQT 194
Cdd:cd18588 103 ARV----RELES-----IRQFLTGsaltlvldLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 195 ASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGIGALRIMSG 274
Cdd:cd18588 174 QRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDG 253
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1091156555 275 AFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18588 254 ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
367-558 |
5.04e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 367 GAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGK----------PITDYEPSQLRQ----EIGMVLQE--TWLKSA- 429
Cdd:PRK10261 42 GETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHvrgaDMAMIFQEpmTSLNPVf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 TIHDNIAYA---NPKASRDEVIEAAKAANADFFIKQlpngYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATS 506
Cdd:PRK10261 122 TVGEQIAESirlHQGASREEAMVEAKRMLDQVRIPE----AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 507 SIDTRTEVLVQEAFQMLMKGRTS--FIIAHRLSTI-QTADIILVMVSGEIVEVGN 558
Cdd:PRK10261 198 ALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVaEIADRVLVMYQGEAVETGS 252
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
30-314 |
5.37e-08 |
|
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: 54.56 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 30 GTVVQVC---LTVYLPVLIGQAVDVVLSP------HSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKA 100
Cdd:cd18780 1 GTIALLVssgTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 101 VMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLAR 180
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 181 FIAKKsyhlyqnqtaSRGRQTQFieemvsQESLIQAFSAQEESSDHFRTInQEYANFSQSAIFYSSTVNPSTRFIN--SL 258
Cdd:cd18780 161 IYGKY----------VRKLSKKF------QDALAAASTVAEESISNIRTV-RSFAKETKEVSRYSEKINESYLLGKklAR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 259 IYGFLAGI---------------GALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAER 314
Cdd:cd18780 224 ASGGFNGFmgaaaqlaivlvlwyGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
346-514 |
8.20e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 346 VIFGynkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVLqeTW 425
Cdd:PRK09544 12 VSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLPL--TV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 426 LKSATIHdniayanPKASRDEVIEAAKAANADFFIKQlpngydtyledAGDSLSQGQCQLLTIARIFLKLPRILILDEAT 505
Cdd:PRK09544 87 NRFLRLR-------PGTKKEDILPALKRVQAGHLIDA-----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
....*....
gi 1091156555 506 SSIDTRTEV 514
Cdd:PRK09544 149 QGVDVNGQV 157
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
352-554 |
1.27e-07 |
|
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: 52.72 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 352 KSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKpITDYEPSQLRQEIGMVL---------- 421
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFgqktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 422 --QETWLKSATIHDnIAYANPKASRDEVIEAAKaanadffikqlpngydtyLEDAGDS----LSQGQCQLLTIARIFLKL 495
Cdd:cd03267 111 pvIDSFYLLAAIYD-LPPARFKKRLDELSELLD------------------LEELLDTpvrqLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 496 PRILILDEATSSIDTRTEVLVQEAFQMLMKGRTSFII--AHRLSTI-QTADIILVMVSGEIV 554
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
354-564 |
1.37e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKS----TLINLLMRFYEVDGGNILLDGKPItdyEPSQLRQEigmvlqetwlKSA 429
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGR----------KIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 430 TIHDNIAYA-NP-KASRDEVIEAAKAANADFFIKQLPNGYDTY-LEDAGDSL-------SQGQCQLLTIARIFLKLPRIL 499
Cdd:PRK10418 83 TIMQNPRSAfNPlHTMHTHARETCLALGKPADDATLTAALEAVgLENAARVLklypfemSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 500 ILDEATSSIDTRTEVLVQEAFQMLMKGRTS--FIIAHRLSTI-QTADIILVMVSGEIVEVGNHSELMA 564
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
357-558 |
1.40e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQ-EIGMVLQE-TWLKSATIHDN 434
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 I---AYANPKASRDEVIEAAKA-ANADFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSI-D 509
Cdd:PRK09700 101 LyigRHLTKKVCGVNIIDWREMrVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 510 TRTEVLVQEAFQMLMKGRTSFIIAHRLSTI-QTADIILVM------VSGEIVEVGN 558
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIrRICDRYTVMkdgssvCSGMVSDVSN 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-553 |
1.90e-07 |
|
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: 53.68 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 351 NKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVD-GGNILLDGKPITDYEPSQ-LRQEIGMVlQETWLKS 428
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMV-PEDRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHD-----NIAYA--NPKASRDEVIEAAKAANADFFIKQLP-NGYDTYLEDAGdsLSQGQCQLLTIARIFLKLPRILI 500
Cdd:TIGR02633 349 GIVPIlgvgkNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvKTASPFLPIGR--LSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 501 LDEATSSIDTRTEVLVQE-AFQMLMKGRTSFIIAHRLSTI-QTADIILVMVSGEI 553
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKlINQLAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-561 |
1.98e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 360 INLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQeiGMVL------QETWLKSATIH 432
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRA--GIMLcpedrkAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIAY-ANPKASRDEVI--EAAKAANADFFIKQL----PNGydtylEDAGDSLSQGQCQLLTIARIFLKLPRILILDEAT 505
Cdd:PRK11288 350 DNINIsARRHHLRAGCLinNRWEAENADRFIRSLniktPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 506 SSID--TRTEVLvQEAFQMLMKGRTSFIIAHRL-STIQTADIILVMVSGEIVEVGNHSE 561
Cdd:PRK11288 425 RGIDvgAKHEIY-NVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
350-509 |
2.72e-07 |
|
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: 53.40 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 350 YNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMrfyEVDggnilldgkpiTDYEPSQLRQE---IGMVLQETWL 426
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA---GVD-----------KDFNGEARPQPgikVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 -KSATIHDNI-------------------AYANPKASRD----------EVIEAAKAANADffiKQLPNGYDTYLEDAGD 476
Cdd:TIGR03719 80 dPTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaelqEIIDAADAWDLD---SQLEIAMDALRCPPWD 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1091156555 477 S----LSQGQCQLLTIARIFLKLPRILILDEATSSID 509
Cdd:TIGR03719 157 AdvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
367-557 |
2.79e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 367 GAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL---RQEIGMVLQETWlKSATIHDNIAYANPKAS 443
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPY-ASLDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 444 RDEVI---EAAKAANADFF--IKQLPNGYDTYLEDagdsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQE 518
Cdd:PRK10261 429 RVHGLlpgKAAAARVAWLLerVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1091156555 519 AFQMLMK--GRTSFIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:PRK10261 505 LLLDLQRdfGIAYLFISHDMAVVErISHRVAVMYLGQIVEIG 546
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-398 |
2.81e-07 |
|
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: 53.40 E-value: 2.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
354-554 |
3.82e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.71 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQ-LRQEIGMV----LQETWLKS 428
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrKGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 429 ATIHDNIAYAN-PKASRDEVI-EAAKAANADFFIKQL----PNgydtyLEDAGDSLSQGQCQLLTIARIFLKLPRILILD 502
Cdd:COG1129 345 LSIRENITLASlDRLSRGGLLdRRRERALAEEYIKRLriktPS-----PEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1091156555 503 EATSSID--TRTEV--LVQEafqmLMKGRTSFIIAhrlST-----IQTADIILVMVSGEIV 554
Cdd:COG1129 420 EPTRGIDvgAKAEIyrLIRE----LAAEGKAVIVI---SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
357-557 |
3.88e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.40 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINllmrfyevDGGnilldgkpitdYEPSQLRqeigmvlqetwlksatihdnIA 436
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGL-----------YASGKAR--------------------LI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 437 YANPKASRDEVIeaakaanadfFIKQLPN------GYDTyLEDAGDSLSQGQCQLLTIAR-IFLKLPRIL-ILDEATSSI 508
Cdd:cd03238 52 SFLPKFSRNKLI----------FIDQLQFlidvglGYLT-LGQKLSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 509 DTRT-EVLVQEAFQMLMKGRTSFIIAHRLSTIQTADIILVM------VSGEIVEVG 557
Cdd:cd03238 121 HQQDiNQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
354-545 |
4.52e-07 |
|
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: 53.09 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPItDYEPSQLRQEIGMVLQETWL-KSATIH 432
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILfHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 433 DNIA-YANPKA-SRDEVIEAAKAANADFFIKQLPNgydtylEDAGDsLSQGQCQLLTIARIFLKLPRILILDEATSSIDT 510
Cdd:TIGR01257 1022 EHILfYAQLKGrSWEEAQLEMEAMLEDTGLHHKRN------EEAQD-LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190
....*....|....*....|....*....|....*
gi 1091156555 511 RTEVLVQEAFQMLMKGRTSFIIAHRLStiqTADII 545
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLL 1126
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-564 |
5.92e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 354 KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-----------RQEIGMVLq 422
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlgvayipedRLGRGLVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 423 etwlkSATIHDNIA---YANPKASR------DEVIEAAKAANADFFIKqlPNGYDTyledAGDSLSQGQCQLLTIARIFL 493
Cdd:COG3845 350 -----DMSVAENLIlgrYRRPPFSRggfldrKAIRAFAEELIEEFDVR--TPGPDT----PARSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 494 KLPRILI-------LDE-ATSSIDTRtevLVQEAfqmlMKGRTSFIIAHRLSTI-QTADIILVMVSGEIVEVGNHSE--- 561
Cdd:COG3845 419 RDPKLLIaaqptrgLDVgAIEFIHQR---LLELR----DAGAAVLLISEDLDEIlALSDRIAVMYEGRIVGEVPAAEatr 491
|
....*...
gi 1091156555 562 -----LMA 564
Cdd:COG3845 492 eeiglLMA 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-553 |
7.44e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 360 INLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQL-----------RQEIGMVLQE--TWL 426
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAplAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 427 KSATIHDNIA-YANPKASRDEVIEAAKAANADFfikqlpngydTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEAT 505
Cdd:PRK15439 362 VCALTHNRRGfWIKPARENAVLERYRRALNIKF----------NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1091156555 506 SSIDTRTEVLVQEAFQMLMKGRTSFI-IAHRLSTI-QTADIILVMVSGEI 553
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
27-313 |
1.53e-06 |
|
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: 49.97 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLpVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKLN 106
Cdd:cd18561 2 VLLGLLITALYIAQA-WLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 107 LLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKS 186
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 187 YHLYQNQTASRGR-QTQFIEEMVSQESLiQAFSA--------QEESSDHF-RTINQEYANFSQSAIfysstvnpsTRFIN 256
Cdd:cd18561 161 KDTGRRHWAAYGRlSAQFLDSLQGMTTL-KAFGAskrrgnelAARAEDLRqATMKVLAVSLLSSGI---------MGLAT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 257 SLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAE 313
Cdd:cd18561 231 ALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
355-509 |
1.79e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 355 PLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYEPSQLRQEIGMVlqeTWLKS-ATIHD 433
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL---PGLKAdLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 434 NIAYANPKASRdeviEAAKAANADFFIKQLPNGYDTYLEdagdSLSQGQCQLLTIARIFLKLPRILILDEATSSID 509
Cdd:PRK13543 102 NLHFLCGLHGR----RAKQMPGSALAIVGLAGYEDTLVR----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
360-509 |
1.97e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 360 INLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITDYE------PSQLRqeIGMVLQETWL-KSATIH 432
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEkgiclpPEKRR--IGYVFQDARLfPHYKVR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 433 DNIAYANPKASRDEVieaakaanaDFFIKQLpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSID 509
Cdd:PRK11144 95 GNLRYGMAKSMVAQF---------DKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
478-564 |
2.65e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 478 LSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVlvqEAFQMLMK-----GRTSFIIAHRLSTI-QTADIILVMVSG 551
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQA---QIFRLLTRlnqnnNTTILLISHDLQMLsQWADKINVLYCG 235
|
90
....*....|...
gi 1091156555 552 EIVEVGNHSELMA 564
Cdd:PRK15093 236 QTVETAPSKELVT 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-398 |
2.90e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 2.90e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 341 IDFKNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNI 398
Cdd:PRK11819 325 IEAENLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-553 |
3.09e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 372 IVGPTGAGKSTLINLLMRFYEvdG---GNILLDGKPITDYEPSQ-LRQEIGMVlQETWLKSATIHD-----NIAYAN-PK 441
Cdd:PRK13549 293 IAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKIRNPQQaIAQGIAMV-PEDRKRDGIVPVmgvgkNITLAAlDR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 442 ASRDEVI-EAAKAANADFFIKQL----PNgydtyLEDAGDSLSQGQCQLLTIARIFLKLPRILILDEATSSID--TRTEV 514
Cdd:PRK13549 370 FTGGSRIdDAAELKTILESIQRLkvktAS-----PELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEI 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1091156555 515 ------LVQEAFQMLMkgrtsfiIAHRLSTI-QTADIILVMVSGEI 553
Cdd:PRK13549 445 yklinqLVQQGVAIIV-------ISSELPEVlGLSDRVLVMHEGKL 483
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
21-315 |
3.51e-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: 49.12 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQwinpLLYNRLIFHYVAS---- 96
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLR----LLRSYILAWIGARfdhr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 97 LRKAVMEKLNLLPIAYLDKRGIGDLISRVTtDTEQLSN-----GLLMVFNQFFVGLLTILVTIFSmakidllmlfLVLFL 171
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREfltgqALLALLDLPFVLIFLGLIWYLG----------GKLVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 172 TPLSLFLARFI-AKKSYHLYQNQTASRGRQTQ----FIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSS 246
Cdd:cd18566 146 VPLVLLGLFVLvAILLGPILRRALKERSRADErrqnFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1091156555 247 TVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18566 226 VAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
325-518 |
4.02e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 325 NITGTEKL--DSSTVKGQIDF--KNVIFGYNkSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL 400
Cdd:PRK11147 300 EVMGTAKMqvEEASRSGKIVFemENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 401 DGKPITDYEpSQLRQEIGmvlqetwlKSATIHDNIAyanpkASRDEVieaakaanadffikqLPNGYD----TYLED--- 473
Cdd:PRK11147 379 GTKLEVAYF-DQHRAELD--------PEKTVMDNLA-----EGKQEV---------------MVNGRPrhvlGYLQDflf 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 474 -------AGDSLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQE 518
Cdd:PRK11147 430 hpkramtPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEE 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
366-563 |
4.60e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 366 AGAKVAIVGPTGAGKSTLINLL--MRFYEvdgGNILLDGKPITDYEPSQLRQEIGMVLQETwlKSATIHDNIAY------ 437
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMagLLPGS---GSIQFAGQPLEAWSAAELARHRAYLSQQQ--TPPFAMPVFQYltlhqp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 438 --ANPKASRDEVIEAAKAAnadffikqlpnGYDTYLEDAGDSLSQGQCQLLTIARIFLKL-PRI------LILDEATSSI 508
Cdd:PRK03695 96 dkTRTEAVASALNEVAEAL-----------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwPDInpagqlLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1091156555 509 DTRTEV-LVQEAFQMLMKGRTSFIIAHRLS-TIQTADIILVMVSGEIVEVGNHSELM 563
Cdd:PRK03695 165 DVAQQAaLDRLLSELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
23-315 |
4.70e-06 |
|
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: 48.70 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 23 LVGMALLgtvVQVcLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVM 102
Cdd:cd18779 7 ILLASLL---LQL-LGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 103 EKLNLLPIAYLDKRGIGDLISRVTTDT---EQLSNGLL-MVFNQFFVGLLTILVTIFS--MAKIdllmlFLVLFLTPLSL 176
Cdd:cd18779 83 EHLLRLPYRFFQQRSTGDLLMRLSSNAtirELLTSQTLsALLDGTLVLGYLALLFAQSplLGLV-----VLGLAALQVAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 177 FLArfIAKKSYHLYQNQTASRGR-QTQFIEeMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPST--- 252
Cdd:cd18779 158 LLA--TRRRVRELMARELAAQAEaQSYLVE-ALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLatl 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1091156555 253 RFINSLIygfLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18779 235 RLAAPLV---LLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
350-509 |
5.80e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 350 YNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTlinlLMRfyevdggnIL--LDgkpiTDYEPSQLRQE---IGMVLQET 424
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKST----LLR--------IMagVD----KEFEGEARPAPgikVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 WL-KSATIHDNI-------------------AYANPKASRD----------EVIEAAKAANADFFIKQ------LPNGyd 468
Cdd:PRK11819 80 QLdPEKTVRENVeegvaevkaaldrfneiyaAYAEPDADFDalaaeqgelqEIIDAADAWDLDSQLEIamdalrCPPW-- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1091156555 469 tyleDAG-DSLSQGQ------CQLLtiarifLKLPRILILDEATSSID 509
Cdd:PRK11819 158 ----DAKvTKLSGGErrrvalCRLL------LEKPDMLLLDEPTNHLD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
348-540 |
7.23e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 348 FGYNkskPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLmrfyevdGGNILLD-GKPI--TDYEPSQLRQ-----EIGM 419
Cdd:PRK11147 13 FSDA---PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIyeQDLIVARLQQdpprnVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 420 V-------LQET--WLKS--ATIHD--------NIayaNPKASRDEVIEAAKAANADFFI----KQLPNGYDTYLedagD 476
Cdd:PRK11147 83 VydfvaegIEEQaeYLKRyhDISHLvetdpsekNL---NELAKLQEQLDHHNLWQLENRInevlAQLGLDPDAAL----S 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 477 SLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRT-EVLvqEAFQMLMKGRTSFiIAHRLSTIQ 540
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL--EGFLKTFQGSIIF-ISHDRSFIR 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
350-534 |
7.84e-06 |
|
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: 47.40 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 350 YNKSKPLLNGINLHIPAGA-----KVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKPITdYEPSQLRQEIGMVLQET 424
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 425 WLKSATIHDNIAYANpkasrDEVIEAAKaanadffIKQLpngYDTYLEDagdsLSQGQCQLLTIARIFLKLPRILILDEA 504
Cdd:cd03237 82 LSSITKDFYTHPYFK-----TEIAKPLQ-------IEQI---LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190
....*....|....*....|....*....|..
gi 1091156555 505 TSSIDTRTEVLVQEAFQ--MLMKGRTSFIIAH 534
Cdd:cd03237 143 SAYLDVEQRLMASKVIRrfAENNEKTAFVVEH 174
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
367-557 |
7.86e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 367 GAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILL---DGKPITDYEPSQ------LRQEIGMVLQ--ETWLKSA-TIHDN 434
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrrlLRTEWGFVHQhpRDGLRMQvSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 435 IA----------YANPKA------SRDEvIEAAKaanadffIKQLPNGYdtyledagdslSQGQCQLLTIARIFLKLPRI 498
Cdd:PRK11701 112 IGerlmavgarhYGDIRAtagdwlERVE-IDAAR-------IDDLPTTF-----------SGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1091156555 499 LILDEATSSIDtrteVLVQEAFQMLMKGRTS------FIIAHRLSTIQ-TADIILVMVSGEIVEVG 557
Cdd:PRK11701 173 VFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
357-519 |
1.02e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 47.77 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGkpitdYEPSQLRQE----IGMVL-QET---W--- 425
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-----YVPFKRRKEfarrIGVVFgQRSqlwWdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 426 -LKSATIHDNIaYanpkasrdEVIEAAKAANADFFIKQLpngydtyleDAGD-------SLSQGQ---CQLltiARIFLK 494
Cdd:COG4586 113 aIDSFRLLKAI-Y--------RIPDAEYKKRLDELVELL---------DLGElldtpvrQLSLGQrmrCEL---AAALLH 171
|
170 180
....*....|....*....|....*
gi 1091156555 495 LPRILILDEATSSIDtrteVLVQEA 519
Cdd:COG4586 172 RPKILFLDEPTIGLD----VVSKEA 192
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
252-315 |
1.40e-05 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 47.14 E-value: 1.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 252 TRFINSLIY--GFLAG--IGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18583 223 LNAVQSLILtlGLLAGcfLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
357-387 |
3.02e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 3.02e-05
10 20 30
....*....|....*....|....*....|.
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLINLL 387
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
110-315 |
5.11e-05 |
|
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: 45.38 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 110 IAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSYHL 189
Cdd:cd18784 84 IGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 190 YQNQTASRGRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQE-YANFSQSAIFYSSTVNPSTRFINSLIYGFLAGIGA 268
Cdd:cd18784 164 SKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDtYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGH 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1091156555 269 LrIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACAERL 315
Cdd:cd18784 244 L-VITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
356-512 |
5.61e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 356 LLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFYE---VDGGNILLDGKPITdyepSQLRQEIGMVLQE-TWLKSATI 431
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLD----SSFQRSIGYVQQQdLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 432 HDNIAYANPKASRDEVIEAAKAANADFFIKQLpnGYDTYLE----DAGDSLSQGQCQLLTIARIFLKLPRILI-LDEATS 506
Cdd:TIGR00956 854 RESLRFSAYLRQPKSVSKSEKMEYVEEVIKLL--EMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
....*.
gi 1091156555 507 SIDTRT 512
Cdd:TIGR00956 932 GLDSQT 937
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
340-562 |
7.14e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 340 QIDFKNVIFGyNKSKPL--LNGINLHIPAGAKVAIVGPTGAGKST-------LINLLMRfyeVDGGNILLDGKPITDYEP 410
Cdd:PRK11022 5 NVDKLSVHFG-DESAPFraVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGR---VMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 411 SQLRQ----EIGMVLQE--TWLK-SATIHDNIAYA-------NPKASRDEVIE-------AAKAANADFFIKQLpngydt 469
Cdd:PRK11022 81 KERRNlvgaEVAMIFQDpmTSLNpCYTVGFQIMEAikvhqggNKKTRRQRAIDllnqvgiPDPASRLDVYPHQL------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 470 yledagdslSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGRTS--FIIAHRLSTI-QTADIIL 546
Cdd:PRK11022 155 ---------SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKII 225
|
250
....*....|....*.
gi 1091156555 547 VMVSGEIVEVGNHSEL 562
Cdd:PRK11022 226 VMYAGQVVETGKAHDI 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
370-552 |
2.00e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 370 VAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKpiTDYEPSQLRQEIGMVLQEtWLKSAT--IHDNIAYAnpkasrdEV 447
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPQYIKPDYDGTVED-LLRSITddLGSSYYKS-------EI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 448 IEAAkaanadffikQLPNGYDTYLEDagdsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQMLMKGR 527
Cdd:PRK13409 438 IKPL----------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|....*...
gi 1091156555 528 --TSFIIAHRLSTIQT-ADIILVmVSGE 552
Cdd:PRK13409 504 eaTALVVDHDIYMIDYiSDRLMV-FEGE 530
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
27-285 |
2.49e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 43.30 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVV---LSPHSMILLLPiMWKMVAVILANTIIQWINPLLYNRLIFH----YVASLRK 99
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVIsrsLKETNGDFIED-LKKPALKLLGLYLLQSLLTFAYISLLSVvgerVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 100 AVMEKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQffvGLLTILVTI---FSMAKIDLLMLFLVLFLTPLSL 176
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQ---GLRSVTQTVgcvVSLYLISPKLTLLLLVIVPVVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 177 ----FLARFIAKKSYHLyQNQTAsrgRQTQFIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQS-----AIFYSST 247
Cdd:cd18574 157 lvgtLYGSFLRKLSRRA-QAQVA---KATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKlglgiGIFQGLS 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 1091156555 248 vnpsTRFINSLIYGFLAGIGALrIMSGAFSVGQLITFL 285
Cdd:cd18574 233 ----NLALNGIVLGVLYYGGSL-VSRGELTAGDLMSFL 265
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
109-315 |
2.64e-04 |
|
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: 43.26 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 109 PIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAkidllmlflvlFLTPLSLFLARFIAkKSYH 188
Cdd:cd18580 86 PMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIA-----------IVSPYFLIVLPPLL-VVYY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 189 LYQNQTASRGRQTQFIeEMVS--------QESL-----IQAFSAQeessDHFRTINQEYANFSQSAIFYSSTVNpstR-- 253
Cdd:cd18580 154 LLQRYYLRTSRQLRRL-ESESrsplyshfSETLsglstIRAFGWQ----ERFIEENLRLLDASQRAFYLLLAVQ---Rwl 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1091156555 254 -----FINSLIYGFLAGIG-ALRIMSGAFSVGQLITFLNYVNQYtkpFNDISSVLSEMQSALACAERL 315
Cdd:cd18580 226 glrldLLGALLALVVALLAvLLRSSISAGLVGLALTYALSLTGS---LQWLVRQWTELETSMVSVERI 290
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
367-389 |
3.36e-04 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 41.33 E-value: 3.36e-04
|
| YqeH |
cd01855 |
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ... |
344-391 |
4.60e-04 |
|
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH 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.
Pssm-ID: 206748 [Multi-domain] Cd Length: 191 Bit Score: 41.48 E-value: 4.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1091156555 344 KNVIFGYNKS----KPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLLMRFY 391
Cdd:cd01855 98 KDVILVSAKKgwgvEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLKSN 149
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
367-552 |
7.03e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 367 GAKVAIVGPTGAGKSTLINLLMRFYEVDGGNILLDGKpITdYEPSQLRQEIGMVLQETwLKSA---TIHDNIAYAnpkas 443
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-IS-YKPQYISPDYDGTVEEF-LRSAntdDFGSSYYKT----- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 444 rdEVIEAakaanadFFIKQLpngYDTYLEDagdsLSQGQCQLLTIARIFLKLPRILILDEATSSIDTRTEVLVQEAFQML 523
Cdd:COG1245 438 --EIIKP-------LGLEKL---LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180 190
....*....|....*....|....*....|....
gi 1091156555 524 M--KGRTSFIIAHRLSTIqtaDII---LVMVSGE 552
Cdd:COG1245 502 AenRGKTAMVVDHDIYLI---DYIsdrLMVFEGE 532
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
369-389 |
1.31e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 38.75 E-value: 1.31e-03
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
21-308 |
1.80e-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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.58 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 21 KSLVGMALLGTVVQVCLTVYLPVLIGQAVDVVLSPHSMILLLPIMWKMVAVILANTIIQWINpllynRLIFHYVAS---- 96
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLR-----RYLLLVATTrida 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 97 -LRKAVMEKLNLLPIAYLDKRGIGDLISRVTtDTEQLSNGL-------------LMVFNQ---FFVGLLTILVTIFSMAk 159
Cdd:cd18783 76 rLALRTFDRLLSLPIDFFERTPAGVLTKHMQ-QIERIRQFLtgqlfgtlldatsLLVFLPvlfFYSPTLALVVLAFSAL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 160 idllmlflvlfltplsLFLARFIAKKSY-HLYQNQTASRGRQTQFIEEMVSQESLIQAFS---AQEESSDH--FRTINqe 233
Cdd:cd18783 154 ----------------IALIILAFLPPFrRRLQALYRAEGERQAFLVETVHGIRTVKSLAlepRQRREWDErvARAIR-- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1091156555 234 yANFSQSAIfySSTVNPSTRFINSLIYGFLAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSA 308
Cdd:cd18783 216 -ARFAVGRL--SNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEA 287
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
27-315 |
1.90e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 40.55 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGTVVQVCLTVYLPVLIGQAVDVVLS----PHSMILLLPIMwkMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVM 102
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSypdePLSEGYLLALA--LFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 103 EKLNLLPIAYLDKRGIGDLISRVTTDTEQLSNGLLMVFN---------------------QFFVGLLTILVTIfsmakid 161
Cdd:cd18579 80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYlwsaplqiivalyllyrllgwAALAGLGVLLLLI------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 162 llmlflvlfltPLSLFLARFIAKksyhLYQNQTASRGRQTQFIEEMVSQeslIQA--FSAQEessDHFRTI-----NQEY 234
Cdd:cd18579 153 -----------PLQAFLAKLISK----LRKKLMKATDERVKLTNEILSG---IKVikLYAWE---KPFLKRieelrKKEL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 235 ANFSQSAIFYSSTVnpstrFINSLIYGF--LAGIGALRIMSGAFSVGQLITFLNYVNQYTKPFNDISSVLSEMQSALACA 312
Cdd:cd18579 212 KALRKFGYLRALNS-----FLFFSTPVLvsLATFATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSL 286
|
...
gi 1091156555 313 ERL 315
Cdd:cd18579 287 KRI 289
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
27-132 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 27 ALLGtVVQVCLTVYLPVLIGQAVD-VVLSPHSMILLLPIMWKMVAVILANTIIQWINPLLYNRLIFHYVASLRKAVMEKL 105
Cdd:cd18584 2 VLLG-LLAALLIIAQAWLLARIIAgVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100
....*....|....*....|....*..
gi 1091156555 106 NLLPIAYLDKRGIGDLISRVTTDTEQL 132
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDAL 107
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
346-385 |
2.56e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1091156555 346 VIFGYNKSKplLNGINLHIPAGAKVAIVGPTGAGKSTLIN 385
Cdd:TIGR00630 615 TLKGARENN--LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-387 |
2.75e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1091156555 341 IDFKNVIFGYNKSKPLLNGINLHIPAGAKVAIVGPTGAGKSTLINLL 387
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI 555
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
357-385 |
3.03e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 3.03e-03
10 20
....*....|....*....|....*....
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLIN 385
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
357-509 |
3.13e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTL-INLLMRFYEVD-GGNILLDGKPITDYEPSQL-----------RQEIGMVLQE 423
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDAidaglayvtedRKGYGLNLID 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 424 TwlksatIHDNIAYAN-PKASRDEVI-EAAKAANADFFIKQLPNGYDTYLEDAGdSLSQGQCQLLTIARIFLKLPRILIL 501
Cdd:NF040905 356 D------IKRNITLANlGKVSRRGVIdENEEIKVAEEYRKKMNIKTPSVFQKVG-NLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*...
gi 1091156555 502 DEATSSID 509
Cdd:NF040905 429 DEPTRGID 436
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
370-387 |
3.46e-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: 39.30 E-value: 3.46e-03
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
367-389 |
3.86e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 40.04 E-value: 3.86e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
357-385 |
5.40e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 5.40e-03
10 20
....*....|....*....|....*....
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLIN 385
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
367-389 |
5.71e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 39.00 E-value: 5.71e-03
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
37-289 |
5.81e-03 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 39.15 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 37 LTVYLPVLIGQAVDVVLSPHSMILLLpIMWKMVAV--ILANTIIQwinpLLYNRLIfHyvaSLRKAVM----EKLNLLPI 110
Cdd:cd18562 14 VQFAEPVLFGRVVDALSSGGDAFPLL-ALWAALGLfsILAGVLVA----LLADRLA-H---RRRLAVMasyfEHVITLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 111 AYLDKRGIGDLISRVTTDTEQLSNGLLMVFNQFFVGLLTILVTIFSMAKIDLLMLFLVLFLTPLSLFLARFIAKKSYHLY 190
Cdd:cd18562 85 SFHSQRGSGRLLRIMLRGTDALFGLWLGFFREHLAALVSLIVLLPVALWMNWRLALLLVVLAAVYAALNRLVMRRTKAGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1091156555 191 ----QNQTASRGRqtqfIEEMVSQESLIQAFSAQEESSDHFRTINQEYANFSQSAIFYSSTVNPSTRFINSLIYGFLAGI 266
Cdd:cd18562 165 aaveEHHSALSGR----VGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVLNWWALASVLTRAASTLTMVAIFAL 240
|
250 260
....*....|....*....|...
gi 1091156555 267 GALRIMSGAFSVGQLITFLNYVN 289
Cdd:cd18562 241 GAWLVQRGELTVGEIVSFVGFAT 263
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
370-401 |
6.53e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 39.16 E-value: 6.53e-03
10 20 30
....*....|....*....|....*....|...
gi 1091156555 370 VAIVGPTGAGKSTLINLLM-RFYEVDGGNILLD 401
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLlQLLRYGARIVIFD 239
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
370-388 |
7.18e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 38.56 E-value: 7.18e-03
|
| trmE |
PRK05291 |
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE; |
367-389 |
7.54e-03 |
|
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
Pssm-ID: 235392 [Multi-domain] Cd Length: 449 Bit Score: 38.94 E-value: 7.54e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
357-385 |
9.09e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 9.09e-03
10 20
....*....|....*....|....*....
gi 1091156555 357 LNGINLHIPAGAKVAIVGPTGAGKSTLIN 385
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| |
