|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-597 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 679.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 18 RQRDPRQLRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFG 97
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL---AGGDLSALLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 98 AAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQ 177
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 178 TSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAAL 257
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 258 RRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELL 337
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 338 DERSDLPGPAAPRPLSRAEGRVRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVE 416
Cdd:COG1132 319 DEPPEIPDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 417 VDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLS 496
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 497 GGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTH 576
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570 580
....*....|....*....|.
gi 499192068 577 EGLMAAGGLYRELYELQFRQQ 597
Cdd:COG1132 559 EELLARGGLYARLYRLQFGEE 579
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
20-594 |
0e+00 |
|
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: 540.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 20 RDPRQLRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKVGStdtGPLDRTVLSLLGIFALSACFGAA 99
Cdd:TIGR02204 1 KRLRPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSS---GLLNRYFAFLLVVALVLALGTAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 100 QAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTS 179
Cdd:TIGR02204 78 RFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 180 PRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRR 259
Cdd:TIGR02204 158 PKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 260 ARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDE 339
Cdd:TIGR02204 238 IRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 340 RSDLPGPAAPRPLS-RAEGRVRFVDVGFTYAGAP---ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRV 415
Cdd:TIGR02204 318 EPDIKAPAHPKTLPvPLRGEIEFEQVNFAYPARPdqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 416 EVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKL 495
Cdd:TIGR02204 398 LLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 496 SGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:TIGR02204 478 SGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
|
570
....*....|....*....
gi 499192068 576 HEGLMAAGGLYRELYELQF 594
Cdd:TIGR02204 558 HAELIAKGGLYARLARLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-593 |
6.29e-171 |
|
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: 502.83 E-value: 6.29e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 16 DARQRDPRQLRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDasflKV-GSTDTGPLDRTVLSLLGIFALSA 94
Cdd:COG2274 135 DKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVID----RVlPNQDLSTLWVLAIGLLLALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 95 CFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLtSDVGTVQAVTSTALAQLASQGFTLIGSVLL 174
Cdd:COG2274 211 LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 175 LVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFR 254
Cdd:COG2274 290 LFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 255 AALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIF 334
Cdd:COG2274 370 ARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 335 ELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTA 412
Cdd:COG2274 450 DILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 413 GRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERG 492
Cdd:COG2274 530 GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 493 VKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVA 572
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
570 580
....*....|....*....|.
gi 499192068 573 DGTHEGLMAAGGLYRELYELQ 593
Cdd:COG2274 690 DGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
26-596 |
5.50e-165 |
|
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: 482.68 E-value: 5.50e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 26 RRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLA 105
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF---GGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLL 185
Cdd:TIGR02203 80 WVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 186 TLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQAL 265
Cdd:TIGR02203 160 VVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 266 MTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSDLPg 345
Cdd:TIGR02203 240 SSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 346 pAAPRPLSRAEGRVRFVDVGFTY--AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR 423
Cdd:TIGR02203 319 -TGTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 424 AYALADLRRQVGLVPQETLLFSGTVAENILYGRPG-ASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQR 502
Cdd:TIGR02203 398 DYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 503 VAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
570
....*....|....
gi 499192068 583 GGLYRELYELQFRQ 596
Cdd:TIGR02203 558 NGLYAQLHNMQFRE 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-602 |
7.60e-140 |
|
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: 419.22 E-value: 7.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 2 TPRSGPRPAASARRDARQRDPRQLRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASflkvgstDTGPLDR 81
Cdd:COG5265 1 APSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDAL-------LSGAAAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 82 TVLSLLGIFA------LSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLT---SRLTSDVGTVqa 152
Cdd:COG5265 74 LVVPVGLLLAygllrlLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSrdiERGTKGIEFL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 153 vTSTALAQLASqgfTLIG----SVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISG 228
Cdd:COG5265 152 -LRFLLFNILP---TLLEialvAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 229 VRVVQSFTAEGLEEERYGQgvlasFRAALRRARLQALMTgvMSFLTFG-------ALALVLWFGGRQVMSGALTPGNLVT 301
Cdd:COG5265 228 YETVKYFGNEAREARRYDE-----ALARYERAAVKSQTS--LALLNFGqaliialGLTAMMLMAAQGVVAGTMTVGDFVL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 302 FLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTY-AGAPALQDITFD 380
Cdd:COG5265 301 VNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYdPERPILKGVSFE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 381 VPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGAS 460
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDAS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 461 QAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL 540
Cdd:COG5265 461 EEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV 540
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 541 MVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYELQFRQQQEARR 602
Cdd:COG5265 541 ARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEA 602
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-589 |
6.96e-138 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 417.97 E-value: 6.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 25 LRRLLAYARPyRLPFVLGVLATLISSGLGLVF-PRLFGTLIDASflkVGSTDTGPLDRTVLSL----LGIFALSACFGAA 99
Cdd:TIGR00958 149 LFRLLGLSGR-DWPWLISAFVFLTLSSLGEMFiPFYTGRVIDTL---GGDKGPPALASAIFFMcllsIASSVSAGLRGGS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 100 QAYLLARVgagvVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTS 179
Cdd:TIGR00958 225 FNYTMARI----NLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 180 PRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRR 259
Cdd:TIGR00958 301 PRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 260 ARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDE 339
Cdd:TIGR00958 381 ALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDR 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 340 RSDLPGPAAPRPlSRAEGRVRFVDVGFTY---AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVE 416
Cdd:TIGR00958 461 KPNIPLTGTLAP-LNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 417 VDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLS 496
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 497 GGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERlmVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTH 576
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
570
....*....|...
gi 499192068 577 EGLMAAGGLYREL 589
Cdd:TIGR00958 698 KQLMEDQGCYKHL 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
359-590 |
2.78e-132 |
|
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: 386.20 E-value: 2.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGL 436
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 517 ILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELY 590
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-596 |
6.74e-131 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 395.54 E-value: 6.74e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 26 RRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLA 105
Cdd:PRK11176 14 RRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGF---GKADRSVLKWMPLVVIGLMILRGITSFISSYCIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLL 185
Cdd:PRK11176 91 WVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 186 TLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQAL 265
Cdd:PRK11176 171 LIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 266 MTGVMSFLTFGALALVLWFGGRQVMSGALTPGNlVTFLFYA-LQVGGTVAALTGVFNQFQEALGASSRIFELLD---ERS 341
Cdd:PRK11176 251 SDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSmIALMRPLKSLTNVNAQFQRGMAACQTLFAILDleqEKD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 342 DlpgpaAPRPLSRAEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG 419
Cdd:PRK11176 330 E-----GKRVIERAKGDIEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 420 HDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGA-SQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGG 498
Cdd:PRK11176 405 HDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 499 QRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEG 578
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
570
....*....|....*...
gi 499192068 579 LMAAGGLYRELYELQFRQ 596
Cdd:PRK11176 565 LLAQNGVYAQLHKMQFGQ 582
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
23-592 |
7.25e-117 |
|
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: 359.08 E-value: 7.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 23 RQLRRLLAYARPYRLPFVLGVLATLIS--SGLGLVFprLFGTLIDASFLkvgstdTGPldrtvlsllgIFALSACFGAAQ 100
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTllAGIGLLA--LSGWLIAAAAL------APP----------ILNLFVPIVGVR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 101 AYLLARVGA-------------GVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFT 167
Cdd:COG4987 63 AFAIGRTVFrylerlvshdatlRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 168 LIGSVLLLVQTSPRLSLlTLAIIPLVIGTAVTI--GRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERY 245
Cdd:COG4987 143 ILAAVAFLAFFSPALAL-VLALGLLLAGLLLPLlaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 246 GQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQE 325
Cdd:COG4987 222 DAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 326 ALGASSRIFELLDERSDLPGPAAPRPLSRAeGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNL 403
Cdd:COG4987 302 VRAAARRLNELLDAPPAVTEPAEPAPAPGG-PSLELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 404 IPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGG 483
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 484 YGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRIL 563
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
570 580
....*....|....*....|....*....
gi 499192068 564 VMDAGRVVADGTHEGLMAAGGLYRELYEL 592
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-584 |
7.34e-117 |
|
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: 358.69 E-value: 7.34e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 26 RRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLA 105
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLL 185
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 186 TLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERygqgvlasFRAA---LRRA-- 260
Cdd:COG4988 164 LLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAER--------IAEAsedFRKRtm 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 261 ---RLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFL-----FYA--LQVGgtvaaltgvfNQF---QEAL 327
Cdd:COG4988 236 kvlRVAFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLllapeFFLplRDLG----------SFYharANGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 328 GASSRIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPR 406
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 407 FWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGA 486
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 487 VVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMD 566
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLD 545
|
570
....*....|....*...
gi 499192068 567 AGRVVADGTHEGLMAAGG 584
Cdd:COG4988 546 DGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
42-333 |
1.80e-115 |
|
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: 345.24 E-value: 1.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 42 GVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFS 121
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAL---GGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 122 HLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIG 201
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 202 RRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALV 281
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 282 LWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
359-593 |
3.26e-109 |
|
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: 327.57 E-value: 3.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY---AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVG 435
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 516 LILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYELQ 593
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
35-593 |
3.62e-103 |
|
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: 327.47 E-value: 3.62e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 35 YRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKVGSTDtgpLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVAD 114
Cdd:TIGR01846 137 YRKQFREVLLISLALQLFALVTPLLFQVVIDKVLVHRGLST---LSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 115 LRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIgSVLLLVQTSPRLSLLTLAIIPLVI 194
Cdd:TIGR01846 214 LGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVV-FLAVMFFYSPTLTGVVIGSLVCYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 195 GTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLT 274
Cdd:TIGR01846 293 LLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQ 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 275 FGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSDlPGPAAPRPLSR 354
Cdd:TIGR01846 373 KLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTE-PRSAGLAALPE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 355 AEGRVRFVDVGFTYA--GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRR 432
Cdd:TIGR01846 452 LRGAITFENIRFRYApdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKD 512
Cdd:TIGR01846 532 QMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 513 PRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYEL 592
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691
|
.
gi 499192068 593 Q 593
Cdd:TIGR01846 692 Q 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
27-602 |
1.05e-102 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 323.07 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 27 RLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgstdtgpldRTVLSLLGIFALSACFGAAQAYLLAR 106
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGK----------GDIFPLLAAWAGFGLFNIIAGVLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 107 vGAGVVADLRRA-----LFSHLLSLSPRFFGNHRTGDLTSRLtsdvgtVQAVTSTALAQLA--SQGFTLIGSVLLLVQTS 179
Cdd:PRK13657 79 -HADRLAHRRRLavlteYFERIIQLPLAWHSQRGSGRALHTL------LRGTDALFGLWLEfmREHLATLVALVVLLPLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 180 P----RLS--LLTLAIIPLVIGTAVTigRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFT---AEGLEEERYGQGVL 250
Cdd:PRK13657 152 LfmnwRLSlvLVVLGIVYTLITTLVM--RKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNrieAETQALRDIADNLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 251 ASFRAALRRARLQALMTGVMSFLTFGA-LALVLWFggrqVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGA 329
Cdd:PRK13657 230 AAQMPVLSWWALASVLNRAASTITMLAiLVLGAAL----VQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 330 SSRIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTYAG-APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFW 408
Cdd:PRK13657 306 LEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 409 DVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVV 488
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 489 GERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAG 568
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
570 580 590
....*....|....*....|....*....|....
gi 499192068 569 RVVADGTHEGLMAAGGLYRELYELQFRQQQEARR 602
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALLRAQGMLQEDERR 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
359-593 |
1.95e-102 |
|
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: 309.93 E-value: 1.95e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:cd03253 1 IEFENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILI 517
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 518 LDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYELQ 593
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
357-584 |
1.70e-98 |
|
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: 299.53 E-value: 1.70e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 357 GRVRFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVG 435
Cdd:cd03254 1 GEIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 516 LILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGG 584
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
43-333 |
2.22e-91 |
|
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: 283.22 E-value: 2.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18575 2 LIALLIAAAATLALGQGLRLLIDQGF---AAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGR 202
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 203 RIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVL 282
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 499192068 283 WFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18575 239 WLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-589 |
8.94e-85 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 279.14 E-value: 8.94e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 20 RDPRQLRRLLAyarpyRLPFVLGVLATLISSGLGLVFPRLF-----GTLIDaSFLKVGSTD-TGPLdrtVLSLLGIFALS 93
Cdd:TIGR03796 137 RKPSLLRALWR-----RLRGSRGALLYLLLAGLLLVLPGLVipafsQIFVD-EILVQGRQDwLRPL---LLGMGLTALLQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 94 ACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDvGTVQAVTSTALAQLASQGFTLIGSVL 173
Cdd:TIGR03796 208 GVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 174 LLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAeeaISGVRVVQSFTAEGLEEERYGQ--GVLA 251
Cdd:TIGR03796 287 LMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVA---ISGLQSIETLKASGLESDFFSRwaGYQA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 252 -SFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGAS 330
Cdd:TIGR03796 364 kLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 331 SRIFELLDERSDL------PGPAAPRPLSRAEGRVRFVDVGFTYA--GAPALQDITFDVPAGQVVALVGPSGAGKTTLVN 402
Cdd:TIGR03796 444 NRLDDVLRNPVDPlleepeGSAATSEPPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 403 LIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEG 482
Cdd:TIGR03796 524 LVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPG 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 483 GYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLmvGRTTFVVAHRLSTIRSADRI 562
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLSTIRDCDEI 681
|
570 580
....*....|....*....|....*..
gi 499192068 563 LVMDAGRVVADGTHEGLMAAGGLYREL 589
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
359-569 |
4.76e-84 |
|
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: 260.01 E-value: 4.76e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGL 436
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSGTVAENILygrpgasqaeveaaahaahaheficeleggygavvgergvklSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03228 81 VPQDPFLFSGTIRENIL------------------------------------------SGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499192068 517 ILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGR 569
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
359-593 |
6.30e-84 |
|
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: 262.42 E-value: 6.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYA--GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGL 436
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 517 ILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYELQ 593
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
42-333 |
1.45e-81 |
|
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: 257.87 E-value: 1.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 42 GVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFS 121
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTI---IKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 122 HLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIG 201
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 202 RRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALV 281
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 282 LWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
84-590 |
2.99e-81 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 269.69 E-value: 2.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 84 LSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLAS 163
Cdd:TIGR01193 200 IGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 164 QGFTLIGSVLLLVQTSpRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLE-- 241
Cdd:TIGR01193 280 MWILVIVGLFLVRQNM-LLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERys 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 242 --EERYGQGVLASFRAALRRARLQALMTGVMSFLTfgalALVLWFGGRQVMSGALTPGNLVTFlfyALQVGGTVAALTGV 319
Cdd:TIGR01193 359 kiDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLITF---NALLSYFLTPLENI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 320 FN---QFQEALGASSRIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGA 395
Cdd:TIGR01193 432 INlqpKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGS 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 396 GKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYG-RPGASQAEVEAAAHAAHAH 474
Cdd:TIGR01193 512 GKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIK 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 475 EFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEalvQAALERL--MVGRTTFVVAHR 552
Cdd:TIGR01193 592 DDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQDKTIIFVAHR 668
|
490 500 510
....*....|....*....|....*....|....*...
gi 499192068 553 LSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELY 590
Cdd:TIGR01193 669 LSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
39-333 |
4.73e-81 |
|
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: 256.71 E-value: 4.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI---PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
39-333 |
6.96e-79 |
|
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: 251.19 E-value: 6.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgsTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVE---KDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18552 238 ALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
27-589 |
1.57e-77 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 256.74 E-value: 1.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 27 RLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgsTDTGPldrtvlsllgIFALSACFGAAQ--AYLL 104
Cdd:TIGR01192 9 RALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSK---SDVLP----------TLALWAGFGVFNtiAYVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 105 ARVGAGVVADLRRAL-----FSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVqavtSTALAQLASQGFTLIGSVLLLVQTS 179
Cdd:TIGR01192 76 VAREADRLAHGRRATllteaFGRIISMPLSWHQQRGTSNALHTLLRATETL----FGLWLEFMRQHLATFVALFLLIPTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 180 PRLSLlTLAIIPLVIGTA-VTIGRRIRRVSREVQDAVAAAN----GQAEEAISGVRVVQSF---TAEGLEEERYGQGVLA 251
Cdd:TIGR01192 152 FAMDW-RLSIVLMVLGILyILIAKLVMQRTKNGQAAVEHHYhnvfKHVSDSISNVSVVHSYnriEAETSALKQFTNNLLS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 252 SFRAALRrarLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASS 331
Cdd:TIGR01192 231 AQYPVLD---WWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 332 RIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVGFTYAG-APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDV 410
Cdd:TIGR01192 308 DFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANsSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 411 TAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGE 490
Cdd:TIGR01192 388 TVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 491 RGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:TIGR01192 468 RGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRL 547
|
570
....*....|....*....
gi 499192068 571 VADGTHEGLMAAGGLYREL 589
Cdd:TIGR01192 548 IEKGSFQELIQKDGRFYKL 566
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
39-333 |
3.70e-77 |
|
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: 246.58 E-value: 3.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgstdtGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG------GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18551 235 LVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
43-600 |
5.37e-77 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 255.02 E-value: 5.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDasflkvGSTDTGPLDRTVLSLLGIFALSAC-------------FGAAqaYLLArvga 109
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVD------GVTEQHMTTGQILMWIGTMVLIAVvvyllryvwrvllFGAS--YQLA---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 110 gvvADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQgfTLIGSVLLLV---QTSPRLSLLT 186
Cdd:PRK10789 69 ---VELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDS--LVMGCAVLIVmstQISWQLTLLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 187 LAIIPLVigtAVTI---GRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQ 263
Cdd:PRK10789 144 LLPMPVM---AIMIkryGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARID 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 264 ALMTGVMsFLTFGALALVLWFGGR-QVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSD 342
Cdd:PRK10789 221 ARFDPTI-YIAIGMANLLAIGGGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 343 LPGPAAPRPLSRAEGRVRFVDvgFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH 420
Cdd:PRK10789 300 VKDGSEPVPEGRGELDVNIRQ--FTYPQTdhPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 421 DVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQR 500
Cdd:PRK10789 378 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 501 QRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLM 580
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
570 580
....*....|....*....|
gi 499192068 581 AAGGLYRELYELqfrQQQEA 600
Cdd:PRK10789 538 QQSGWYRDMYRY---QQLEA 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
35-565 |
1.07e-76 |
|
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: 252.98 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 35 YRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFlkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVAD 114
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLI--SAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 115 LRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVI 194
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 195 GTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERygqgvLASFRAALRRA-----RLQALMTGV 269
Cdd:TIGR02857 159 IFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA-----IRRSSEEYRERtmrvlRIAFLSSAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 270 MSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDER-----SDLP 344
Cdd:TIGR02857 234 LELFATLSVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAprplaGKAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 345 GPAAPRPlsraegRVRFVDVGFTYAGA-PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR 423
Cdd:TIGR02857 314 VTAAPAS------SLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 424 AYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRV 503
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 504 AIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVM 565
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-593 |
7.54e-76 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 252.72 E-value: 7.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 25 LRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLL 104
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAK-GNLPLGLVAGLAAAYVGLQLLAAGLHYAQSLLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 105 ARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQ----AVTSTALAQLAsqgftLIGSVLL-LVQTS 179
Cdd:PRK10790 90 NRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRdlyvTVVATVLRSAA-----LIGAMLVaMFSLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 180 PRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRR 259
Cdd:PRK10790 165 WRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 260 ARLQA-LMTGVMSFltFGAL---ALVLWFGGRqvMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFE 335
Cdd:PRK10790 245 LRLDGfLLRPLLSL--FSALilcGLLMLFGFS--ASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 336 LLDERSDLPGPAApRPLSraEGRVRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGR 414
Cdd:PRK10790 321 LMDGPRQQYGNDD-RPLQ--SGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 415 VEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVK 494
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALeRLMVGRTTFVV-AHRLSTIRSADRILVMDAGRVVAD 573
Cdd:PRK10790 477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQ 555
|
570 580
....*....|....*....|
gi 499192068 574 GTHEGLMAAGGLYRELYELQ 593
Cdd:PRK10790 556 GTHQQLLAAQGRYWQMYQLQ 575
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
42-333 |
7.78e-76 |
|
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: 243.31 E-value: 7.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 42 GVLATLISSGLGLVFPRLFGTLIDASFLKVGSTDTGP---LDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAlraLNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
40-593 |
6.92e-73 |
|
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: 246.79 E-value: 6.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 40 VLGVLATLissgLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRAL 119
Cdd:TIGR03797 143 AMGLLGTL----LGMLVPIATGILIGTA---IPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 120 FSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQtSPRLSLLTLAIIPLVIGTAVT 199
Cdd:TIGR03797 216 WDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYY-SWKLALVAVALALVAIAVTLV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 200 IGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALA 279
Cdd:TIGR03797 295 LGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSA 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 280 LVLWFGGRQVMSGALTPGNLVTFlFYALqvGGTVAALTGVFNQFQEALGA------SSRIFELLDERSDlpGPAAPRPLS 353
Cdd:TIGR03797 375 ALFAAAISLLGGAGLSLGSFLAF-NTAF--GSFSGAVTQLSNTLISILAViplwerAKPILEALPEVDE--AKTDPGKLS 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 354 raeGRVRFVDVGFTYA--GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLR 431
Cdd:TIGR03797 450 ---GAIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQETLLFSGTVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILK 511
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERLMVGRttFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYE 591
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683
|
..
gi 499192068 592 LQ 593
Cdd:TIGR03797 684 RQ 685
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
42-333 |
5.35e-72 |
|
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: 233.18 E-value: 5.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 42 GVLATLISSGLGLVFPRLFGTLIDASFLKVGSTDTG--PLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRAL 119
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 120 FSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVT 199
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 200 IGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALA 279
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499192068 280 LVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
345-570 |
1.10e-69 |
|
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: 224.66 E-value: 1.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 345 GPAAPRPLsraEGRVRFVDVGFTYAGAPA---LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHD 421
Cdd:cd03248 1 GSLAPDHL---KGIVKFQNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 422 VRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQ 501
Cdd:cd03248 78 ISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 502 RVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
83-582 |
5.34e-68 |
|
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: 230.79 E-value: 5.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 83 VLSLL--GIFALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLtsrltSDVGTV-QAVTSTALA 159
Cdd:COG4618 61 MLTLLalGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLrQFLTGPGLF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 160 QLASQGFTLI--GSVLLLvqtSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQsftA 237
Cdd:COG4618 136 ALFDLPWAPIflAVLFLF---HPLLGLLALVGALVLVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIE---A 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 238 EGLEE---ERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLV--TFLfyalqVGGT 312
Cdd:COG4618 210 MGMLPalrRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIaaSIL-----MGRA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 313 VA---ALTGVFNQFQEALGASSRIFELLDersDLPGPAAPRPLSRAEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVV 387
Cdd:COG4618 285 LApieQAIGGWKQFVSARQAYRRLNELLA---AVPAEPERMPLPRPKGRLSVENLTVVPPGSkrPILRGVSFSLEPGEVL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 388 ALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENIlyGR-PGASQAEVEA 466
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 467 AAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL-MVGRT 545
Cdd:COG4618 440 AAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGAT 519
|
490 500 510
....*....|....*....|....*....|....*..
gi 499192068 546 TFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG4618 520 VVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
111-591 |
1.68e-67 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 229.71 E-value: 1.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 111 VVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLS------- 183
Cdd:PRK11160 91 VLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLAltlggil 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 184 LLTLAIIPLV-------IGTAVTIGRRIRRVSrevqdAVAAANGQAEEAIsgvrvvqsFTAEGLEEERYGQGVLASFRAA 256
Cdd:PRK11160 171 LLLLLLLPLLfyrlgkkPGQDLTHLRAQYRVQ-----LTEWLQGQAELTL--------FGAEDRYRQQLEQTEQQWLAAQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 257 LRRARLQALMTGVMSFLTFGALALVLWFGGrQVMSGALTPGNLV-TFLFYALQVGGTVAALTGVFNQFQEALGASSRIFE 335
Cdd:PRK11160 238 RRQANLTGLSQALMILANGLTVVLMLWLAA-GGVGGNAQPGALIaLFVFAALAAFEALMPVAGAFQHLGQVIASARRINE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 336 LLDERSDLPGPAAPRPlSRAEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAG 413
Cdd:PRK11160 317 ITEQKPEVTFPTTSTA-AADQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 414 RVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFIcELEGGYGAVVGERGV 493
Cdd:PRK11160 396 EILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVAD 573
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
490
....*....|....*...
gi 499192068 574 GTHEGLMAAGGLYRELYE 591
Cdd:PRK11160 555 GTHQELLAQQGRYYQLKQ 572
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
39-333 |
1.04e-66 |
|
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: 219.26 E-value: 1.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEY---IPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18545 79 LFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18545 159 LLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18545 239 ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
357-574 |
2.31e-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: 215.92 E-value: 2.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 357 GRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQV 434
Cdd:cd03245 1 GRIEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPR 514
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 515 ILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADG 574
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
8.91e-66 |
|
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: 217.38 E-value: 8.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLID------------ASFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLAR 106
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdvlgdkplpgllGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 107 VGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLT 186
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 187 LAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALM 266
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 267 TGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
39-333 |
2.45e-65 |
|
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: 215.71 E-value: 2.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDaSFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAID-DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18544 80 LFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18544 160 LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
39-333 |
7.69e-65 |
|
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: 214.20 E-value: 7.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDAsfLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDA--LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18541 79 LFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18541 159 RLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18541 239 LIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
39-333 |
2.55e-64 |
|
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: 213.06 E-value: 2.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV---IGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18542 158 VFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18542 238 VLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
42-333 |
2.66e-63 |
|
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: 210.09 E-value: 2.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 42 GVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFS 121
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAV---VADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 122 HLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIG 201
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 202 RRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALV 281
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 282 LWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
39-333 |
5.73e-62 |
|
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: 206.87 E-value: 5.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLID---ASFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADL 115
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDliiEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 116 RRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIG 195
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 196 TAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFtaeGLEEErygqgVLASFRA---ALRRARLQA-----LMT 267
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAF---NREEE-----AIEEFDEineELYKASFKAqfysgLLM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 268 GVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18547 233 PIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
357-575 |
2.67e-61 |
|
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: 202.34 E-value: 2.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 357 GRVRFVDVGFTYA--GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQV 434
Cdd:cd03244 1 GDIEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSGTVAENI-LYGRpgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDP 513
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 514 RILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
7.10e-61 |
|
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: 203.92 E-value: 7.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDAsfLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDL--VTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18778 79 LYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18778 159 LYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18778 239 VLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-553 |
1.05e-60 |
|
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: 210.68 E-value: 1.05e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 25 LRRLLAYARPYRLPFVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgstdtGPLDRTVLSLLGIFALSACFGAAQaYLL 104
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEM------PPVLYLSVAAVAVRAFGIGRAVFR-YLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 105 ARVGAGVV----ADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSP 180
Cdd:TIGR02868 74 RLVGHDAAlrslGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 181 RLS-------LLTLAIIPLVIGTAVTIGRRIRRVSRE--VQDAVAAANGQAEEAISGVrvVQSFTAEGLEEERygqgvlA 251
Cdd:TIGR02868 154 PAAlilaaglLLAGFVAPLVSLRAARAAEQALARLRGelAAQLTDALDGAAELVASGA--LPAALAQVEEADR------E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 252 SFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASS 331
Cdd:TIGR02868 226 LTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 332 RIFELLDERSDLPGPAAPRPLSRAEG--RVRFVDVGFTYAGAP-ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFW 408
Cdd:TIGR02868 306 RIVEVLDAAGPVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 409 DVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVV 488
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 489 GERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRL 553
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
6.61e-60 |
|
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: 201.58 E-value: 6.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLID-ASFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRR 117
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 118 ALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTA 197
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 198 VTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGA 277
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 278 LALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
39-313 |
1.28e-58 |
|
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: 197.48 E-value: 1.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDaSFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD-VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTV 313
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
363-570 |
1.41e-58 |
|
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: 193.59 E-value: 1.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQE 440
Cdd:cd03246 5 NVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSGTVAENIlygrpgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILKDPRILILDE 520
Cdd:cd03246 85 DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499192068 521 ATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
83-582 |
3.23e-58 |
|
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: 204.12 E-value: 3.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 83 VLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRffgnhRTGDLTSRLTSDVGTV-QAVTSTALAQL 161
Cdd:TIGR01842 49 TVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLR-----RGSGDGLQALRDLDQLrQFLTGPGLFAF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 162 ASQGFTLIgSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLE 241
Cdd:TIGR01842 124 FDAPWMPI-YLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 242 EERYG---QGVLASFRAALRRArlqALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTG 318
Cdd:TIGR01842 203 TKRWGrfhSKYLSAQSAASDRA---GMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 319 VFNQFQEALGASSRIFELLDErsdLPGPAAPRPLSRAEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAG 396
Cdd:TIGR01842 280 GWKQFSGARQAYKRLNELLAN---YPSRDPAMPLPEPEGHLSVENVTIVPPGGkkPTLRGISFSLQAGEALAIIGPSGSG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 397 KTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEF 476
Cdd:TIGR01842 357 KSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHEL 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 477 ICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLST 555
Cdd:TIGR01842 437 ILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSL 516
|
490 500
....*....|....*....|....*..
gi 499192068 556 IRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:TIGR01842 517 LGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
39-333 |
2.62e-54 |
|
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: 186.54 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSG---VRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
366-601 |
3.24e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 194.29 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 366 FTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTaGRVEVDGHDVRAYALADLRRQVGLVPQETLLFS 445
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 GTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSAL 525
Cdd:PRK11174 437 GTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 526 DNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYelqfRQQQEAR 601
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL----AHRQEEI 588
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-333 |
3.72e-54 |
|
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: 186.14 E-value: 3.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDAsFLKVGSTDTGP------LDRTVLSLLGIFALSACFGAAQAYLLARVGAGVV 112
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDA-FTDFGSGESSPdeflddVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 113 ADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLL-LVQtSPRLSLLTLAIIP 191
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIaFIY-SWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 192 LVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMS 271
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 272 FLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
39-333 |
8.10e-54 |
|
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: 184.99 E-value: 8.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGP---IAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALaQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGP-FLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18543 157 RFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18543 237 AAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
39-333 |
4.16e-52 |
|
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: 180.67 E-value: 4.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEG---IANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18548 158 LIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18548 238 VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
2.31e-49 |
|
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: 173.05 E-value: 2.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFLKvgsTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQ---GDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEE--AISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFG 276
Cdd:cd18550 158 RVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 277 ALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18550 238 GPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
359-582 |
1.39e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.09 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlADLRRQVGLVP 438
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENI-----LYGRPGASQAEVEAAAHAahahefICELEGGYGAVVGergvKLSGGQRQRVAIARAILKD 512
Cdd:COG1131 80 QEPALYPDlTVRENLrffarLYGLPRKEARERIDELLE------LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 513 PRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
355-571 |
3.88e-48 |
|
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: 167.20 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 355 AEGRVRFVDVGFTYAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRR 432
Cdd:cd03369 3 EHGEIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQETLLFSGTVAENI-LYGRPGASQAeveaaahaahaheficeleggYGAV-VGERGVKLSGGQRQRVAIARAIL 510
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSDEEI---------------------YGALrVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVV 571
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
359-575 |
1.36e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 163.66 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA-PALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVRAYALADLRR 432
Cdd:COG1122 1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllkP-----TSGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQ--ETLLFSGTVAENILYGrpgasqaeveaaahaahaheficeLEG-GYG------------AVVG-----ERG 492
Cdd:COG1122 76 KVGLVFQnpDDQLFAPTVEEDVAFG------------------------PENlGLPreeirerveealELVGlehlaDRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 493 V-KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVA-HRLSTI-RSADRILVMDAGR 569
Cdd:COG1122 132 PhELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGR 211
|
....*.
gi 499192068 570 VVADGT 575
Cdd:COG1122 212 IVADGT 217
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
39-325 |
1.63e-46 |
|
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: 165.70 E-value: 1.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFlkvGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLL---PSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVqavtstalAQLASQG--------FTLIGSVLLLVQTSPRLSLLTLAII 190
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI--------SELAHHGpedlfisiITIIGSFIILLTINVPLTLIVFALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 191 PLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLAsFRAALRRA-RLQALMTGV 269
Cdd:cd18549 153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAyKAMAYFFSG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 270 MSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQE 325
Cdd:cd18549 232 MNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
29-342 |
8.80e-46 |
|
Six-transmembrane helical domain 2 (TMD2) 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: 350022 [Multi-domain] Cd Length: 317 Bit Score: 164.16 E-value: 8.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 29 LAYARPYRLPFVLGVLATLISsglGLVFPR---LFGTLIDASFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLA 105
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIA---GAVFPVfaiLFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFF--GNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLS 183
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 184 LLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQ 263
Cdd:cd18578 158 LVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 264 ALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSD 342
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
43-333 |
4.16e-45 |
|
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: 161.56 E-value: 4.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLID--ASFLKVGSTDT-GPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRAL 119
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNviSRSLKETNGDFiEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 120 FSHLLSLSPRFFGNHRTGDLTSRLTSDVgtvQAVTStALAQLASQGF----TLIGSVLLLVQTSPRLSLLTLAIIPLVIG 195
Cdd:cd18574 82 FSSLLRQDIAFFDTHRTGELVNRLTADV---QEFKS-SFKQCVSQGLrsvtQTVGCVVSLYLISPKLTLLLLVIVPVVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 196 TAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYgqgvlasfRAALRRARLQALMTGV------ 269
Cdd:cd18574 158 VGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELY--------EEEVEKAAKLNEKLGLgigifq 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 270 -MSFLTFGALAL-VLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18574 230 gLSNLALNGIVLgVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
83-581 |
1.32e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 170.93 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 83 VLSLLGIFALSACFgaAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLA 162
Cdd:PLN03232 955 VYALLGFGQVAVTF--TNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 163 SQGFTLIgSVLLLVQTSPRLSLLtlAIIPLVIGTAVT------IGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFT 236
Cdd:PLN03232 1033 NQLWQLL-STFALIGTVSTISLW--AIMPLLILFYAAylyyqsTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYD 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 237 AEGLEEERYGQGVLASFRAALRRARLQAL----MTGVMSFLTfgALALVLWFGGRQVMSG-ALTPGNLVTflfYALQVgg 311
Cdd:PLN03232 1110 RMAKINGKSMDNNIRFTLANTSSNRWLTIrletLGGVMIWLT--ATFAVLRNGNAENQAGfASTMGLLLS---YTLNI-- 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 312 tVAALTGVFNQFQEA---LGASSRIFELLDERSDLPG------PAAPRPLSraeGRVRFVDVGFTYAGA--PALQDITFD 380
Cdd:PLN03232 1183 -TTLLSGVLRQASKAensLNSVERVGNYIDLPSEATAiiennrPVSGWPSR---GSIKFEDVHLRYRPGlpPVLHGLSFF 1258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 381 VPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENIlygRPGAS 460
Cdd:PLN03232 1259 VSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSE 1335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 461 QAEVEA--AAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALE 538
Cdd:PLN03232 1336 HNDADLweALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499192068 539 RLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PLN03232 1416 EEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
360-570 |
3.47e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.51 E-value: 3.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ 439
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 ETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEficelegGYGAVVGERGVK-LSGGQRQRVAIARAILKDPRILIL 518
Cdd:COG4619 82 EPALWGGTVRDNLPFPFQLRERKFDRERALELLERL-------GLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 519 DEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRV 570
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-565 |
5.01e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 169.44 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 34 PYRLPF---------VLGV--LATLISSGLGLVFPRLFGTLIDAsfLKVGSTdtgpLDRTVLSL--LGIFALSACFgaAQ 100
Cdd:PTZ00265 46 PFFLPFkclpashrkLLGVsfVCATISGGTLPFFVSVFGVIMKN--MNLGEN----VNDIIFSLvlIGIFQFILSF--IS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 101 AYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSP 180
Cdd:PTZ00265 118 SFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 181 RLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAE-------GLEEERYGQGVL-AS 252
Cdd:PTZ00265 198 RLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEktilkkfNLSEKLYSKYILkAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 253 FraalrrarLQALMTGVMSFLTFGALALVLWFGGRQVMSGA--------LTPGNLVTFLFYALQVGGTVAALTGVFNQFQ 324
Cdd:PTZ00265 278 F--------MESLHIGMINGFILASYAFGFWYGTRIIISDLsnqqpnndFHGGSVISILLGVLISMFMLTIILPNITEYM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 325 EALGASSRIFELLDERSDLPGPAAPRPLSRAEgRVRFVDVGFTY---AGAPALQDITFDVPAGQVVALVGPSGAGKTTLV 401
Cdd:PTZ00265 350 KSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 402 NLIPRFWDVTAGRVEV-DGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYG----------------RPGASQAEV 464
Cdd:PTZ00265 429 KLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 465 EAAAHAAHAHE-----------------------------------------FICELEGGYGAVVGERGVKLSGGQRQRV 503
Cdd:PTZ00265 509 NKRNSCRAKCAgdlndmsnttdsneliemrknyqtikdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRI 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 504 AIARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRSADRILVM 565
Cdd:PTZ00265 589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-592 |
8.01e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 168.67 E-value: 8.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 18 RQRDPRQLRRLLAYARPYRLPFVLGVLATLISSGL----GLVFPRLFGTLIDASFLKVGStdtgplDRTVLSLLGIFALS 93
Cdd:PTZ00265 806 KPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLypvfALLYAKYVSTLFDFANLEANS------NKYSLYILVIAIAM 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 94 ACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGN--HRTGDLTSRLTSDVGTVQavtsTALAQlasqGFTLIGS 171
Cdd:PTZ00265 880 FISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLK----TGLVN----NIVIFTH 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 172 VLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRV------SREVQDAVAAANGQA-----------------EEAISG 228
Cdd:PTZ00265 952 FIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIrarltaNKDVEKKEINQPGTVfaynsddeifkdpsfliQEAFYN 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 229 VRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQ 308
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLF 1111
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 309 VGGTVAALTGVFNQFQEALGASSRIFELLDERSDLP----GPAAPRPLSRAEGRVRFVDVGFTYAGAPAL---QDITFDV 381
Cdd:PTZ00265 1112 TGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDvrdnGGIRIKNKNDIKGKIEIMDVNFRYISRPNVpiyKDLTFSC 1191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 382 PAGQVVALVGPSGAGKTTLVNLIPRFWDV--------------------------------------------------- 410
Cdd:PTZ00265 1192 DSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedst 1271
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 411 ---TAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAV 487
Cdd:PTZ00265 1272 vfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTN 1351
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 488 VGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRSADRILVM 565
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1431
|
650 660 670
....*....|....*....|....*....|...
gi 499192068 566 D-----AGRVVADGTHEGLMAA-GGLYRELYEL 592
Cdd:PTZ00265 1432 NnpdrtGSFVQAHGTHEELLSVqDGVYKKYVKL 1464
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
360-569 |
8.80e-44 |
|
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: 153.55 E-value: 8.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ 439
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 etllfsgtvaenilygrpgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILKDPRILILD 519
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 520 EATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTI-RSADRILVMDAGR 569
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
358-595 |
5.55e-43 |
|
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: 154.43 E-value: 5.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLL-FSGTVAENILYGR-PGASQAEVEAAAHAAHAHEFICELEGGYGAvvgERGV-KLSGGQRQRVAIARAILKDPR 514
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyPHLGLFGRPSAEDREAVEEALERTGLEHLA---DRPVdELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 515 ILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAGGLyRELYE 591
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLTPELL-EEVYG 236
|
....
gi 499192068 592 LQFR 595
Cdd:COG1120 237 VEAR 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
363-570 |
1.37e-42 |
|
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: 150.63 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlADLRRQVGLVPQETL 442
Cdd:cd03230 5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAENIlygrpgasqaeveaaahaahaheficeleggygavvgergvKLSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:cd03230 84 LYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499192068 522 TSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRV 570
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
359-579 |
1.61e-42 |
|
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: 152.33 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDV-----TAGRVEVDGHDVRA--YALADLR 431
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQETLLFSGTVAENILYG-RPGASQAEVEAAAHAAHAheficeLEG-GYGAVVGER--GVKLSGGQRQRVAIAR 507
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlRLHGIKLKEELDERVEEA------LRKaALWDEVKDRlhALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGL 579
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
4.65e-42 |
|
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: 153.88 E-value: 4.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASFLKVGSTDTGPLDR------------TVLSLLGIFALSACFGAAQAYLLAR 106
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPASlgpadprgqlwlLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 107 VGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLT 186
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 187 LAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALM 266
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 267 TGVMSFLTFGALALVLWFGGRQVMSG------ALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
359-569 |
6.23e-41 |
|
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: 146.56 E-value: 6.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA--LADLRRQVGL 436
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSG-TVAENILYGrpgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILKDPRI 515
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 516 LILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLS-TIRSADRILVMDAGR 569
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
359-590 |
7.88e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 148.67 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA-PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV 434
Cdd:COG3638 3 LELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAheficELEGGYGAV--VG------ERGVKLSGGQRQRVAI 505
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVLAGRLGRTSTWRSLLGLFPPE-----DRERALEALerVGladkayQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDNES-----EALVQAALERlmvGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGL 579
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARED---GITVVVNLHQVDLARRyADRIIGLRDGRVVFDGPPAEL 234
|
250
....*....|.
gi 499192068 580 MAAggLYRELY 590
Cdd:COG3638 235 TDA--VLREIY 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
359-570 |
1.46e-40 |
|
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: 146.87 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLR 431
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 R-QVGLVPQETLLFSG-TVAENI-----LYGRPGASQAEVEAAAhaahaheficeLEG-GYGAVVGERGVKLSGGQRQRV 503
Cdd:cd03255 81 RrHIGFVFQSFNLLPDlTALENVelpllLAGVPKKERRERAEEL-----------LERvGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 504 AIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
363-600 |
1.70e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 147.31 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAdLRRQVGLVPQETL 442
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAENI-----LYGRPGASQAEVEAAAHAAHaheficELEGgygavVGERGV-KLSGGQRQRVAIARAILKDPRI 515
Cdd:COG4555 85 LYDRlTVRENIryfaeLYGLFDEELKKRIEELIELL------GLEE-----FLDRRVgELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 516 LILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAAGG---LYRELY 590
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGeenLEDAFV 233
|
250
....*....|
gi 499192068 591 ELQFRQQQEA 600
Cdd:COG4555 234 ALIGSEEGEA 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
359-573 |
1.87e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY----AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVRAY---A 426
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrP-----TSGEVLIDGQDISSLserE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 427 LADLRRQ-VGLVPQETLLFSG-TVAENI----LYGRPGASQAEVEAAAHaahaheficeLEG-GYGAVVGERGVKLSGGQ 499
Cdd:COG1136 80 LARLRRRhIGFVFQFFNLLPElTALENValplLLAGVSRKERRERAREL----------LERvGLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 500 RQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRSADRILVMDAGRVVAD 573
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
359-569 |
2.05e-40 |
|
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: 146.08 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-----AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdvrayaladlrrq 433
Cdd:cd03250 1 ISVEDASFTWdsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 434 VGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHaahahefiCELE-------GGYGAVVGERGVKLSGGQRQRVAIA 506
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKA--------CALEpdleilpDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 507 RAILKDPRILILDEATSALDNESEALV--QAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGR 569
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
39-333 |
2.21e-40 |
|
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: 148.75 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDaSFLKVGSTDTgpLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILID-DIIPSGDINL--LNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLtSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18570 160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTflFYALQV--GGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIA--FNALLGyfLGPIENLINLQPKIQEAKVAADRL 294
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
82-586 |
2.61e-40 |
|
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: 158.19 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 82 TVLSLLGIFALSACFGAAQAYLLARVGAGVVadLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQL 161
Cdd:TIGR00957 1009 SVYGALGILQGFAVFGYSMAVSIGGIQASRV--LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMF 1086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 162 ASQGFTLIGSVLLLVQTSPrlsLLTLAIIPL------VIGTAVTIGRRIRRVSREVQDAVAAangQAEEAISGVRVVQSF 235
Cdd:TIGR00957 1087 MGSLFNVIGALIVILLATP---IAAVIIPPLgllyffVQRFYVASSRQLKRLESVSRSPVYS---HFNETLLGVSVIRAF 1160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 236 TaeglEEERY----------GQGVLASFRAALRRARLQALMTGVMSFLtFGALALVLwfgGRQvmsgALTPGNLVTFLFY 305
Cdd:TIGR00957 1161 E----EQERFihqsdlkvdeNQKAYYPSIVANRWLAVRLECVGNCIVL-FAALFAVI---SRH----SLSAGLVGLSVSY 1228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 306 ALQVGGTVAALTGVFNQFQEALGASSRIFELLDERSDLP----GPAAPRPLSRAeGRVRFVDVGFTYAGAP--ALQDITF 379
Cdd:TIGR00957 1229 SLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiqETAPPSGWPPR-GRVEFRNYCLRYREDLdlVLRHINV 1307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 380 DVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAENI-LYGRpg 458
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ-- 1385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 459 ASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALE 538
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499192068 539 RLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLY 586
Cdd:TIGR00957 1466 TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
360-569 |
4.14e-40 |
|
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: 145.30 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQ--ETLLFSGTVAENILYGrPGASQAEVEAAAHAAHAHEFICELEGgygavVGERGV-KLSGGQRQRVAIARAILKDPR 514
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFG-LENLGLPEEEIEERVEEALELVGLEG-----LRDRSPfTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 515 ILILDEATSALDNESEALVQAALERLMVGRTTFVVA-HRLSTIRS-ADRILVMDAGR 569
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
359-582 |
6.11e-40 |
|
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: 145.80 E-value: 6.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG----APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLR 431
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQE-TLLFSGTVAENILY-----GRPGASQAEVEAAAHAahahefICELEGGYGAVVGErgvkLSGGQRQRVAI 505
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVALpleiaGVPKAEIEERVLELLE------LVGLEDKADAYPAQ----LSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDNESealVQAALERLM-----VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGL 579
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPET---TQSILALLRdinreLGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 499192068 580 MAA 582
Cdd:cd03258 229 FAN 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
359-574 |
1.76e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.04 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV 434
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQET-LLFSGTVAENILY-----GRPGASqaeveaaahAAHAHEFICE---LEGGYGAVVGErgvkLSGGQRQRVAI 505
Cdd:COG2884 82 GVVFQDFrLLPDRTVYENVALplrvtGKSRKE---------IRRRVREVLDlvgLSDKAKALPHE----LSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 506 ARAILKDPRILILDEATSALDNESEALVQAALERL-MVGrTTFVVA-HRLSTIRSAD-RILVMDAGRVVADG 574
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRG-TTVLIAtHDLELVDRMPkRVLELEDGRLVRDE 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
359-574 |
2.22e-39 |
|
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: 143.43 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVraYALADLRRQVGLVP 438
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYGrPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRILI 517
Cdd:cd03259 79 QDYALFPHlTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADG 574
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-333 |
2.55e-39 |
|
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: 145.70 E-value: 2.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDaSFLKVGSTDTgpldrtvlsLLGIFALSACFGAAQA-------YLLARVGAGV 111
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAID-HFITPGTLDG---------LTGFILLYLGLILIQAlsvflfiRLAGKIEMGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 112 VADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIP 191
Cdd:cd18540 74 SYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 192 LVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMS 271
Cdd:cd18540 154 VLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 272 FLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18540 234 FLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
374-523 |
6.00e-39 |
|
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: 140.09 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSG-TVAENI 452
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 453 LYGRPGASQAEVEAAAHAAHAHEFIcELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
328-582 |
6.03e-39 |
|
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: 150.05 E-value: 6.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 328 GASSRIFELLDERSDLPGPAAPRPLSRAEGR-----VRFVDVGFTYAGA-----PALQDITFDVPAGQVVALVGPSGAGK 397
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAAAaaeplLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 398 TTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQVGLVPQ--ETLLFSG-TVAENI-----LYGRPGASQAEVEA 466
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQdpYSSLNPRmTVGDIIaeplrLHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 467 AAHAAHahefiCELEGGYGavvGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMV---- 542
Cdd:COG1123 385 AELLER-----VGLPPDLA---DRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRdlqr 452
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499192068 543 --GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG1123 453 elGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
372-574 |
1.15e-38 |
|
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: 141.87 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQVGLVPQE---TLLFS 445
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRRKEIQMVFQDpmsSLNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 GTVAENILygRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSAL 525
Cdd:cd03257 99 MTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 526 DneseALVQAALERLMV------GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03257 177 D----VSVQAQILDLLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
359-582 |
1.52e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.04 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQVG 435
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENILYG---RPGASQAEveaaahaahahefICELEGGYGAVVGERGVK------LSGGQRQRVAI 505
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPlreHTDLSEAE-------------IRELVLEKLELVGLPGAAdkmpseLSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDNESealvQAALERLMV------GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEG 578
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPIT----SAVIDELIRelrdelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
....
gi 499192068 579 LMAA 582
Cdd:COG1127 229 LLAS 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
359-575 |
3.41e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayalADL---RRQVG 435
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENILYG----RPGASQAEVEAAAHAAhahefICELEGgygavVGERGVK-LSGGQRQRVAIARAI 509
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGlrmrGVPKAEIRARVAELLE-----LVGLEG-----LADRYPHqLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 510 LKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLS---TIrsADRILVMDAGRVVADGT 575
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
363-574 |
5.12e-38 |
|
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: 138.72 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ--E 440
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQalE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLlfsgtvaeNILYgrpgasqaeveaaahaahaheficeleggygavVGERGVK-LSGGQRQRVAIARAILKDPRILILD 519
Cdd:cd03214 84 LL--------GLAH---------------------------------LADRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 520 EATSALD--NESEALVQAALERLMVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADG 574
Cdd:cd03214 123 EPTSHLDiaHQIELLELLRRLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
115-333 |
1.01e-37 |
|
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: 141.29 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 115 LRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVI 194
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 195 GTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLT 274
Cdd:cd18784 151 IVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTE 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 275 FGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18784 231 LALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
359-575 |
1.48e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.36 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV--RAYALADLRRQVGL 436
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSG-TVAENILY------GRPGAsqaeveaaahaahaheficELEggygavvgERGVK--------------- 494
Cdd:COG1126 82 VFQQFNLFPHlTVLENVTLapikvkKMSKA-------------------EAE--------ERAMEllervgladkadayp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 --LSGGQRQRVAIARAILKDPRILILDEATSALDNEseaLVQAALErLMV-----GRTTFVVAHRLSTIRS-ADRILVMD 566
Cdd:COG1126 135 aqLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMGFAREvADRVVFMD 210
|
....*....
gi 499192068 567 AGRVVADGT 575
Cdd:COG1126 211 GGRIVEEGP 219
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
130-584 |
2.12e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 149.12 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 130 FFGNHRTGDLTSRLTSDVGTVQ---AVTS----TALAQLASQgFTLIGSVlllvqtsprlSLLTL-AIIPLVIGTAV--- 198
Cdd:PLN03130 1003 FFHTNPLGRIINRFAKDLGDIDrnvAVFVnmflGQIFQLLST-FVLIGIV----------STISLwAIMPLLVLFYGayl 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 ---TIGRRIRRVSREVQDAVAAangQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRR--------ARLQALmT 267
Cdd:PLN03130 1072 yyqSTAREVKRLDSITRSPVYA---QFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNmssnrwlaIRLETL-G 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 268 GVMSFLTfGALALVLWFGGRQVMSGALTPGNLvtfLFYALQVGGTvaaLTGVFNQFQEA---LGASSRIFELLDERSDLP 344
Cdd:PLN03130 1148 GLMIWLT-ASFAVMQNGRAENQAAFASTMGLL---LSYALNITSL---LTAVLRLASLAensLNAVERVGTYIDLPSEAP 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 345 GPAA---PRPLSRAEGRVRFVDVGFTYAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG 419
Cdd:PLN03130 1221 LVIEnnrPPPGWPSSGSIKFEDVVLRYRPelPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 420 HDVRAYALADLRRQVGLVPQETLLFSGTVAENiLYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQ 499
Cdd:PLN03130 1301 CDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-LDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQ 1379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 500 RQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGL 579
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
....*
gi 499192068 580 MAAGG 584
Cdd:PLN03130 1460 LSNEG 1464
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
359-581 |
2.72e-37 |
|
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: 138.59 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG-APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSG-TVAENI-----LYGRPGAsQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILK 511
Cdd:cd03295 81 IQQIGLFPHmTVEENIalvpkLLKWPKE-KIRERADELLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRL-STIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
359-574 |
3.65e-37 |
|
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: 136.29 E-value: 3.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlADLRRQVGL 436
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSGTVAENIlygrpgasqaeveaaahaahaheficeleggygavvgerGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 517 ILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADG 574
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
359-573 |
5.07e-37 |
|
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: 137.22 E-value: 5.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhdvraYALADLRRQV 434
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFS-GTVAENILYgrpGASQAEVEAAAHAAHAHEFI--CELEGGYGAVVGErgvkLSGGQRQRVAIARAILK 511
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVAL---GLELQGVPKAEARERAEELLelVGLSGFENAYPHQ----LSGGMRQRVALARALAV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 512 DPRILILDEATSALDneseALVQAALERLMV------GRTTFVVAHRLS-TIRSADRILVMDA--GRVVAD 573
Cdd:cd03293 149 DPDVLLLDEPFSALD----ALTREQLQEELLdiwretGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
359-581 |
5.21e-37 |
|
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: 137.63 E-value: 5.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADL---RRQVG 435
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENI---LYGRPGASQAEveaaahaahahefICELEGGYGAVVGERGVK------LSGGQRQRVAI 505
Cdd:cd03261 81 MLFQSGALFDSlTVFENVafpLREHTRLSEEE-------------IREIVLEKLEAVGLRGAEdlypaeLSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 506 ARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
358-582 |
1.01e-36 |
|
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: 137.24 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGF--TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVG 435
Cdd:COG1124 3 EVRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQE---------TLLfsGTVAENI-LYGRPGASQAEVEaaahaahahefICELEGGYGAVVGERGVKLSGGQRQRVAI 505
Cdd:COG1124 83 MVFQDpyaslhprhTVD--RILAEPLrIHGLPDREERIAE-----------LLEQVGLPPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDneseALVQAA----LERLMV--GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEG 578
Cdd:COG1124 150 ARALILEPELLLLDEPTSALD----VSVQAEilnlLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
....
gi 499192068 579 LMAA 582
Cdd:COG1124 226 LLAG 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
359-600 |
1.33e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyaladLRRQVGLVP 438
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLL---FSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICE---LEGGYGAVVGErgvkLSGGQRQRVAIARAILKD 512
Cdd:COG1121 82 QRAEVdwdFPITVRDVVLMGRYGRRGLFRRPSRADREAVDEALErvgLEDLADRPIGE----LSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 513 PRILILDEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTIRS-ADRILVMDaGRVVADGTHEGLMAAGGLyRELY 590
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLN-RGLVAHGPPEEVLTPENL-SRAY 235
|
250
....*....|
gi 499192068 591 ELQFRQQQEA 600
Cdd:COG1121 236 GGPVALLAHG 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
358-582 |
1.43e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 143.12 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTL----VNLIPRFWDVTaGRVEVDGHDVRAYALADLRRQ 433
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLalalMGLLPHGGRIS-GEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 434 VGLVPQE--TLLFSGTVAENILYG--RPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAI 509
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 510 LKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
106-591 |
3.16e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 145.50 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVtSTALAQLASQGFTLIGSVLLLVQTSPRLSLL 185
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQI-AEQLHGLWSAPFRIIVSMVLLYQQLGVASLF 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 186 TLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYgQGVLASFRAALRRARLqal 265
Cdd:PLN03232 446 GSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRI-QGIRNEELSWFRKAQL--- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 266 MTGVMSFL--TFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFELL--DERS 341
Cdd:PLN03232 522 LSAFNSFIlnSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLlsEERI 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 342 DLPGPaaprPLSRAEGRVRFVDVGFTY---AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVnliprfwdvTAGRVEVD 418
Cdd:PLN03232 602 LAQNP----PLQPGAPAISIKNGYFSWdskTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLI---------SAMLGELS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 419 GHDVrayALADLRRQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFicELEGGYGAV-VGERGVKLSG 497
Cdd:PLN03232 669 HAET---SSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDL--DLLPGRDLTeIGERGVNISG 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 498 GQRQRVAIARAILKDPRILILDEATSALDNE-SEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTH 576
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTF 823
|
490
....*....|....*
gi 499192068 577 EGLMAAGGLYRELYE 591
Cdd:PLN03232 824 AELSKSGSLFKKLME 838
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-575 |
3.45e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.29 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLR 431
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQE-TLLFSGTVAENILY-----GRPGASQAEVEAaahaahaheficELEggygAVVG--ERG----VKLSGGQ 499
Cdd:COG1135 82 RKIGMIFQHfNLLSSRTVAENVALpleiaGVPKAEIRKRVA------------ELL----ELVGlsDKAdaypSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 500 RQRVAIARAILKDPRILILDEATSALDNESE----ALVQAALERLmvGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
.
gi 499192068 575 T 575
Cdd:COG1135 224 P 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
353-573 |
7.42e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.22 E-value: 7.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 353 SRAEGRVRFVDVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyala 428
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 429 dLRRQVGLVPQETLLFS-GTVAENILYGRPGASQAEVEAAAHAAHaheficeleggYGAVVGERGVK------LSGGQRQ 501
Cdd:COG1116 78 -PGPDRGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARE-----------LLELVGLAGFEdayphqLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 502 RVAIARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAH------RLstirsADRILVMDA--GRVV 571
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
|
..
gi 499192068 572 AD 573
Cdd:COG1116 221 EE 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
360-575 |
2.31e-35 |
|
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: 133.08 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQVG 435
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQE-TLLFSGTVAENILYGRPGASQAEVEAAAHAAHAheficELEGGYGAV--VG------ERGVKLSGGQRQRVAIA 506
Cdd:cd03256 82 MIFQQfNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKE-----EKQRALAALerVGlldkayQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 507 RAILKDPRILILDEATSALDNES-----EALVQAALERlmvGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASsrqvmDLLKRINREE---GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
358-581 |
2.89e-35 |
|
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: 132.17 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGftYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAD-LRRQVGL 436
Cdd:cd03224 2 EVENLNAG--YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSG-TVAENILYGRpgasqaEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGA------YARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 516 LILDEATSALdneSEALVQ---AALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:cd03224 154 LLLDEPSEGL---APKIVEeifEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
363-574 |
1.39e-34 |
|
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: 130.35 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRayalaDLRRQVGLVPQETL 442
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 L---FSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGavVGERGV-KLSGGQRQRVAIARAILKDPRILIL 518
Cdd:cd03235 79 IdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSE--LADRQIgELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 519 DEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTI-RSADRILVMDaGRVVADG 574
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLN-RTVVASG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
363-575 |
1.73e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 133.73 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVRAyALADLRRQVGLV 437
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletP-----DSGRIVLNGRDLFT-NLPPRERRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSG-TVAENILYG---RPgASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDP 513
Cdd:COG1118 81 FQHYALFPHmTVAENIAFGlrvRP-PSKAEIRARVEELLELVQLEGLADRYPS-------QLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 514 RILILDEATSALDneseALVQAALERLM------VGRTTFVVAH-RLSTIRSADRILVMDAGRVVADGT 575
Cdd:COG1118 153 EVLLLDEPFGALD----AKVRKELRRWLrrlhdeLGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
359-575 |
1.74e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 131.78 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVR-AYALADL 430
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnglllP-----TSGKVTVDGLDTLdEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 431 RRQVGLVPQ--ETLLFSGTVAENILYGrpgasqaeveaaahaahaheficeLEggygavvgERGV--------------- 493
Cdd:TIGR04520 76 RKKVGMVFQnpDNQFVGATVEDDVAFG------------------------LE--------NLGVpreemrkrvdealkl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 ------------KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRSA 559
Cdd:TIGR04520 124 vgmedfrdrephLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLA 203
|
250
....*....|....*.
gi 499192068 560 DRILVMDAGRVVADGT 575
Cdd:TIGR04520 204 DRVIVMNKGKIVAEGT 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
368-570 |
4.59e-34 |
|
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: 128.80 E-value: 4.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV--RAYALADLRRQVGLVPQETLLFS 445
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 G-TVAENILYG---RPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:cd03262 90 HlTVLENITLApikVKGMSKAEAEERALELLEKVGLADKADAYPA-------QLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 522 TSALDNEseaLVQAALErLMV-----GRTTFVVAHRLSTIRS-ADRILVMDAGRV 570
Cdd:cd03262 163 TSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
359-575 |
4.67e-34 |
|
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: 129.28 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVraYALADLRRQVGLVP 438
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYG--RPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRI 515
Cdd:cd03300 79 QNYALFPHlTVFENIAFGlrLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 516 LILDEATSALDNESEALVQAALERL--MVGrTTFV-VAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLqkELG-ITFVfVTHDQEEALTmSDRIAVMNKGKIQQIGT 214
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
43-333 |
7.79e-34 |
|
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: 130.76 E-value: 7.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASfLKVGSTDTgpLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18568 8 LLASLLLQLLGLALPLFTQIILDRV-LVHKNISL--LNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALaQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGR 202
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSAL-TTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 203 RIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLE----EERYGQGVLASFRAALRRARLQaLMTGVMSFLTfgaL 278
Cdd:cd18568 164 KLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIrwrwENKFAKALNTRFRGQKLSIVLQ-LISSLINHLG---T 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18568 240 IAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
358-581 |
1.94e-33 |
|
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: 127.79 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGftYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALAdlRRQV 434
Cdd:COG0410 5 EVENLHAG--YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglPPHRIA--RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSG-TVAENIL---YGRPGASQAEVEaaahaahaheficeLEGGYGA--VVGER----GVKLSGGQRQRVA 504
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDRAEVRAD--------------LERVYELfpRLKERrrqrAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 505 IARAILKDPRILILDEATSALdneSEALVQ---AALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGL 579
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNrEGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAEL 223
|
..
gi 499192068 580 MA 581
Cdd:COG0410 224 LA 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
106-591 |
4.67e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 136.02 E-value: 4.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 106 RVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTaLAQLASQGFTLIGSVLLLVQTSPRLSLL 185
Cdd:PLN03130 367 RVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQ-LHTLWSAPFRIIIAMVLLYQQLGVASLI 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 186 TLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYgQGV----LASFRAAlrrar 261
Cdd:PLN03130 446 GSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKV-QTVrddeLSWFRKA----- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 262 lqALMTGVMSFL--TFGALALVLWFGGRQVMSGALTPGNLVTFL--FYALQVggTVAALTGVFNQFQEALGASSRIFELL 337
Cdd:PLN03130 520 --QLLSAFNSFIlnSIPVLVTVVSFGVFTLLGGDLTPARAFTSLslFAVLRF--PLFMLPNLITQAVNANVSLKRLEELL 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 338 --DERSDLPGPaaprPLSRAEGRVRFVDVGFTY---AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPRf 407
Cdd:PLN03130 596 laEERVLLPNP----PLEPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISamlgeLPPR- 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 408 wdvtagrveVDGHDVrayaladLRRQVGLVPQETLLFSGTVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAV 487
Cdd:PLN03130 671 ---------SDASVV-------IRGTVAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 488 VGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNE-SEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMD 566
Cdd:PLN03130 734 IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVH 813
|
490 500
....*....|....*....|....*
gi 499192068 567 AGRVVADGTHEGLMAAGGLYRELYE 591
Cdd:PLN03130 814 EGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
368-575 |
1.06e-32 |
|
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: 125.63 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALAdlRRQVGLVPQETLLF 444
Cdd:cd03219 10 FGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPHEIA--RLGIGRTFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SG-TVAENILYGRPGASQAEVEAAAHAAHAHEF---------ICELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPR 514
Cdd:cd03219 88 PElTVLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 515 ILILDEATSALdNESEALVQAALERLMV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:cd03219 164 LLLLDEPAAGL-NPEETEELAELIRELRerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
359-575 |
1.15e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 125.87 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV 434
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQE-TLLFSGTVAENILYGRPGAS---QAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAIL 510
Cdd:TIGR02315 82 GMIFQHyNLIERLTVLENVLHGRLGYKptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGA 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
376-581 |
1.44e-32 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 128.68 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH----DVRAYALADLRRQVGLVPQETLLFSG-TVAE 450
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPGASQAEVEAAAHAahahefICELEGgYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESE 530
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDE------VVELLG-IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 531 ALVQAALERLmvgRTTF-----VVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMA 581
Cdd:COG4148 170 AEILPYLERL---RDELdipilYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
373-575 |
1.57e-32 |
|
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: 125.92 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLrrqvGLVP--QETLLFSG- 446
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHRIARL----GIARtfQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENILYGRPGASQAEVEAAAHAAHAHEF--------------ICELEGGYGAVVGErgvkLSGGQRQRVAIARAILKD 512
Cdd:COG0411 95 TVLENVLVAAHARLGRGLLAALLRLPRARReereareraeelleRVGLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 513 PRILILDEATSAL-DNESEALVQaALERL--MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELAE-LIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
363-574 |
6.15e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.99 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDV-----TAGRVEVDGHDVRA--YALADLRRQVG 435
Cdd:COG1117 16 NLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYDpdVDVVELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSGTVAENILYG------RPGAsqaeveaaahaahaheficELEggygAVV-----------------GERG 492
Cdd:COG1117 96 MVFQKPNPFPKSIYDNVAYGlrlhgiKSKS-------------------ELD----EIVeeslrkaalwdevkdrlKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 493 VKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEalvqAALERLMV---GRTTFV-VAHRLS-TIRSADRILVMDA 567
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIST----AKIEELILelkKDYTIViVTHNMQqAARVSDYTAFFYL 228
|
....*..
gi 499192068 568 GRVVADG 574
Cdd:COG1117 229 GELVEFG 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
359-575 |
1.12e-31 |
|
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: 122.83 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADlrRQVGLVP 438
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYG---RPGASQAEVEAAAHAAHAHEFICELEGgygavVGER-GVKLSGGQRQRVAIARAILKDP 513
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGlrvKPRSERPPEAEIRAKVHELLKLVQLDW-----LADRyPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 514 RILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGT 575
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
376-574 |
1.57e-31 |
|
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: 121.63 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPaGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG---HDVR-AYALADLRRQVGLVPQETLLFSG-TVAE 450
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRILILDEATSALDNESE 530
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499192068 531 ALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADG 574
Cdd:cd03297 168 LQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
357-575 |
6.86e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 123.64 E-value: 6.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 357 GRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayalADL---RRQ 433
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLppkDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 434 VGLVPQETLLF-SGTVAENILYGrpgasqaeveaaahaahahefiCELEGGYGAVVGERgVK------------------ 494
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFP----------------------LKLRKVPKAEIDRR-VReaaellgledlldrkpkq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKDPRILILDEATSALD----NESEALVQAALERLmvgRTTFV-VAHRLS---TIrsADRILVMD 566
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIyVTHDQVeamTL--ADRIAVMN 208
|
....*....
gi 499192068 567 AGRVVADGT 575
Cdd:COG3839 209 DGRIQQVGT 217
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
39-333 |
1.37e-30 |
|
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: 121.46 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNV---IVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLTSDVgTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNV-YIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSR-EVQDAVAAANGQAEeAISGVRVVQSFtaeGLEEERYGQ------GVLASFRaalRRARLQALMTGVMS 271
Cdd:cd18555 160 LTRKKIKKLNQeEIVAQTKVQSYLTE-TLYGIETIKSL---GSEKNIYKKwenlfkKQLKAFK---KKERLSNILNSISS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 272 FLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18555 233 SIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
115-333 |
1.53e-30 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 121.29 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 115 LRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTV-QAVTSTALAQLASQGFTLiGSVLLLVQTSPRLSLLTLAIIPLV 193
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMsRSVALNANVLLRSLVKTL-GMLGFMLSLSWQLTLLTLIEMPLT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 194 IGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFL 273
Cdd:cd18590 150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 274 TFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18590 230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-580 |
1.72e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAD--LRRQVGL 436
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSGTVA-ENILYGrP----GASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILK 511
Cdd:PRK09493 82 VFQQFYLFPHLTAlENVMFG-PlrvrGASKEEAEKQARELLAKVGLAERAHHYPS-------ELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLM 580
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEeGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
359-575 |
1.86e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 122.22 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLR 431
Cdd:PRK11153 2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQE-TLLFSGTVAENIlygrpgasqaeveaaahaahahEFICELEGGYGAVVGER--------GV--------- 493
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNV----------------------ALPLELAGTPKAEIKARvtellelvGLsdkadrypa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAAL----ERLmvGRTTFVVAHRLSTIRS-ADRILVMDAG 568
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdinREL--GLTIVLITHEMDVVKRiCDRVAVIDAG 217
|
....*..
gi 499192068 569 RVVADGT 575
Cdd:PRK11153 218 RLVEQGT 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
43-326 |
2.21e-30 |
|
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: 120.78 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18782 8 LALSFVVQLLGLANPLLFQVIIDKV---LVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLtSDVGTVQA-VTSTALAQLASQGFTLIGSVLLLVqTSPRLSLLTLAIIPLVIGTAVTIG 201
Cdd:cd18782 85 LLRLPLGFFDKRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIYIAVLFS-YSPLLTLVVLATVPLQLLLTFLFG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 202 RRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLE----EERYGQGVLASFRAALrrarLQALMTGVMSFLTFGA 277
Cdd:cd18782 163 PILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKArwrwQNRYARSLGEGFKLTV----LGTTSGSLSQFLNKLS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499192068 278 LALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEA 326
Cdd:cd18782 239 SLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQEL 287
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
376-585 |
4.34e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 121.37 E-value: 4.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG---HDVRAYA-LADLRRQVGLVPQETLLFSG-TVAE 450
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIfLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPGASQAEVEAAAHAahahefICELEGgYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESE 530
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFER------VIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 531 ALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAAGGL 585
Cdd:TIGR02142 168 YEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
363-571 |
6.02e-30 |
|
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: 116.97 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAP-ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayALADLRRQVGLVPQET 441
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 --LLFSGTVAENILYGRPGASQAEVEAAAhaahahefICELEGGYGAVvgERG-VKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAGNEQAET--------VLKDLDLYALK--ERHpLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 519 DEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTI-RSADRILVMDAGRVV 571
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
43-333 |
9.74e-30 |
|
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: 119.14 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDasflKV---GSTDTgpLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRAL 119
Cdd:cd18588 8 LLASLFLQLFALVTPLFFQVIID----KVlvhRSLST--LDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 120 FSHLLSLSPRFFGNHRTGDLTSRLtSDVGTV-QAVTSTALAQLASQGFTLIGSVLLLVqTSPRLSLLTLAIIPLVIGTAV 198
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVARV-RELESIrQFLTGSALTLVLDLVFSVVFLAVMFY-YSPTLTLIVLASLPLYALLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 199 TIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYgQGVLASF-RAALRRARLQALMTGVMSFLTFGA 277
Cdd:cd18588 160 LVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRW-EELLARYvKASFKTANLSNLASQIVQLIQKLT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 278 LALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
361-574 |
1.14e-29 |
|
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: 115.73 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 361 FVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGR---------VEVDGHDVRAYALadlR 431
Cdd:cd03213 12 TVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRrtglgvsgeVLINGRPLDKRSF---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQETLLFSG-TVAENILygrpgasqaeveaaahaahaheFICELEGgygavvgergvkLSGGQRQRVAIARAIL 510
Cdd:cd03213 82 KIIGYVPQDDILHPTlTVRETLM----------------------FAAKLRG------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLST--IRSADRILVMDAGRVVADG 574
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-573 |
1.63e-29 |
|
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: 114.45 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQ-VGLV 437
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQetllfsgtvaenilygrpgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILKDPRILI 517
Cdd:cd03216 81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 518 LDEATSAL-DNESEALVqAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVAD 573
Cdd:cd03216 106 LDEPTAALtPAEVERLF-KVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
363-575 |
1.96e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 117.14 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL 442
Cdd:COG4559 6 NLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 L-FSGTVAENILYGR-PGASQAEVEAAAHAAHAHEfiCELEGgygavVGERGVK-LSGGQRQRVAIARAIL-------KD 512
Cdd:COG4559 86 LaFPFTVEEVVALGRaPHGSSAAQDRQIVREALAL--VGLAH-----LAGRSYQtLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 513 PRILILDEATSALD-----NESEALVQAALERLMVgrttFVVAHRLS-TIRSADRILVMDAGRVVADGT 575
Cdd:COG4559 159 PRWLFLDEPTSALDlahqhAVLRLARQLARRGGGV----VAVLHDLNlAAQYADRILLLHQGRLVAQGT 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
359-570 |
2.45e-29 |
|
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: 115.58 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV 434
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSG-TVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDP 513
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 514 RILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTI--RSADRILVMDAGRV 570
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
360-581 |
2.76e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYAGAPAlqDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADlrRQVGLVPQ 439
Cdd:COG3840 3 RLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 ETLLFSG-TVAENILYG-----RPGASQAEVEAAAHAAHaheficelegGYGAVVGERGVKLSGGQRQRVAIARAILKDP 513
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGlrpglKLTAEQRAQVEQALERV----------GLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 514 RILILDEATSALD----NESEALV-QAALERlmvGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:COG3840 149 PILLLDEPFSALDpalrQEMLDLVdELCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
372-575 |
2.82e-29 |
|
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: 115.68 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRaYALADLRRQVGLVPQETLLFSG-TVAE 450
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NI-----LYGRPGASQAEVEAAAHAahahefICELEGgygavVGERGVK-LSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:cd03263 95 HLrfyarLKGLPKSEIKEEVELLLR------VLGLTD-----KANKRARtLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 525 LDNESEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:cd03263 164 LDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGS 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
363-574 |
4.05e-29 |
|
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: 114.60 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGqVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAdLRRQVGLVPQETL 442
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAE-----NILYGRPGASQAEVeaaahaahahefICEL--EGGYGAVVGERGVKLSGGQRQRVAIARAILKDPR 514
Cdd:cd03264 83 VYPNfTVREfldyiAWLKGIPSKEVKAR------------VDEVleLVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 515 ILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
372-577 |
6.36e-29 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 115.82 E-value: 6.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQ-VGLVPQETLLFSG- 446
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENILYGRPGASQAEVEAAAHAAHAHEFIcELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRILILDEATSALD 526
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELV-GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499192068 527 NESEALVQAALERL--MVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHE 577
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
359-574 |
1.35e-28 |
|
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: 113.36 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFdvPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADlrRQVGLVP 438
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYGR-PGASQAEVEAAAHAAHAHEFicelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03298 77 QENNLFAHlTVEQNVGLGLsPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 517 ILDEATSALD----NESEALV-QAALERLMvgrTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLVlDLHAETKM---TVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
368-593 |
2.05e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.96 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSG- 446
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENILYGRP------GASQAEVEAAAHAAHAHEFICELeggygavvGERGV-KLSGGQRQRVAIARAILKDPRILILD 519
Cdd:PRK11231 92 TVRELVAYGRSpwlslwGRLSAEDNARVNQAMEQTRINHL--------ADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 520 EATSALD-NEsealvQAALERLM-----VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAgGLYRELYEL 592
Cdd:PRK11231 164 EPTTYLDiNH-----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTP-GLLRTVFDV 237
|
.
gi 499192068 593 Q 593
Cdd:PRK11231 238 E 238
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
368-579 |
2.09e-28 |
|
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: 113.39 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTL----VNLIPrfwdVTAGRVEVDGHDV---RAYALAdlRRQVGLVPQE 440
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLlktlMGLLP----VKSGSIRLDGEDItklPPHERA--RAGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSG-TVAENILYG---RPGASQAEVEaaahaahaheFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:TIGR03410 84 REIFPRlTVEENLLTGlaaLPRRSRKIPD----------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 517 ILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGL 579
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
367-574 |
2.89e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.58 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVRAYALADLRRQ-VGLVPQE 440
Cdd:COG1129 13 SFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILsgvyqP-----DSGEILLDGEPVRFRSPRDAQAAgIAIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGY--GAVVGErgvkLSGGQRQRVAIARAILKDPRILI 517
Cdd:COG1129 88 LNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIdpDTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSAL-DNESEALVqAALERLMVGRTTFV-VAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:COG1129 164 LDEPTASLtEREVERLF-RIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-589 |
5.21e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 355 AEGRVRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRR 432
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQ--ETLLFSGTVAENILYGrpgasqaeveaaahaahaheficeLEggygavvgERGV----------------- 493
Cdd:PRK13635 82 QVGMVFQnpDNQFVGATVQDDVAFG------------------------LE--------NIGVpreemvervdqalrqvg 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 ----------KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRSADR 561
Cdd:PRK13635 130 medflnrephRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADR 209
|
250 260
....*....|....*....|....*...
gi 499192068 562 ILVMDAGRVVADGTHEGLMAAGGLYREL 589
Cdd:PRK13635 210 VIVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
359-574 |
6.19e-28 |
|
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: 112.49 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRF-WDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 ---------PQETLL------FSGTVAeniLYGRPGASQAEVEAAAhaahahefICELegGYGAVVGERGVKLSGGQRQR 502
Cdd:COG1119 84 spalqlrfpRDETVLdvvlsgFFDSIG---LYREPTDEQRERAREL--------LELL--GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 503 VAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTTFV-VAHRLSTIRSA-DRILVMDAGRVVADG 574
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
363-575 |
6.67e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.56 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQE-T 441
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHsS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 LLFSGTVAENILYGR-PGASQAEVEAAAHAAHAHEfiCELEGgygavVGERGV-KLSGGQRQRVAIARAIL------KDP 513
Cdd:PRK13548 87 LSFPFTVEEVVAMGRaPHGLSRAEDDALVAAALAQ--VDLAH-----LAGRDYpQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 514 RILILDEATSALD-----NESEALVQAALERlmvGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGT 575
Cdd:PRK13548 160 RWLLLDEPTSALDlahqhHVLRLARQLAHER---GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
359-571 |
9.23e-28 |
|
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: 111.19 E-value: 9.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayalADLR---RQVG 435
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPpkdRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENILYG--RPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKD 512
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlkLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 513 PRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAH-RLSTIRSADRILVMDAGRVV 571
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
372-581 |
9.67e-28 |
|
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: 112.31 E-value: 9.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFSGTVAEN 451
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 452 iLYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEA 531
Cdd:cd03288 115 -LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499192068 532 LVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
373-572 |
1.28e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.66 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGHDVRAYALAD-LRRQVGLVPQETLLFSG 446
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILyglyqP-----DSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 -TVAENILYGRPGASQAEVEAAAHAAHahefICELEGGYG------AVVGErgvkLSGGQRQRVAIARAILKDPRILILD 519
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRLDRKAARAR----IRELSERYGldvdpdAKVED----LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 520 EATSAL-DNESEALVqAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVA 572
Cdd:COG3845 167 EPTAVLtPQEADELF-EILRRLAAeGKSIIFITHKLREVMAiADRVTVLRRGKVVG 221
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
115-333 |
1.48e-27 |
|
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: 112.56 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 115 LRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQL---ASQGFTLIGSVLLLvqtSPRLSLLTLAIIP 191
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLmwyLARGLFLFIFMLWL---SPKLALLTALGLP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 192 LVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMS 271
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSS 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 272 FltfGALAL---VLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18589 228 F---SGLALkvgILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
368-579 |
1.75e-27 |
|
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: 110.54 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlADLRRQVGLVPQETLLFSG- 446
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENI-----LYGRPGASQAEVeaaahaahahefICELEGGYG-AVVGERGVK-LSGGQRQRVAIARAILKDPRILILD 519
Cdd:cd03265 89 TGWENLyiharLYGVPGAERRER------------IDELLDFVGlLEAADRLVKtYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 520 EATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGL 579
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
358-571 |
2.33e-27 |
|
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: 112.84 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFvdvgFTYAGA-PALQDITFDVPAGQVVALVGPSGAGKTTL----VNLIPRfWDVTAGRVEVDGHDVRAYALADLR- 431
Cdd:COG0444 8 KVYF----PTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPP-PGITSGEILFDGEDLLKLSEKELRk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 ---RQVGLVPQE---------TLLFSgtVAENILYGRPGASQAEVEAAAHAahaheficeLEggygaVVG----ERGVK- 494
Cdd:COG0444 83 irgREIQMIFQDpmtslnpvmTVGDQ--IAEPLRIHGGLSKAEARERAIEL---------LE-----RVGlpdpERRLDr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 ----LSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMV------GRTTFVVAHRLSTIRS-ADRIL 563
Cdd:COG0444 147 ypheLSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQILNLLKdlqrelGLAILFITHDLGVVAEiADRVA 222
|
....*...
gi 499192068 564 VMDAGRVV 571
Cdd:COG0444 223 VMYAGRIV 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
367-591 |
2.94e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayalADL---RRQVGLVPQETLL 443
Cdd:PRK09452 23 SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVpaeNRHVNTVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 444 FSG-TVAENILYG-----RPGASQAEVEAAAHAahahefICELEGgygavVGERGVK-LSGGQRQRVAIARAILKDPRIL 516
Cdd:PRK09452 98 FPHmTVFENVAFGlrmqkTPAAEITPRVMEALR------MVQLEE-----FAQRKPHqLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 517 ILDEATSALDNESEALVQAALERLMvgRT---TFV-VAH-RLSTIRSADRILVMDAGRVVADGTHeglmaagglyRELYE 591
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQ--RKlgiTFVfVTHdQEEALTMSDRIVVMRDGRIEQDGTP----------REIYE 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
363-595 |
3.57e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 110.56 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL 442
Cdd:COG4604 6 NVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAENILYGRpgasqaeveaaahaahaheF-----------------------ICELEGGYgavVGErgvkLSGG 498
Cdd:COG4604 86 INSRlTVRELVAFGR-------------------FpyskgrltaedreiideaiayldLEDLADRY---LDE----LSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 499 QRQRVAIARAILKDPRILILDEATSALD-NESEALVQaALERLM--VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADG 574
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQG 218
|
250 260
....*....|....*....|.
gi 499192068 575 THEGLMAAGGLyRELYELQFR 595
Cdd:COG4604 219 TPEEIITPEVL-SDIYDTDIE 238
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
373-574 |
3.85e-27 |
|
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: 109.38 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrAYALADLRRQVGLVPQETLLFSG-TVAEN 451
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 452 I-----LYGRPGASQAEVeaaahaahahefICELEG--GYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:cd03266 99 LeyfagLYGLKGDELTAR------------LEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 525 LDNESEALVQAALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03266 167 LDVMATRALREFIRQLRaLGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
374-578 |
7.58e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 108.96 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyaLADLRRQVGLVPQETLLFSG-TVAENI 452
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 LYGRPGASQAEVEAAAHAAHAHEFIcelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEAL 532
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499192068 533 VQAALERLM--VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEG 578
Cdd:cd03299 168 LREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
374-575 |
1.16e-26 |
|
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: 108.29 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQ-VGLVPQ-ETLLFSGTV 448
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQsFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI-----LYGRPGASQAEVEaaahaahaheficELEG-GYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEAT 522
Cdd:COG4181 108 LENVmlpleLAGRRDARARARA-------------LLERvGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 523 SALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:COG4181 175 GNLDAATGEQIIDLLFELNreRGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
80-324 |
1.47e-26 |
|
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: 109.86 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 80 DRTVLSLLGI-----FALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSdVGTVQAVT 154
Cdd:cd18567 37 DRDLLTVLAIgfgllLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 155 STALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQS 234
Cdd:cd18567 116 TTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 235 FTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVA 314
Cdd:cd18567 196 FGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRAS 275
|
250
....*....|
gi 499192068 315 ALTGVFNQFQ 324
Cdd:cd18567 276 SLIDKLFELR 285
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
332-589 |
1.87e-26 |
|
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: 115.43 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 332 RIFELLDERSDLPGPAAPRPLSRAEGRVRFVDVG-FTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFW 408
Cdd:TIGR00957 609 RLRIFLSHEELEPDSIERRTIKPGEGNSITVHNAtFTWARDlpPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 409 DVTAGRVEVDGhdvrayaladlrrQVGLVPQETLLFSGTVAENILYGRPgasqAEVEAAAHAAHAHEFICELE---GGYG 485
Cdd:TIGR00957 689 DKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKA----LNEKYYQQVLEACALLPDLEilpSGDR 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 486 AVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNE-SEALVQAAL--ERLMVGRTTFVVAHRLSTIRSADRI 562
Cdd:TIGR00957 752 TEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVI 831
|
250 260
....*....|....*....|....*..
gi 499192068 563 LVMDAGRVVADGTHEGLMAAGGLYREL 589
Cdd:TIGR00957 832 IVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
373-575 |
2.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV--RAYALADLRRQVGLVPQ--ETLLFSGTV 448
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENILYG--RPGASQAEVEAAAHAAHaheficELEG-GYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSAL 525
Cdd:PRK13637 102 EKDIAFGpiNLGLSEEEIENRVKRAM------NIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499192068 526 D--NESEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK13637 176 DpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
374-575 |
2.71e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADlrRQVGLVPQETLLFSG-TVAENI 452
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 LYG--------RPGASQAEVEAAAHAAHAHefICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:PRK10851 96 AFGltvlprreRPNAAAIKAKVTQLLEMVQ--LAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 525 LDneseALVQAALERLM------VGRTTFVVAH-RLSTIRSADRILVMDAGRVVADGT 575
Cdd:PRK10851 167 LD----AQVRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
359-577 |
3.63e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLV---NL--IPRfwdvtAGRVEVDGH------DVRAYAL 427
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLleTPD-----SGQLNIAGHqfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 428 ADLRRQVGLVPQETLLFSG-TVAENILYGrPgasqaeveaaahaahahefiCELEGGYGAVVGERGVK------------ 494
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHlTVMENLIEA-P--------------------CKVLGLSKEQAREKAMKllarlrltdkad 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 -----LSGGQRQRVAIARAILKDPRILILDEATSALDNESEA-LVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDA 567
Cdd:COG4161 137 rfplhLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEK 216
|
250
....*....|
gi 499192068 568 GRVVADGTHE 577
Cdd:COG4161 217 GRIIEQGDAS 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
344-591 |
3.67e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.49 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 344 PGPAAPRPLSraEGRVRFVDVGFTY-AGAP-ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHD 421
Cdd:PTZ00243 1296 PTSAAPHPVQ--AGSLVFEGVQMRYrEGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 422 VRAYALADLRRQVGLVPQETLLFSGTVAENIlygRP--GASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQ 499
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQ 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 500 RQRVAIARAILKDPRILIL-DEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT-HE 577
Cdd:PTZ00243 1451 RQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSpRE 1530
|
250
....*....|....
gi 499192068 578 GLMAAGGLYRELYE 591
Cdd:PTZ00243 1531 LVMNRQSIFHSMVE 1544
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
364-577 |
4.32e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 107.02 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 364 VGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLV---NL--IPRfwdvtAGRVEVDGH------DVRAYALADLRR 432
Cdd:PRK11124 8 INCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLleMPR-----SGTLNIAGNhfdfskTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQETLLFSG-TVAENiLYGRP----GASQAEVEAAAHAAHAHEFICELEGGYgavvgerGVKLSGGQRQRVAIAR 507
Cdd:PRK11124 83 NVGMVFQQYNLWPHlTVQQN-LIEAPcrvlGLSKDQALARAEKLLERLRLKPYADRF-------PLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHE 577
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAeTGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
25-568 |
7.38e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.82 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 25 LRRLLAYARPY----RLPFVLGVLATLISSGLGLV-----FPRLFGTLIDAsflkVGSTDTGPLDRTVLSLLGIFALSAC 95
Cdd:COG4178 4 LRQFWRLARPYwrseEKWKAWGLLALLLLLTLASVglnvlLNFWNRDFYDA----LQARDAAAFWQQLGVFALLAAISIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 96 FGAAQAYLLARVGAgvvaDLRRALFSHLLS--LSPR-FFGNHRTGDLTS----RLTSDVgtvQAVTSTALaqlaSQGFTL 168
Cdd:COG4178 80 LAVYQTYLRQRLQI----RWREWLTERLLDrwLSNRaYYRLQLSGGEIDnpdqRIAEDI---RLFTETTL----SLSLGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 169 IGSVLLLV-------QTSPRLSLLT-------------LAIIPLVIGTAVT--IGRRIRRVS-----------------R 209
Cdd:COG4178 149 LSSVVTLIsfigilwSLSGSLTFTLggysitipgymvwAALIYAIIGTLLThlIGRPLIRLNfeqqrreadfrfalvrvR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 210 EVQDAVAAANGQAEEaisGVRVVQSFTAegleeerygqgVLASFRA-ALRRARLQALMTGVMSFLTFGALALVLwfggRQ 288
Cdd:COG4178 229 ENAESIALYRGEAAE---RRRLRRRFDA-----------VIANWRRlIRRQRNLTFFTTGYGQLAVIFPILVAA----PR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 289 VMSGALTPGNLVTflfyalqvggTVAAltgvFNQFQEALG--------------ASSRIFELLD--ERSDLPGPAAPRPL 352
Cdd:COG4178 291 YFAGEITLGGLMQ----------AASA----FGQVQGALSwfvdnyqslaewraTVDRLAGFEEalEAADALPEAASRIE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 353 SRAEGRVRFVDVG-FTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDvrayaladlr 431
Cdd:COG4178 357 TSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA---------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 rQVGLVPQETLLFSGTVAENILYGRPGA--SQAEVEAAAHAAHAHEFICELEggygaVVGERGVKLSGGQRQRVAIARAI 509
Cdd:COG4178 427 -RVLFLPQRPYLPLGTLREALLYPATAEafSDAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARLL 500
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 510 LKDPRILILDEATSALDNESEALVQAALERLMVGrTTFV-VAHRLSTIRSADRILVMDAG 568
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
389-582 |
1.05e-25 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 107.96 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 389 LVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyaLADLRRQVGLVPQETLLFSG-TVAENILYG----RPGASQAE 463
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFPHmTVEENVAFGlkmrKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 464 VEAAAHAAHAHEficeleGGYGAvvgERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM-- 541
Cdd:TIGR01187 79 PRVLEALRLVQL------EEFAD---RKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeq 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499192068 542 VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:TIGR01187 150 LGITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
352-582 |
1.90e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.51 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 352 LSRAEGRVRFVDvgftyagapalqDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALA 428
Cdd:COG4608 24 FGRTVGVVKAVD------------GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 429 DLRRQVGLV---PQETLLFSGTVAENILYG------RPGASQAEVeaaahaahahefICELEggygAVVG---------- 489
Cdd:COG4608 92 PLRRRMQMVfqdPYASLNPRMTVGDIIAEPlrihglASKAERRER------------VAELL----ELVGlrpehadryp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 490 -ErgvkLSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAA----LERLM--VGRTTFVVAHRLSTIRS-ADR 561
Cdd:COG4608 156 hE----FSGGQRQRIGIARALALNPKLIVCDEPVSALD----VSIQAQvlnlLEDLQdeLGLTYLFISHDLSVVRHiSDR 227
|
250 260
....*....|....*....|.
gi 499192068 562 ILVMDAGRVVADGTHEGLMAA 582
Cdd:COG4608 228 VAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
363-574 |
3.23e-25 |
|
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: 103.45 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRayALADLRRQVG-LVPQET 441
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGaLIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 LLFSGTVAENI-----LYGRPGASQAEveaaahaahahefiCELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:cd03268 83 FYPNLTARENLrllarLLGIRKKRIDE--------------VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 517 ILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
358-567 |
4.35e-25 |
|
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: 103.33 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyALADLRRQVGLV 437
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSG-TVAENI-----LYGRPGASQAEVEAaahaahaheficeLEG-GYGAVVGERGVKLSGGQRQRVAIARAIL 510
Cdd:COG4133 81 GHADGLKPElTVRENLrfwaaLYGLRADREAIDEA-------------LEAvGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVA-HRLSTIRSADRILVMDA 567
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGDF 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
378-581 |
6.54e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.51 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 378 TFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAdlRRQVGLVPQETLLFSG-TVAENILYG- 455
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 456 RPG-----ASQAEVEAAAHAAHAHEFICELEGgygavvgergvKLSGGQRQRVAIARAILKDPRILILDEATSALD---- 526
Cdd:PRK10771 97 NPGlklnaAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 527 NESEALV-QAALERLMvgrTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK10771 166 QEMLTLVsQVCQERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
367-602 |
7.33e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRayalADLRRQVGLVPQETLLFSG 446
Cdd:COG4152 10 RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERGLYPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 -TVAENILY-----GRPGAsqaeVEAAAHAAHAHEFicELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRILILDE 520
Cdd:COG4152 86 mKVGEQLVYlarlkGLSKA----EAKRRADEWLERL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 521 ATSALD--NeSEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAAGGlyRELYELQFRQQ 597
Cdd:COG4152 156 PFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG--RNTLRLEADGD 232
|
....*
gi 499192068 598 QEARR 602
Cdd:COG4152 233 AGWLR 237
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
102-333 |
8.28e-25 |
|
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: 104.81 E-value: 8.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 102 YLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPR 181
Cdd:cd18554 68 YFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 182 LSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRAR 261
Cdd:cd18554 148 LTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTR 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 262 LQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18554 228 WNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
359-581 |
8.36e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.30 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA-LADLRRQVGL 436
Cdd:PRK13644 2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQ--ETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEficelEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPR 514
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALA-----EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 515 ILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-574 |
9.50e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 9.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 329 ASSRIFELLDERSDLPGPAAPRPLSRAEGRV--RFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPR 406
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPGSMSTVaiDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 407 FWDVTAGRVEVDGHDVRAYALAdLRRQVGLVPQ-ETLLFSGTVAENIL-YGRpgASQAEVEAAAHAAHAHEFICELEGGY 484
Cdd:PRK13536 90 MTSPDAGKITVLGVPVPARARL-ARARIGVVPQfDNLDLEFTVRENLLvFGR--YFGMSTREIEAVIPSLLEFARLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 485 GAVVGErgvkLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTI-RSADRI 562
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRL 242
|
250
....*....|..
gi 499192068 563 LVMDAGRVVADG 574
Cdd:PRK13536 243 CVLEAGRKIAEG 254
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
43-326 |
1.36e-24 |
|
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: 104.17 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASflkVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18779 8 LLASLLLQLLGLALPLLTGVLVDRV---IPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLTSdVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGR 202
Cdd:cd18779 85 LLRLPYRFFQQRSTGDLLMRLSS-NATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 203 RIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVL 282
Cdd:cd18779 164 RVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 499192068 283 WFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEA 326
Cdd:cd18779 244 WVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLL 287
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
367-582 |
1.71e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTL---VNLI--PRFWDVTAGRVEVDGH---DVRAYALADLRRQVGLVP 438
Cdd:PRK11264 12 KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLeqPEAGTIRVGDITIDTArslSQQKGLIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYGrPGASQAEVEAAAHAAHAHEFiceleggygAVVGERGV------KLSGGQRQRVAIARAILK 511
Cdd:PRK11264 92 QNFNLFPHrTVLENIIEG-PVIVKGEPKEEATARARELL---------AKVGLAGKetsyprRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
367-590 |
2.32e-24 |
|
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: 101.85 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALaDLRRQVGL--VPQETLLF 444
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SG-TVAENILygrpGASQAEVEAAAHAAHAHEFICElEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:cd03218 88 RKlTVEENIL----AVLEIRGLSKKEREEKLEELLE-EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 524 ALDNESEALVQAALERLM-VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLmAAGGLYRELY 590
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEI-AANELVRKVY 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
367-574 |
2.57e-24 |
|
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: 101.20 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAladlRRQVGLVPQETLLFSG 446
Cdd:cd03269 9 RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 -TVAENILYgrpGASQAEVEAAAHAAHAHEFICELE-GGYGAVVGErgvKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:cd03269 85 mKVIDQLVY---LAQLKGLKKEEARRRIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 525 LDNES-EALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADG 574
Cdd:cd03269 159 LDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
366-568 |
3.20e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.25 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 366 FTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRV----EVDGHDVRAYALADLRRQVGLVPQE 440
Cdd:cd03290 8 FSWgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEfICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDE 520
Cdd:cd03290 88 PWLLNATVEENITFGSPFNKQRYKAVTDACSLQPD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499192068 521 ATSALD-NESEALVQAALERLMVG--RTTFVVAHRLSTIRSADRILVMDAG 568
Cdd:cd03290 167 PFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-573 |
4.11e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.09 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV-------RAyaladlrRQVGLVPQETLL-- 443
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRA-------KYIGRVFQDPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 444 -FSGTVAENIL--YGRpgaSQAEVEAAAHAAHAHEFICE--------LEGGYGAVVGergvKLSGGQRQRVAIARAILKD 512
Cdd:COG1101 94 aPSMTIEENLAlaYRR---GKRRGLRRGLTKKRRELFREllatlglgLENRLDTKVG----LLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 513 PRILILDEATSALDNESEALVQAALERLmVGR---TTFVVAHRLS-TIRSADRILVMDAGRVVAD 573
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRIILD 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
381-570 |
5.20e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 100.32 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 381 VPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVraYALADLRRQVGLVPQETLLFSG-TVAENILYG-RPG 458
Cdd:TIGR01277 21 VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGlHPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 459 ASQAEVEAAAHAAHAHEFicelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALD----NESEALV- 533
Cdd:TIGR01277 99 LKLNAEQQEKVVDAAQQV------GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVk 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 499192068 534 QAALERlmvGRTTFVVAHRLS-TIRSADRILVMDAGRV 570
Cdd:TIGR01277 173 QLCSER---QRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
335-582 |
5.50e-24 |
|
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: 105.92 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 335 ELLD---ERSDLPGPAAPRPLSRAEG-RVRF-VDVGF---TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTL----VN 402
Cdd:COG4172 255 KLLAaepRGDPRPVPPDAPPLLEARDlKVWFpIKRGLfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 403 LIPrfwdvTAGRVEVDGHDVRAY---ALADLRRQVGLVPQETllFSG-----TVAENILYG----RPGASQAeveaaaha 470
Cdd:COG4172 335 LIP-----SEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAA-------- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 471 ahaheficELEGGYGAVVGERGVK----------LSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAA---- 536
Cdd:COG4172 400 --------ERRARVAEALEEVGLDpaarhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildl 467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499192068 537 LERLMV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG4172 468 LRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
359-575 |
5.73e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGL 436
Cdd:PRK13632 8 IKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQ--ETLLFSGTVAENILYGrpgasqaeveaaahaahaheficeLEG-------------GYGAVVGERGV------KL 495
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFG------------------------LENkkvppkkmkdiidDLAKKVGMEDYldkepqNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 496 SGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVA--HRLSTIRSADRILVMDAGRVVAD 573
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQ 223
|
..
gi 499192068 574 GT 575
Cdd:PRK13632 224 GK 225
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-333 |
1.09e-23 |
|
Six-transmembrane helical domain 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: 350002 [Multi-domain] Cd Length: 312 Bit Score: 101.97 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 39 FVLGVLATLISSGLGLVFPRLFGTLIDaSFLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGV------- 111
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTD-SFTNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVlitayiq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 112 -----------VADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSP 180
Cdd:cd18558 80 gsfwglaagrqTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 181 RLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRA 260
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 261 RLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
372-592 |
1.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.58 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ--ETLLFSGTVA 449
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQnpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 450 ENILYGRPGASQAEVEAAAHAAHAHEFIcelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNES 529
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 530 E-ALVQAALE-RLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGlyrELYEL 592
Cdd:PRK13650 176 RlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN---DLLQL 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
359-571 |
2.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYA-GAP----ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRA----YALAD 429
Cdd:PRK13641 3 IKFENVDYIYSpGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 LRRQVGLVPQ--ETLLFSGTVAENILYGrP---GASQAEVEAAAHAAHAHEFICEleggygAVVGERGVKLSGGQRQRVA 504
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFG-PknfGFSEDEAKEKALKWLKKVGLSE------DLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 505 IARAILKDPRILILDEATSALDNES-EALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVV 571
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLI 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
374-571 |
2.99e-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: 98.50 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIP---RFWDVTAGRVEVDGHDVRAYALadlRRQVGLVPQ-ETLLFSGTVA 449
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQF---QKCVAYVRQdDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 450 ENILYGRPGASQAEVEAAAHAAHAHEFIcELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNES 529
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVEDVL-LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499192068 530 EALVQAALERLMV-GRTTFVVAH--RLSTIRSADRILVMDAGRVV 571
Cdd:cd03234 179 ALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
359-575 |
5.66e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGA--PALQDITFDVPAGQVVALVGPSGAGKTT---LVN--LIPRfwDVTAGRVEVDGHDVRAYALADLR 431
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTiskLINglLLPD--DNPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQ--ETLLFSGTVAENILYG-------RPgasqaeveaaahaahaheficELEGGYGAVVGERGV--------- 493
Cdd:PRK13640 84 EKVGIVFQnpDNQFVGATVGDDVAFGlenravpRP---------------------EMIKIVRDVLADVGMldyidsepa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTIRSADRILVMDAGRVV 571
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
....
gi 499192068 572 ADGT 575
Cdd:PRK13640 223 AQGS 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
359-601 |
6.03e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 6.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAP----ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH----DVRAYALAD 429
Cdd:PRK13634 3 ITFQKVEHRYqYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 LRRQVGLVPQ--ETLLFSGTVAENILYGrP---GASQAEVEAAAHAahahefICELEGGYGAVVGERGVKLSGGQRQRVA 504
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFG-PmnfGVSEEDAKQKARE------MIELVGLPEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 505 IARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGL-- 579
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIfa 235
|
250 260
....*....|....*....|....*..
gi 499192068 580 ----MAAGGLyrELYE-LQFRQQQEAR 601
Cdd:PRK13634 236 dpdeLEAIGL--DLPEtVKFKRALEEK 260
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
366-575 |
9.36e-23 |
|
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: 98.39 E-value: 9.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 366 FTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhdvrayaladlrrQVGLVPQETLLFS 445
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 GTVAENILYGrpgasqaeVEAAAHAAHAHEFICELEGGYGA-------VVGERGVKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:cd03291 112 GTIKENIIFG--------VSYDEYRYKSVVKACQLEEDITKfpekdntVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 519 DEATSALDNESEALV-QAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
363-599 |
1.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQE- 440
Cdd:PRK13647 9 DLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 -TLLFSGTVAENILYG--RPGASQAeveaaahaahaheficELEGGYGAVVGERGVK---------LSGGQRQRVAIARA 508
Cdd:PRK13647 89 dDQVFSSTVWDDVAFGpvNMGLDKD----------------EVERRVEEALKAVRMWdfrdkppyhLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 509 ILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVA-HRLSTIRS-ADRILVMDAGRVVADG-----THEGLMA 581
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVE 232
|
250
....*....|....*...
gi 499192068 582 AGGLYRELYELQFRQQQE 599
Cdd:PRK13647 233 QAGLRLPLVAQIFEDLPE 250
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
359-570 |
3.52e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDghDVRAYALADLRRQVGLVP 438
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG-TVAENILYGR--PGASQAEVEAAAHAAHAhefICELeggygAVVGERGVK-LSGGQRQRVAIARAILKDPR 514
Cdd:PRK11000 82 QSYALYPHlSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL-----AHLLDRKPKaLSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 515 ILILDEATSALDnesEAL-VQAALE--RL--MVGRTTFVVAH-RLSTIRSADRILVMDAGRV 570
Cdd:PRK11000 154 VFLLDEPLSNLD---AALrVQMRIEisRLhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
363-562 |
3.76e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDV-----TAGRVEVDGHDVraYA----LADLRRQ 433
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNI--YSprtdTVDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 434 VGLVPQETLLFSGTVAENILYG-RPGASQAEVEAAAHAAHAHEficeleggyGAVVGER--------GVKLSGGQRQRVA 504
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLK---------GASIWDEvkdrlhdsALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 505 IARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHrlsTIRSADRI 562
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
363-526 |
3.96e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPRFwdVTAGRVEVDGHDVRAyaLADLRRQVGLV 437
Cdd:COG4136 6 NLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaiagtLSPAF--SASGEVLLNGRRLTA--LPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEfiCELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRIL 516
Cdd:COG4136 82 FQDDLLFPHlSVGENLAFALPPTIGRAQRRARVEQALEE--AGLAGFADRDPAT----LSGGQRARVALLRALLAEPRAL 155
|
170
....*....|
gi 499192068 517 ILDEATSALD 526
Cdd:COG4136 156 LLDEPFSKLD 165
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
368-565 |
4.47e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.22 E-value: 4.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdvrayaladlrRQVGLVPQETLL---F 444
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SGTVAENILYGRPGASQAEVEAAAHAAHAHEFICE---LEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:NF040873 71 PLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALErvgLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499192068 522 TSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRSADRILVM 565
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
347-591 |
4.98e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 347 AAPRPLSRAEGRVRFV----DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV 422
Cdd:PRK11607 4 AIPRPQAKTRKALTPLleirNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 423 RAyaLADLRRQVGLVPQETLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICELEggygaVVGERGVKLSGGQRQ 501
Cdd:PRK11607 84 SH--VPPYQRPINMMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-----FAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 502 RVAIARAILKDPRILILDEATSALDNESEALVQAA----LERlmVGRTTFVVAH-RLSTIRSADRILVMDAGRVVADGTH 576
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdiLER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
250
....*....|....*
gi 499192068 577 EglmaagglyrELYE 591
Cdd:PRK11607 235 E----------EIYE 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
369-566 |
7.72e-22 |
|
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: 92.60 E-value: 7.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 369 AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdvrayaladlrRQVGLVPQETLLFSGTV 448
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENILYgrPGASqaeveaaahaahaheficeleggygavvgergvKLSGGQRQRVAIARAILKDPRILILDEATSALDNE 528
Cdd:cd03223 81 REQLIY--PWDD---------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 499192068 529 SEALVQAALERLMvgrTTFV-VAHRLSTIRSADRILVMD 566
Cdd:cd03223 126 SEDRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLD 161
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
373-574 |
8.89e-22 |
|
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: 94.14 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayALADLrrQVGLVPqetllfSGTVAENI 452
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---SLLGL--GGGFNP------ELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 -----LYGRPGASqaeveaaahAAHAHEFI---CELEGgygavVGERGVK-LSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:cd03220 106 ylngrLLGLSRKE---------IDEKIDEIiefSELGD-----FIDLPVKtYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 524 ALDnesEALVQAALERL--MV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03220 172 VGD---AAFQEKCQRRLreLLkqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
373-575 |
1.16e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLI-----PrfwdvTAGRVEVDGhdvRAYALADLrrQVGLVPQetllFSGt 447
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIagileP-----TSGRVEVNG---RVSALLEL--GAGFHPE----LTG- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 448 vAENI-----LYGRPGASqaeveaaahAAHAHEFICELeggygAVVGE---RGVK-LSGGQRQRVAIARAILKDPRILIL 518
Cdd:COG1134 106 -RENIylngrLLGLSRKE---------IDEKFDEIVEF-----AELGDfidQPVKtYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 519 DEATSALDnesEALVQAALERLMV----GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:COG1134 171 DEVLAVGD---AAFQKKCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
373-575 |
1.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPRFWDVTAGRVeVDGHDVRAYALAD------------LRRQVG 435
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDI-YIGDKKNNHELITnpyskkiknfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQ--ETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAheficeLEG-GYGAVVGERG-VKLSGGQRQRVAIARAILK 511
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFY------LNKmGLDDSYLERSpFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 512 DPRILILDEATSALDNESEA-LVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
359-570 |
1.23e-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: 94.92 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDvTAGRVEVDGHDVRAYALADLRRQVGLVP 438
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSGTVAENI-LYGRpgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILI 517
Cdd:cd03289 84 QKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499192068 518 LDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-570 |
1.30e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.50 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 357 GRVRFVDVGFTyaGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQ-VG 435
Cdd:cd03215 1 GEPVLEVRGLS--VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVP---QETLLFSG-TVAENILYGRPgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILK 511
Cdd:cd03215 79 YVPedrKREGLVLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTIRS-ADRILVMDAGRV 570
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-574 |
1.70e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 347 AAPRPLSRAEGrvrfvdVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdVRAYA 426
Cdd:PRK15439 6 TTAPPLLCARS------ISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-PCARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 427 LADLRRQVG--LVPQETLLFSG-TVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvkLSGGQRQRV 503
Cdd:PRK15439 79 TPAKAHQLGiyLVPQEPLLFPNlSVKENILFGLP-KRQASMQKMKQLLAALGCQLDLDSSAGS--------LEVADRQIV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 504 AIARAILKDPRILILDEATSALD-NESEALVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
359-575 |
1.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAP----ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA----LAD 429
Cdd:PRK13649 3 INLQNVSYTYqAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 LRRQVGLVPQ--ETLLFSGTVAENILYGrP---GASQAEVEAAAHAAHAHEFICEleggygAVVGERGVKLSGGQRQRVA 504
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PqnfGVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 505 IARAILKDPRILILDEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
43-309 |
2.34e-21 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 94.49 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASflkvgSTDTGPLDRTVLSLLGIFA----LSACFGAAQAYLLARVGAGVVADLRRA 118
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDAL-----SAPASALLAVPLLLLLAYGlariLSSLFNELRDALFARVSQRAVRRLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 119 LFSHLLSLSPRFFGNHRTGDLTSRLtsDVGT--VQAVTSTALAQLASQGFTLIG-SVLLLVQTSPRLSLLTLAIIPLVIG 195
Cdd:cd18582 77 VFRHLHSLSLRFHLSRKTGALSRAI--ERGTrgIEFLLRFLLFNILPTILELLLvCGILWYLYGWSYALITLVTVALYVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 196 TAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQgVLASFRAALRRarlqalMTGVMSFLTF 275
Cdd:cd18582 155 FTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDK-ALAKYEKAAVK------SQTSLALLNI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499192068 276 G-------ALALVLWFGGRQVMSGALTPGNLVTFLFYALQV 309
Cdd:cd18582 228 GqaliislGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQL 268
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
359-575 |
3.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.66 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGL 436
Cdd:PRK13648 8 IVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQ--ETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEficelEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPR 514
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALK-----QVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 515 ILILDEATSALDNESEALVQAALERLMVGR--TTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
363-565 |
3.23e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL 442
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSGTVAENILYG---RPGASQaeveaaahaahAHEFICELEG-GYGAVVGERGV-KLSGGQRQRVAIARAILKDPRILI 517
Cdd:PRK10247 92 LFGDTVYDNLIFPwqiRNQQPD-----------PAIFLDDLERfALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSALDNESEALVQAALERLMVGRTTFV--VAHRLSTIRSADRILVM 565
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITL 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
367-520 |
5.92e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTT----LVNLIPrfwdVTAGRVEVDGHDV-------RAyaladlRRQVG 435
Cdd:COG1137 12 SYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDIthlpmhkRA------RLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENIL-----YGRPGASQAEveaaahaahaheficELEG-----GYGAVVGERGVKLSGGQRQRVA 504
Cdd:COG1137 82 YLPQEASIFRKlTVEDNILavlelRKLSKKEREE---------------RLEElleefGITHLRKSKAYSLSGGERRRVE 146
|
170
....*....|....*.
gi 499192068 505 IARAILKDPRILILDE 520
Cdd:COG1137 147 IARALATNPKFILLDE 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
374-602 |
6.63e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.21 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVN----LIPrfwdvTAGRVEVDGHDVRAYALADLRRQVGLVPQETL-LFSGTV 448
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLArmagLLP-----GQGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI-LYGRPGASQaeveaaAHAAHAHEFICE---LEGGYGAVVGergvKLSGGQRQRVAIARAILK-------DPRILI 517
Cdd:COG4138 87 FQYLaLHQPAGASS------EAVEQLLAQLAEalgLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSALDnesealV--QAALERLMV-----GRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAGGLyREL 589
Cdd:COG4138 157 LDEPMNSLD------VaqQAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENL-SEV 229
|
250
....*....|...
gi 499192068 590 YELQFRQQQEARR 602
Cdd:COG4138 230 FGVKFRRLEVEGH 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-580 |
9.07e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 349 PRPLSRAEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAG-RVE--VDGHDVRAY 425
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGfRVEgkVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 426 A----LADLRRQVGLVPQETLLFSGTVAENILYGrpgasqaeveaaahaahahEFICELEGGYGAVVgER---------- 491
Cdd:PRK14243 81 ApdvdPVEVRRRIGMVFQKPNPFPKSIYDNIAYG-------------------ARINGYKGDMDELV-ERslrqaalwde 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 492 --------GVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLstiRSADRIL 563
Cdd:PRK14243 141 vkdklkqsGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARVS 217
|
250 260
....*....|....*....|
gi 499192068 564 VMDA---GRVVADGTHEGLM 580
Cdd:PRK14243 218 DMTAffnVELTEGGGRYGYL 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
359-590 |
1.25e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.54 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAP----ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG----HDVRAYALAD 429
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 LRRQVGLVPQ--ETLLFSGTVAENILYGRPGASQAEVEAAAHAahaheFICELEGGYGA-VVGERGVKLSGGQRQRVAIA 506
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 507 RAILKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAAG 583
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
....*..
gi 499192068 584 GLYRELY 590
Cdd:PRK13646 238 KKLADWH 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
366-593 |
1.36e-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: 96.90 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 366 FTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhdvrayaladlrrQVGLVPQETLLFS 445
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 GTVAENILYGrpgasqaeVEAAAHAAHAHEFICELEGGYG-------AVVGERGVKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:TIGR01271 501 GTIKDNIIFG--------LSYDEYRYTSVIKACQLEEDIAlfpekdkTVLGEGGITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 519 DEATSALDNESEA-LVQAALERLMVGRTTFVVAHRLSTIRSADRILVMdagrvvadgtHEGLMAAGGLYRELYELQ 593
Cdd:TIGR01271 573 DSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLL----------HEGVCYFYGTFSELQAKR 638
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
374-581 |
1.62e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ--ETLLFSGTVAEN 451
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 452 ILYGRPGASQAEVEAAAHAAHAHEFICELEggygaVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEA 531
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 532 LVQAALERL--MVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK13642 178 EIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
363-577 |
3.40e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGA-PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQ-- 439
Cdd:PRK13652 8 DLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 ETLLFSGTVAENILYG--RPGASQAEVEAAAHAAHAHEFICELEggygavvgERGVK-LSGGQRQRVAIARAILKDPRIL 516
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGpiNLGLDEETVAHRVSSALHMLGLEELR--------DRVPHhLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 517 ILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHE 577
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVE 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
368-551 |
5.56e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrayalADLRRQVGLVPQ-ETLLFSG 446
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQnEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENILYGRPGASQAEVEAAAHAAHAHEFIcELEGgygavVGERGV-KLSGGQRQRVAIARAILKDPRILILDEATSAL 525
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKV-GLEG-----AEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 499192068 526 DNESEALVQAALERLM--VGRTTFVVAH 551
Cdd:PRK11248 160 DAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
43-329 |
6.12e-20 |
|
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: 90.65 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDasflKV---GSTDTgpldRTVLSLLGIFAL--SACFGAAQAYLLARVGAGVVADLRR 117
Cdd:cd18783 8 AIASLILHVLALAPPIFFQIVID----KVlvhQSYST----LYVLTIGVVIALlfEGILGYLRRYLLLVATTRIDARLAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 118 ALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALaqlasqgFTLIGSVLLLVQT------SPRLSLLTLA--- 188
Cdd:cd18783 80 RTFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLF-------GTLLDATSLLVFLpvlffySPTLALVVLAfsa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 189 IIPLVIGTAVtigRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTG 268
Cdd:cd18783 153 LIALIILAFL---PPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 269 VMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGA 329
Cdd:cd18783 230 LTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLS 290
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-582 |
6.80e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR-AYALADLRRQVGLVP 438
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QE-TLLFSGTVAENILYGR-PGASQAEVEAAAHAAHAHeficELEGGYGAVVGERGVK-LSGGQRQRVAIARAILKDPRI 515
Cdd:PRK11288 86 QElHLVPEMTVAENLYLGQlPHKGGIVNRRLLNYEARE----QLEHLGVDIDPDTPLKyLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 516 LILDEATSALD-NESEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVV------ADGTHEGLMAA 582
Cdd:PRK11288 162 IAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVatfddmAQVDRDQLVQA 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
363-585 |
8.75e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.83 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL 442
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 L-FSGTVAENILYGR-PGASQAEVEAAAHAAHAHEFICelEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDE 520
Cdd:PRK09536 88 LsFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVERAME--RTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 521 ATSALDNESEALVQAALERLM-VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAGGL 585
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVdDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
343-582 |
9.61e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 343 LPGPAAPrplsraegrVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV 422
Cdd:PRK13537 1 GPMSVAP---------IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 423 RAYAlADLRRQVGLVPQ-ETLLFSGTVAENIL-YGRP-GASQAEVEAAAHAAHAhefICELEGGYGAVVGErgvkLSGGQ 499
Cdd:PRK13537 72 PSRA-RHARQRVGVVPQfDNLDPDFTVRENLLvFGRYfGLSAAAARALVPPLLE---FAKLENKADAKVGE----LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 500 RQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHE 577
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPH 223
|
....*
gi 499192068 578 GLMAA 582
Cdd:PRK13537 224 ALIES 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
359-578 |
1.22e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV 434
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQET-LLFSGTVAENILYGR--PGASQAEVEAAAHAAHAHEFICELEGGYGavvgergVKLSGGQRQRVAIARAILK 511
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFP-------IQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 512 DPRILILDEATSALDNE-SEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVadGTHEG 578
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLH--GGVGG 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
359-570 |
1.33e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.44 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDvTAGRVEVDGHDVRAYALADLRRQVGLVP 438
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSGTVAENIlygRPGA--SQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRIL 516
Cdd:TIGR01271 1299 QKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499192068 517 ILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRV 570
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
363-526 |
1.50e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGA----PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyalADLRRqvGLVP 438
Cdd:COG4525 8 HVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG---PGADR--GVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 Q-ETLLFSGTVAENI-----LYGRPGASQAEVEAAAHAAHAheficeLEGGYGAVVGErgvkLSGGQRQRVAIARAILKD 512
Cdd:COG4525 83 QkDALLPWLNVLDNVafglrLRGVPKAERRARAEELLALVG------LADFARRRIWQ----LSGGMRQRVGIARALAAD 152
|
170
....*....|....
gi 499192068 513 PRILILDEATSALD 526
Cdd:COG4525 153 PRFLLMDEPFGALD 166
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
376-577 |
1.81e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.32 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH----DVRAYALADLRRQVGLVPQETLLFSG-TVAE 450
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdAEKGICLPPEKRRIGYVFQDARLFPHyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPGASQAEveaaahaahaheficeleggYGAVVGERGVK---------LSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:PRK11144 96 NLRYGMAKSMVAQ--------------------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 522 TSALDNESEALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHE 577
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
363-575 |
2.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH--DVRAYALADLRRQVGLVPQ 439
Cdd:PRK13636 10 ELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 --ETLLFSGTVAENILYG--RPGASQAEVEAAAHAAHAHEFICELEGgygavvgERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:PRK13636 90 dpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 516 LILDEATSALD----NESEALVQAALERLmvGRTTFVVAHRLSTIR-SADRILVMDAGRVVADGT 575
Cdd:PRK13636 163 LVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
374-591 |
2.43e-19 |
|
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: 86.43 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLI---PRFwDVTAGRVEVDGHDV-------RAyaladlRRQVGLVPQETLL 443
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPKY-EVTEGEILFKGEDItdlppeeRA------RLGIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 444 FSG-TVAEnilygrpgasqaeveaaahaahaheFICELeggygavvgerGVKLSGGQRQRVAIARAILKDPRILILDEAT 522
Cdd:cd03217 89 IPGvKNAD-------------------------FLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 523 SALDNESEALVQAALERLM-VGRTTFVVAH--RLSTIRSADRILVMDAGRVVADGTHEglmaaggLYRELYE 591
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE-------LALEIEK 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
374-573 |
2.60e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.09 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQ-VGLVPQETLLFSG-TV 448
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI----LYGRPGASQAEVEAAAHAAHAheficelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:PRK10535 104 AQNVevpaVYAGLERKQRLLRAQELLQRL---------GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499192068 525 LDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVMDAGRVVAD 573
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
376-587 |
5.73e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.62 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAdlRRQVGLVPQETLLFSG-TVAENILY 454
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 455 G-----RPGASQAEVEAAAHAahahefICELEGgygavVGERGV-KLSGGQRQRVAIARAILKDPRILILDEATSALDne 528
Cdd:PRK11432 102 GlkmlgVPKEERKQRVKEALE------LVDLAG-----FEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLD-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 529 sealvqAALERLM----------VGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTheglmaAGGLYR 587
Cdd:PRK11432 169 ------ANLRRSMrekirelqqqFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS------PQELYR 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-556 |
6.97e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTA-----GRVEVDGHDV--RAYALADLR 431
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILK 511
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499192068 512 DPRILILDEATSALDNESEALVQAALE--RLMVGRTTFVVAHRLSTI 556
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
373-581 |
7.42e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.10 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLRRQVGLV---PQETLLFSG 446
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVfqnPYGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVaENILyGRP-------GASQAEVEAAAHAahaheficeleggygAVVGERGVK-------LSGGQRQRVAIARAILKD 512
Cdd:PRK11308 110 KV-GQIL-EEPllintslSAAERREKALAMM---------------AKVGLRPEHydryphmFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 513 PRILILDEATSALDneseALVQAALERLMVG-----RTTFV-VAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK11308 173 PDVVVADEPVSALD----VSVQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-582 |
7.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 362 VDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAG-----RVEVDGHDVRAYA-LADLRRQVG 435
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 516 LILDEATSALDNESEALVQAALERLMVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
363-582 |
1.11e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.38 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL 442
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAENILYGR---PGASqaeveaaahaahaheficeleGGYGAVVGER--------GVK---------LSGGQRQ 501
Cdd:PRK10575 96 AAEGmTVRELVAIGRypwHGAL---------------------GRFGAADREKveeaislvGLKplahrlvdsLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 502 RVAIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEG 578
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAE 234
|
....
gi 499192068 579 LMAA 582
Cdd:PRK10575 235 LMRG 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
372-574 |
1.18e-18 |
|
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: 85.46 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhdVRAYALAD-LRRQVGLV--PQETLLFSGTV 448
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKkFLRRIGVVfgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI-----LYGRPGASQAEVEAAahaahahefICELEGgYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:cd03267 113 IDSFyllaaIYDLPPARFKKRLDE---------LSELLD-LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499192068 524 ALDNESEALVQAALERLMVGRTTFVV--AHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
362-575 |
1.31e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 362 VDVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR--AYALADLRRQVGLVP 438
Cdd:PRK13639 5 RDLKYSYPdGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 Q--ETLLFSGTVAENILYGrP---GASQAEVEAAAHAAHaheficeleggygAVVGERGVK------LSGGQRQRVAIAR 507
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFG-PlnlGLSKEEVEKRVKEAL-------------KAVGMEGFEnkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
363-529 |
1.69e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhdvrayalaDLRrqVGLVPQETL 442
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICELE------------GGYGA---------------VVGERGVK 494
Cdd:COG0488 72 LDDDlTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLErlaelqeefealGGWEAearaeeilsglgfpeEDLDRPVS 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 499192068 495 -LSGGQRQRVAIARAILKDPRILILDEATSALDNES 529
Cdd:COG0488 152 eLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
374-581 |
2.11e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 89.84 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDghdvrayaladlrRQVGLVPQETLLFSGTVAENIL 453
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 454 YGRPGASQAEVEAAAhaahahefICELE-------GGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALD 526
Cdd:PTZ00243 743 FFDEEDAARLADAVR--------VSQLEadlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 527 NE-SEALVQAALERLMVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PTZ00243 815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
368-595 |
2.77e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.56 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTT----LVNLIPRfwdvTAGRVEVDGHDVRAYAL-ADLRRQVGLVPQETL 442
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSG-TVAEN---ILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:PRK10895 89 IFRRlSVYDNlmaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQ-------SLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 519 DEATSALDNESEALVQAALERLM-VGRTTFVVAHRL-STIRSADRILVMDAGRVVADGTHEGLMAAGGLYRELYELQFR 595
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFR 240
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-596 |
2.82e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPrfwdvTAGRVEVDGHDV----RAYAladlrRQVGLV------ 437
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgiLVP-----TSGEVRVLGYVPfkrrKEFA-----RRIGVVfgqrsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 ------PQETLLFSGTVaenilYGRPGAsqaeveaaAHAAHAHEFICELEggygavVGE------RgvKLSGGQRQRVAI 505
Cdd:COG4586 107 lwwdlpAIDSFRLLKAI-----YRIPDA--------EYKKRLDELVELLD------LGElldtpvR--QLSLGQRMRCEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDNESEALVQAAL-----ERlmvGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGL 579
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeynrER---GTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEEL 242
|
250
....*....|....*..
gi 499192068 580 MAAGGLYRELyELQFRQ 596
Cdd:COG4586 243 KERFGPYKTI-VLELAE 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-571 |
2.85e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVD------GHDVRayaladlrr 432
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-------AGELEPDsgtvklGETVK--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 qVGLVPQETLLFSG--TVAENILYGRPGASQAEVEaaahaahaheficelegGY-------GAVVGERGVKLSGGQRQRV 503
Cdd:COG0488 380 -IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVR-----------------GYlgrflfsGDDAFKPVGVLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 504 AIARAILKDPRILILDEATSALDNES-EALVQAalerLMV--GrTTFVVAH-R--LSTIrsADRILVMDAGRVV 571
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETlEALEEA----LDDfpG-TVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
57-327 |
4.04e-18 |
|
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: 84.89 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 57 PRLFGTLIDAsfLKVGSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRT 136
Cdd:cd18583 16 PRQLGIIVDS--LSGGSGKSPWKEIGLYVLLRFLQSGGGLGLLRSWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 137 GDLTSRLtsDVGT-VQAVTSTALAQLASQGFTL-IGSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDA 214
Cdd:cd18583 94 GEVLKAI--EQGSsINDLLEQILFQIVPMIIDLvIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 215 VAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLAsFRAALRRARLQ-ALMTGVMSFLTFGALALVLWFGGRQVMSGA 293
Cdd:cd18583 172 DREERSILTESLLNWETVKYFNREPYEKERYREAVKN-YQKAERKYLFSlNLLNAVQSLILTLGLLAGCFLAAYQVSQGQ 250
|
250 260 270
....*....|....*....|....*....|....
gi 499192068 294 LTPGNLVTFLFYALQVGGTVAALTGVFNQFQEAL 327
Cdd:cd18583 251 ATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDL 284
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
359-577 |
4.10e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRF--WDVTAG-RVEVDGHDV-RAYALA-DLRR- 432
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGsHIELLGRTVqREGRLArDIRKs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 --QVGLVPQE-TLLFSGTVAENILYGRPGAS---QAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIA 506
Cdd:PRK09984 85 raNTGYIFQQfNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 507 RAILKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHE 577
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
363-573 |
4.40e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.34 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVRAYA--LADLRRQVGLVPQE 440
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL-------AGLETPSAGELLAGTapLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 T-LLFSGTVAENILYG-----RPGASQAeveaaahaahaheficeLEG-GYGAVVGERGVKLSGGQRQRVAIARAILKDP 513
Cdd:PRK11247 90 ArLLPWKKVIDNVGLGlkgqwRDAALQA-----------------LAAvGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 514 RILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLS-TIRSADRILVMDAGRVVAD 573
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKIGLD 215
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
372-569 |
1.08e-17 |
|
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: 82.48 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDgHDVRAYALA--------DLRRQ-VGLVPQ--- 439
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAqaspreilALRRRtIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 -----ETLlfsGTVAENILygrpgasqaeveaaahaahaheficelEGGYGAVVGERGVK-------------------L 495
Cdd:COG4778 104 viprvSAL---DVVAEPLL---------------------------ERGVDREEARARARellarlnlperlwdlppatF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 496 SGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFV-VAHRLSTI-RSADRILVMDAGR 569
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPFS 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
358-582 |
1.34e-17 |
|
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: 86.28 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 358 RVRFVDVGFTyagAPALQDITFDVPAGQVVALVGPSGAGKT----TLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRR- 432
Cdd:COG4172 13 SVAFGQGGGT---VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 ---QVGLVPQETL-----LFS-GT-VAENIL----YGRPGASQAeveaaahaahahefICELEggygAVVG----ERGVK 494
Cdd:COG4172 90 rgnRIAMIFQEPMtslnpLHTiGKqIAEVLRlhrgLSGAAARAR--------------ALELL----ERVGipdpERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 -----LSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMV------GRTTFVVAHRLSTIRS-ADRI 562
Cdd:COG4172 152 ayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 499192068 563 LVMDAGRVVADGTHEGLMAA 582
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
359-575 |
1.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYA-----GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA----LAD 429
Cdd:PRK13643 2 IKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 LRRQVGLVPQ--ETLLFSGTVAENILYGrpgaSQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIAR 507
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALERL-MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
373-579 |
1.67e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 83.60 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPRFWDV-----------TAGRVEVDGHDV--------RAYALA 428
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnalLLPDTGTIewifkdeknkkKTKEKEKVLEKLviqktrfkKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 429 DLRRQVGLVPQ--ETLLFSGTVAENILYGrP---GASQAEVEaaahaahaheficELEGGYGAVVG------ERG-VKLS 496
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PvsmGVSKEEAK-------------KRAAKYIELVGldesylQRSpFELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 497 GGQRQRVAIARAILKDPRILILDEATSALDNESealVQAALERL----MVGRTTFVVAHRL-STIRSADRILVMDAGRVV 571
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFdnlnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKII 244
|
....*....
gi 499192068 572 ADG-THEGL 579
Cdd:PRK13651 245 KDGdTYDIL 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-575 |
2.04e-17 |
|
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: 86.61 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 366 FTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyALADLRRQVGLVPQETLLFS 445
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 G-TVAENILYgrpgASQAEVEAAAHAAHAHEFICElEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:TIGR01257 1017 HlTVAEHILF----YAQLKGRSWEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499192068 525 LDNESEALVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGT 575
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
359-570 |
2.07e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.12 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAG-APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADlrRQVGLV 437
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLLFSG-TVAENILYG---RpGASQAEVEAAAHAAHAhefICELEggygAVVGERGVKLSGGQRQRVAIARAILKDP 513
Cdd:PRK11650 82 FQNYALYPHmSVRENMAYGlkiR-GMPKAEIEERVAEAAR---ILELE----PLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 514 RILILDEATSALDnesEAL-VQAALE------RLmvGRTTFVVAH-RLSTIRSADRILVMDAGRV 570
Cdd:PRK11650 154 AVFLFDEPLSNLD---AKLrVQMRLEiqrlhrRL--KTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-575 |
2.27e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH------DVRAYALADLRRQVGLVPQETLLFSG- 446
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TVAENILYgrPGASQAEVEAAAHAAHAHEfiCELEGGYGAVVGER----GVKLSGGQRQRVAIARAILKDPRILILDEAT 522
Cdd:PRK14246 106 SIYDNIAY--PLKSHGIKEKREIKKIVEE--CLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499192068 523 SALDNESEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGS 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
355-581 |
3.21e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 355 AEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAD----- 429
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 430 --------LRRQVGLVPQETLLFSG-TVAENILygrPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQR 500
Cdd:PRK10619 82 adknqlrlLRTRLTMVFQHFNLWSHmTVLENVM---EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 501 QRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEG 578
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQ 238
|
...
gi 499192068 579 LMA 581
Cdd:PRK10619 239 LFG 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-574 |
3.60e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.50 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDV-----TAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 -----PQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFIC-ELEGGYGAVVGergvKLSGGQRQRVAIARAILK 511
Cdd:PRK14247 88 fqipnPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWdEVKDRLDAPAG----KLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 512 DPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAH-RLSTIRSADRILVMDAGRVVADG 574
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
363-575 |
3.97e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.06 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGA------PALQDITFDVPAGQVVALVGPSGAGKTTLVN-----LIPrfwdvTAGRVEVDGHDVR-AYALADL 430
Cdd:PRK13633 9 NVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnalLIP-----SEGKVYVDGLDTSdEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 431 RRQVGLVPQ--ETLLFSGTVAENILYGrP---GASQAEVEAAAHAAHAHeficeleggygavVGERGVK------LSGGQ 499
Cdd:PRK13633 84 RNKAGMVFQnpDNQIVATIVEEDVAFG-PenlGIPPEEIRERVDESLKK-------------VGMYEYRrhaphlLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 500 RQRVAIARAILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRSADRILVMDAGRVVADGT 575
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
374-580 |
4.80e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR---AYALADLR-RQVGLVPQ-ETLLFSGTV 448
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklsSAAKAELRnQKLGFIYQfHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI----LYGRPGASQAEVEAAAHAAHAheficelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:PRK11629 105 LENVamplLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 525 LDNESEALVQAALERLMVGRTT--FVVAHRLSTIRSADRILVMDAGRVVADGTHEGLM 580
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE 233
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
111-334 |
6.01e-17 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 81.76 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 111 VVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPRLSLLTLAII 190
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 191 pLVIGTAVTI--GRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTG 268
Cdd:cd18585 146 -LLAGVVIPLlfYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 269 VMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIF 334
Cdd:cd18585 225 LMILLSGLTVWLVLWLGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
373-580 |
6.34e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLR----RQVGLVPQE-TLLFSGT 447
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 448 VAENILYGR--PGASQAEVEAAAHAAHAHEFICELEGGYGAvvgergvKLSGGQRQRVAIARAILKDPRILILDEATSAL 525
Cdd:PRK10070 123 VLDNTAFGMelAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 526 DNESEALVQAALERLMVG--RTTFVVAHRL-STIRSADRILVMDAGRVVADGTHEGLM 580
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
363-575 |
6.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAP-----ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRA-----YALADLRR 432
Cdd:PRK13645 11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVGLVPQ--ETLLFSGTVAENILYG--RPGASQAEVEAAAHAAHAhefICELEGGYgavVGERGVKLSGGQRQRVAIARA 508
Cdd:PRK13645 91 EIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 509 ILKDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
359-569 |
9.24e-17 |
|
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: 77.49 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVRAYAladlRRQVGLVP 438
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPDEGIVTWGS----TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QetllfsgtvaenilygrpgasqaeveaaahaahaheficeleggygavvgergvkLSGGQRQRVAIARAILKDPRILIL 518
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 519 DEATSALDNESealvQAALERLMVG--RTTFVVAH-R--LSTIrsADRILVMDAGR 569
Cdd:cd03221 95 DEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
368-577 |
1.20e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQvGLVP--QETLLF- 444
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SGTVAENILYGR---------------PGASQAEVEAAAHAAHAHEFIcelegGYGAVVGERGVKLSGGQRQRVAIARAI 509
Cdd:PRK11300 94 EMTVIENLLVAQhqqlktglfsgllktPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 510 LKDPRILILDEATSALD-NESEALVQAALE-RLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHE 577
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNpKETKELDELIAElRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPE 239
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
43-327 |
2.09e-16 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 79.96 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDAsfLKVGSTDTGPLDRTVLSLLGIFALSA-CFGAAQAYLLARVGAGVVADLRRALFS 121
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNA--LTLAKVKDLESAVTLILLYALLRFSSkLLKELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 122 HLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIG-SVLLLVQTSPRLSLLTLaiIPLVIGTAVTI 200
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVvSVVFAFHFGAWLALIVF--LSVLLYGVFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 201 GRRIRRVS--REVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGAL 278
Cdd:cd18560 158 KVTEWRTKfrRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499192068 279 ALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEAL 327
Cdd:cd18560 238 TLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
374-577 |
4.70e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 4.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLI---PRFwDVTAGRVEVDGHDV-------RAYAladlrrqvGLV-----P 438
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPKY-EVTSGSILLDGEDIlelspdeRARA--------GIFlafqyP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QEtllFSGTVAENILYGrpgASQAEVEAAAHAAHAHEFICEleggYGAVVG------ERGV--KLSGGQRQRVAIARAIL 510
Cdd:COG0396 87 VE---IPGVSVSNFLRT---ALNARRGEELSAREFLKLLKE----KMKELGldedflDRYVneGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAH--RLSTIRSADRILVMDAGRVVADGTHE 577
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
371-571 |
5.45e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 78.31 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 371 APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV----RAYALAdLRRQVGLVPQETLlfsG 446
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRRA-FRRDVQLVFQDSP---S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 TV-----AENILyGRPgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:TIGR02769 100 AVnprmtVRQII-GEP-LRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499192068 522 TSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRS-ADRILVMDAGRVV 571
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQqaFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
363-587 |
6.51e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYA-GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLrrqVGLVPQ-E 440
Cdd:PRK15056 11 DVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQsE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSGTV-AENIL----YGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRI 515
Cdd:PRK15056 88 EVDWSFPVlVEDVVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 516 LILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAAGGLYR 587
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLEL 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
352-593 |
8.77e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 8.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 352 LSRAEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLR 431
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 RQVGLVPQE-TLLFSGTVAENILYGRPgASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAIL 510
Cdd:PRK10253 81 RRIGLLAQNaTTPGDITVQELVARGRY-PHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAgGLYR 587
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTA-ELIE 238
|
....*.
gi 499192068 588 ELYELQ 593
Cdd:PRK10253 239 RIYGLR 244
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
44-333 |
1.01e-15 |
|
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: 78.01 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 44 LATLISSGLGLVFPRLFGTLIDasflKV-GSTDTGPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18566 9 LASLFINILALATPLFILQVYD----RViPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLTsDVGTV-QAVTSTALAQLASQGFTLIGSVLLLVqTSPRLSLLTLAIIPLVIGTAVTIG 201
Cdd:cd18566 85 LLSLPLSFFEREPSGAHLERLN-SLEQIrEFLTGQALLALLDLPFVLIFLGLIWY-LGGKLVLVPLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 202 RRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEEERY----GQGVLASFRAALRRARLQALMTGVMSfltfGA 277
Cdd:cd18566 163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYerlqANAAYAGFKVAKINAVAQTLGQLFSQ----VS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 278 LALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18566 239 MVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
384-575 |
1.33e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVNLIPrFWDVT----AGRVEVDGHDVRAyalADLRRQVGLVPQETLLF-SGTVAENILYGRPG 458
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIpTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 459 ASQAEVEAAAHAAHAHEFICELEGGYGA--VVGERGVK--LSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQ 534
Cdd:TIGR00955 127 RMPRRVTKKEKRERVDEVLQALGLRKCAntRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499192068 535 AALERL-MVGRTTFVVAHRLST--IRSADRILVMDAGRVVADGT 575
Cdd:TIGR00955 207 QVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
36-333 |
1.50e-15 |
|
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: 77.52 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 36 RLPFVLGVLATLISSGLGLVFP---RLFgtlIDaSFLkvgstdTGPLDRTVLSLLGIFALSACFGAA----QAYLLARVG 108
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPvfsRIF---ID-DIL------VGGLPDWLRPLLLGMALTALLQGLltwlQQYYLLRLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 109 AGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTaLAQLASQGFTLIGSVLLLVQTSPRLSLLTLA 188
Cdd:cd18569 71 TKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQ-LATTVLNLVMAVFYALLMLQYDVPLTLIGIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 189 IIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAeeaISGVRVVQSFTAEGLEEERYGQ--GVLASFRAALRR-ARLQAL 265
Cdd:cd18569 150 IALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTT---MSGLQMIETLKASGAESDFFSRwaGYQAKVLNAQQElGRTNQL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 266 MTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18569 227 LGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
324-566 |
1.76e-15 |
|
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: 79.79 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 324 QEALGASSRIFELLD--------------ERSDLPGPAAPRPLSRAEGR--VRFVDVGF--------TYAGAPALQDITF 379
Cdd:TIGR00954 394 TRLAGFTARVDTLLQvlddvksgnfkrprVEEIESGREGGRNSNLVPGRgiVEYQDNGIkfeniplvTPNGDVLIESLSF 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 380 DVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYaladlrrqvglVPQETLLFSGTVAENILY----- 454
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY-----------VPQRPYMTLGTLRDQIIYpdsse 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 455 --GRPGASQAEVEAAAHAAHAHeFICELEGGYGAVVGERGVkLSGGQRQRVAIARAILKDPRILILDEATSALDNESE-A 531
Cdd:TIGR00954 543 dmKRRGLSDKDLEQILDNVQLT-HILEREGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEgY 620
|
250 260 270
....*....|....*....|....*....|....*
gi 499192068 532 LVQAALErlmVGRTTFVVAHRLSTIRSADRILVMD 566
Cdd:TIGR00954 621 MYRLCRE---FGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
363-581 |
1.77e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA---LADLRRQVGLVPQ 439
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 ETLLFSG-TVAENILYGRPGASQAEVEAAAHAAhahefICELEGgygavVGERGV------KLSGGQRQRVAIARAILKD 512
Cdd:PRK11831 92 SGALFTDmNVFDNVAYPLREHTQLPAPLLHSTV-----MMKLEA-----VGLRGAaklmpsELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 513 PRILILDEATSALDNESEALVQAALERL--MVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
384-602 |
2.01e-15 |
|
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: 76.29 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVRAyaladLRRQVGLVPQE-TLLFSGTVaENILYGRpgasqa 462
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEI-----ELDTVSYKPQYiKADYEGTV-RDLLSSI------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 463 eveaAAHAAHAHEFICE------LEGGYGAVVGErgvkLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAA 536
Cdd:cd03237 86 ----TKDFYTHPYFKTEiakplqIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 537 LERLMVG--RTTFVVAHRLSTIRS-ADRILVMDaGRVVADGTHEGLMA-AGGLYRELYELQ--FRQQQEARR 602
Cdd:cd03237 158 IRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGVANPPQSlRSGMNRFLKNLDitFRRDPETGR 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
374-568 |
2.70e-15 |
|
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: 74.59 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVnliprfwDVTAGRVE---------VDGHDVRayalADLRRQVGLVPQETLLF 444
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLL-------DVLAGRKTagvitgeilINGRPLD----KNFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SG-TVAENILygrpgasqaeveaaahaahaheFICELEGgygavvgergvkLSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:cd03232 92 PNlTVREALR----------------------FSALLRG------------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499192068 524 ALDNESEALVQAALERL-MVGRTTFVVAHRLS--TIRSADRILVMDAG 568
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
377-602 |
3.07e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 377 ITFDVPAGQVVALVGPSGAGKTTLV----NLIPrfwdvTAGRVEVDGHDVRAYALADLRRQVG-LVPQETLLFSGTVAEN 451
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLLP-----GSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 452 I-LYGRPGASqaeveaAAHAAHAHEFICELeggygavVG-----ERGV-KLSGGQRQRVAIARAILK-DPRI------LI 517
Cdd:PRK03695 90 LtLHQPDKTR------TEAVASALNEVAEA-------LGlddklGRSVnQLSGGEWQRVRLAAVVLQvWPDInpagqlLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSALDNESealvQAALERLMV-----GRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMAAGGLyRELYE 591
Cdd:PRK03695 157 LDEPMNSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFG 231
|
250
....*....|.
gi 499192068 592 LQFRQQQEARR 602
Cdd:PRK03695 232 VNFRRLDVEGH 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
347-574 |
3.15e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.73 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 347 AAPRPLSRAEGRVRFvdvgftYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA 426
Cdd:PRK11701 1 MMDQPLLSVRGLTKL------YGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 427 LADLRRqvglvPQETLLFS---GTVAENILYG-RPGASQaeveaaahaahaheficeleggyGAVVGER----GVK---- 494
Cdd:PRK11701 75 LYALSE-----AERRRLLRtewGFVHQHPRDGlRMQVSA-----------------------GGNIGERlmavGARhygd 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 -------------------------LSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMVGRTT--- 546
Cdd:PRK11701 127 iratagdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelg 202
|
250 260 270
....*....|....*....|....*....|..
gi 499192068 547 ---FVVAHRLSTIR-SADRILVMDAGRVVADG 574
Cdd:PRK11701 203 lavVIVTHDLAVARlLAHRLLVMKQGRVVESG 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
361-581 |
3.81e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 361 FVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI---PRfwdVTAGRVEVDGHDVRAYALADLRRQ-VGL 436
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 437 VPQETLLFSG-TVAENILYGRPGASQAEVEAAAHAahahefICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 516 LILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLS-TIRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-574 |
4.33e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.29 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 355 AEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR------AYALA 428
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkldhklAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 429 dlrrqVGLVPQE-TLLFSGTVAENILYGRP------GASQAEVEAAAHAAHAHEFICELEGGYGAVVGErgvkLSGGQRQ 501
Cdd:PRK09700 82 -----IGIIYQElSVIDELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 502 RVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
359-584 |
5.14e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR-AYALADLRRQVGLV 437
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdARHRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQ-------ETLlfsgTVAENI-----LYGRPGASQAEVeaaahaahahefICELEGGYG-AVVGERGV-KLSGGQRQRV 503
Cdd:NF033858 82 PQglgknlyPTL----SVFENLdffgrLFGQDAAERRRR------------IDELLRATGlAPFADRPAgKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 504 AIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRT--TFVVAhrlstirSA--------DRILVMDAGRVVAD 573
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA-------TAymeeaerfDWLVAMDAGRVLAT 218
|
250
....*....|.
gi 499192068 574 GTHEGLMAAGG 584
Cdd:NF033858 219 GTPAELLARTG 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-582 |
5.24e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.75 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI----PRfwdvTAGRVEVDGHDVRAYALAD-LRRQVGLVP----QE 440
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgadPA----DSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSGTVAENIL------YGRPGasqaEVEAAAHAAHAHEFICELE---GGYGAVVGErgvkLSGGQRQRVAIARAILK 511
Cdd:COG1129 340 GLVLDLSIRENITlasldrLSRGG----LLDRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 512 DPRILILDEATSALD----NESEALVQAALERlmvGRTTFVVahrlST-----IRSADRILVMDAGRVVA-----DGTHE 577
Cdd:COG1129 412 DPKVLILDEPTRGIDvgakAEIYRLIRELAAE---GKAVIVI----SSelpelLGLSDRILVMREGRIVGeldreEATEE 484
|
....*
gi 499192068 578 GLMAA 582
Cdd:COG1129 485 AIMAA 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
373-581 |
7.67e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEV-----------DGHDVRAYAladlRRQVGLVPQET 441
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRA----KRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 LLFS-GTVAENIL--YGRPGASQAEVEAAAHAAHAHEFIcelEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:TIGR03269 375 DLYPhRTVLDNLTeaIGLELPDELARMKAVITLKMVGFD---EEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 519 DEATSALDNESEALVQAAL--ERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMA 581
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
373-577 |
2.21e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.33 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH------------DVR------AYAL------- 427
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckHIRmifqdpNTSLnprlnig 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 428 ----ADLRRQVGLVPQE-------TLLFSGTVAENILYGRPgasqaeveaaahaahaheficeleggygavvgergvKLS 496
Cdd:COG4167 108 qileEPLRLNTDLTAEEreerifaTLRLVGLLPEHANFYPH------------------------------------MLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 497 GGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMV------GRTTFVVAHRLSTIRS-ADRILVMDAGR 569
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALD----MSVRSQIINLMLelqeklGISYIYVSQHLGIVKHiSDKVLVMHQGE 227
|
....*....
gi 499192068 570 VVADG-THE 577
Cdd:COG4167 228 VVEYGkTAE 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
374-575 |
2.75e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAD---LRRQVGLVPQETLlfsGTVAE 450
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSI---SAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPGASQAEVEAAAHAAHAHEFICELEGGYG---AVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDN 527
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDlddSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499192068 528 ESEALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADGT 575
Cdd:PRK10419 185 VLQAGVIRLLKKLQqqFGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQP 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
370-584 |
3.45e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQ-VGLVPQETLLF---- 444
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvp 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVK---LSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:COG3845 350 DMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTParsLSGGNQQKVILARELSRDPKLLIAAQP 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499192068 522 TSALDNESEALVQAAL-ERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVV-----ADGTHE--GLMAAGG 584
Cdd:COG3845 430 TRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgevpaAEATREeiGLLMAGV 501
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
367-572 |
9.39e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRF-----WDvtaGRVEVDGHDVRAYALADLRRQ-VGLVPQE 440
Cdd:PRK13549 14 TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtYE---GEIIFEGEELQASNIRDTERAgIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICELegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILD 519
Cdd:PRK13549 91 LALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 520 EATSALdNESEALVQAALERLMV--GRTTFVVAHRLSTIRS-ADRILVMDAGRVVA 572
Cdd:PRK13549 169 EPTASL-TESETAVLLDIIRDLKahGIACIYISHKLNEVKAiSDTICVIRDGRHIG 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
373-591 |
1.08e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR---AYALADLRRQVGLVPQETL------- 442
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkDDEWRAVRSDIQMIFQDPLaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 LFSGTVAENILYGRPGASQAeveaaahaahaheficELEGGYGAVVGERGV----------KLSGGQRQRVAIARAILKD 512
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSRQ----------------EVKDRVKAMMLKVGLlpnlinryphEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 513 PRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTheglmaagglYREL 589
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQreMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT----------YDEV 249
|
..
gi 499192068 590 YE 591
Cdd:PRK15079 250 YH 251
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
367-590 |
1.19e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQ-VGLVPQE-TLLF 444
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQElNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 445 SGTVAENILYGRpgasqaeveaaahaahaheficELEGGYGAV-------------------------VGErgvkLSGGQ 499
Cdd:PRK10762 93 QLTIAENIFLGR----------------------EFVNRFGRIdwkkmyaeadkllarlnlrfssdklVGE----LSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 500 RQRVAIARAILKDPRILILDEATSAL-DNESEALVQAALERLMVGRTTFVVAHRLSTI-RSADRILVMDAG-----RVVA 572
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGqfiaeREVA 226
|
250 260
....*....|....*....|
gi 499192068 573 DGTHEGL--MAAGGLYRELY 590
Cdd:PRK10762 227 DLTEDSLieMMVGRKLEDQY 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
374-568 |
1.63e-13 |
|
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: 70.19 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyalADLRRQVglVPQE-TLLFSGTVAENI 452
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE---PGPDRMV--VFQNySLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 LYG----RPGASQAEVEAAAHAAHAHEficelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDne 528
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEEHIALV-------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD-- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499192068 529 seALVQAAL-ERLM-----VGRTTFVVAHRL-STIRSADRILVMDAG 568
Cdd:TIGR01184 147 --ALTRGNLqEELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
373-582 |
2.86e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTT----LVNLIPrfwdvTAGRVEVDG---HDVRAYALADLRRQVGLVPQET---- 441
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGqplHNLNRRQLLPVRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 ---LLFSGTVAENILYGRPGASQAEVEAAAHAAHAheficelEGGYGAVVGER-GVKLSGGQRQRVAIARAILKDPRILI 517
Cdd:PRK15134 376 nprLNVLQIIEEGLRVHQPTLSAAQREQQVIAVME-------EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 518 LDEATSALDNESEALVQAALERLMVGR--TTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
367-571 |
4.34e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNliprfwdVTAG---------RVEVDGHDVRayaLADLR--RQVG 435
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMK-------VLSGvyphgsyegEILFDGEVCR---FKDIRdsEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LV--PQETLLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICE--LEGGYGAVVGERGVklsgGQRQRVAIARAIL 510
Cdd:NF040905 80 IViiHQELALIPYlSIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 511 KDPRILILDEATSAL-DNESEALVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRVV 571
Cdd:NF040905 156 KDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTI 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
367-585 |
6.83e-13 |
|
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: 71.01 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 367 TYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRF-----WDvtaGRVEVDGHDVRAYALADLRRQ-VGLVPQE 440
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtWD---GEIYWSGSPLKASNIRDTERAgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 -TLLFSGTVAENILYGR----PGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGvklsGGQRQRVAIARAILKDPRI 515
Cdd:TIGR02633 87 lTLVPELSVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 516 LILDEATSAL-DNESEALVQAALERLMVGRTTFVVAHRLSTIRSadrilVMDAGRVVADGTHEGLMAAGGL 585
Cdd:TIGR02633 163 LILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKA-----VCDTICVIRDGQHVATKDMSTM 228
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
86-333 |
9.32e-13 |
|
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: 69.23 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 86 LLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLAsqg 165
Cdd:cd18561 42 IAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 166 FTLIGSVLLLVQTSPR---LSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEGLEE 242
Cdd:cd18561 119 VALLGPLLILIYLFFLdplVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 243 ERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQ 322
Cdd:cd18561 199 NELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHA 278
|
250
....*....|.
gi 499192068 323 FQEALGASSRI 333
Cdd:cd18561 279 GYQGISAADSI 289
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
370-539 |
1.32e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGlvPQETLLFSGTVA 449
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 450 ENI-----LYGRPGASQAEVEAAAHAAHahefICELEGGYgavvgergvkLSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:PRK13539 92 ENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*
gi 499192068 525 LDNESEALVQAALER 539
Cdd:PRK13539 158 LDAAAVALFAELIRA 172
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-569 |
2.51e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.62 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 33 RPYRLPFVLGVLATLISSGLG---LVFprlfgtlIDASFLKVGSTDTGPLDRTVLSLLGIFALSAcfgAAQAYLLArVGA 109
Cdd:PRK10522 9 RQYRWPFISVMALSLASAALGiglIAF-------INQRLIETADTSLLVLPEFLGLLLLLMAVTL---GSQLALTT-LGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 110 GVVADLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVqavtSTALAQLAS--QGFTL-IGSVLLLVQTSPRLSLLT 186
Cdd:PRK10522 78 HFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNI----TIAFVRLPElvQGIILtLGSAAYLAWLSPKMLLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 187 LAIIPLVIGTAVTIGRRIRR---VSREVQDAV-----AAANGQAEEAISGVRvvqsftAEGLEEERYGQGVLAsFRAALR 258
Cdd:PRK10522 154 AIWMAVTIWGGFVLVARVYKhmaTLRETEDKLyndyqTVLEGRKELTLNRER------AEYVFENEYEPDAQE-YRHHII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 259 RARLQALMTGVMS-FLTFGALALVLWfggrqvMSGALTPGNL-------VTFLFYALQVGGTVAALTGVFNQfQEALGAS 330
Cdd:PRK10522 227 RADTFHLSAVNWSnIMMLGAIGLVFY------MANSLGWADTnvaatysLTLLFLRTPLLSAVGALPTLLSA-QVAFNKL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 331 SRiFELLDERSDLPGPAAPRPLSRAEGRvrfvDVGFTY-AGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWD 409
Cdd:PRK10522 300 NK-LALAPYKAEFPRPQAFPDWQTLELR----NVTFAYqDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 410 VTAGRVEVDGHDVRAYALADLRRQVGLVPQETLLFsgtvaENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYGAvvg 489
Cdd:PRK10522 375 PQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-----DQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRIS--- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 490 erGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRSADRILVMDA 567
Cdd:PRK10522 447 --NLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMRN 524
|
..
gi 499192068 568 GR 569
Cdd:PRK10522 525 GQ 526
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
359-581 |
5.79e-12 |
|
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: 68.29 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRF--WDVTAGRV--------------------- 415
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 416 ------------EVDGHDVRAYALADLRRQVGLVPQETLLFSG--TVAENILYGRPgasQAEVEAAAHAAHAHEFICELE 481
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALE---EIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 482 GGYGAVVGERgvKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTIRS- 558
Cdd:TIGR03269 158 LSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDl 235
|
250 260
....*....|....*....|...
gi 499192068 559 ADRILVMDAGRVVADGTHEGLMA 581
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
370-571 |
8.04e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.59 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTL----VNLIPRFWDVTaGRVEVDGHDVRAYAlADLRRQVGLVPQETLLFS 445
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSVE-GDIHYNGIPYKEFA-EKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 G-TVAENIlygrpgasqaeveaaahaahahEFICELEGGygAVVgeRGVklSGGQRQRVAIARAILKDPRILILDEATSA 524
Cdd:cd03233 97 TlTVRETL----------------------DFALRCKGN--EFV--RGI--SGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 525 LDNESealvqaALERLMVGRTtfvVAH--RLSTIRSA-----------DRILVMDAGRVV 571
Cdd:cd03233 149 LDSST------ALEILKCIRT---MADvlKTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
374-581 |
8.16e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEvdGHDVRAYALADLR-------RQVGLVPQETLLFSG 446
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQ--GNNFTGTILANNRkptkqilKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 -TVAENILYGRPGASQAEVEAAAHAAHAHEFICEL--EGGYGAVVGE---RGVklSGGQRQRVAIARAILKDPRILILDE 520
Cdd:PLN03211 155 lTVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 521 ATSALDNESE-ALVQAALERLMVGRTTFVVAHRLST--IRSADRILVMDAGRVVADGTHEGLMA 581
Cdd:PLN03211 233 PTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
368-582 |
9.37e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.49 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAGAPALQDITFDVPAGQVVALVGPSGAGKT----TLVNLIPRFWDVTAGRVEVDGhdvRAYALADLR-RQVGLVPQ--- 439
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRgRKIATIMQnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 --------------ETLLFSGtvaenilygRPGASQAEVEAAAHAAHAHEficeleggyGAVVGERGVKLSGGQRQRVAI 505
Cdd:PRK10418 90 safnplhtmhtharETCLALG---------KPADDATLTAALEAVGLENA---------ARVLKLYPFEMSGGMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 506 ARAILKDPRILILDEATSALDNESEALVQAALERLMVGRT--TFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
40-335 |
1.01e-11 |
|
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: 65.99 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 40 VLGVLATLISSGLGLVFPRLFGTLidasFLKVGSTDTGPLDRTVLS--LLGIFALSACFGAAQAYLLARVGAGVVADLRR 117
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDW----WSSDWSSSPNSSSGYYLGvyAALLVLASVLLVLLRWLLFVLAGLRASRRLHD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 118 ALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPrlslLTLAIIPLVIGTA 197
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 198 VTIGRRIRRVSREVQ--DAVAAA--NGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRA-----ALRRA---RLQAL 265
Cdd:cd18580 153 YLLQRYYLRTSRQLRrlESESRSplYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAfylllAVQRWlglRLDLL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 266 MTGVMSFLTFGALALvlwfggrqvmSGALTPGNLVTFLFYALQVGGTVAALTGVFNQFQEALGASSRIFE 335
Cdd:cd18580 233 GALLALVVALLAVLL----------RSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILE 292
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-574 |
2.47e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.09 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 362 VDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTA-----GRVEVDGHDVRAYAL--ADLRRQV 434
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVdpIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQETLLFSG-TVAENILYGrpgasqAEVEAAAHAAHAHEFICELEGGYGAVVGErgVK---------LSGGQRQRVA 504
Cdd:PRK14267 88 GMVFQYPNPFPHlTIYDNVAIG------VKLNGLVKSKKELDERVEWALKKAALWDE--VKdrlndypsnLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 505 IARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHR-LSTIRSADRILVMDAGRVVADG 574
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
362-560 |
2.54e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 362 VDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyALADLRRQVGLVPQET 441
Cdd:PRK13540 5 IELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 LLFSG-TVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGYgavvgergvkLSGGQRQRVAIARAILKDPRILILDE 520
Cdd:PRK13540 84 GINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499192068 521 ATSALDNES-EALVQAALERLMVGRTTFVVAHRLSTIRSAD 560
Cdd:PRK13540 154 PLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
364-577 |
3.84e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 364 VGFTYAGAP--ALQDITFDVPAGQVVALVGPSGAGKT----TLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:PRK11022 11 VHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 -------PQETLLFSGTVAENILYGrpgasqaeveaaahaahahefICELEGGYGAVVGERGV----------------- 493
Cdd:PRK11022 91 vamifqdPMTSLNPCYTVGFQIMEA---------------------IKVHQGGNKKTRRQRAIdllnqvgipdpasrldv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 ---KLSGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLMV------GRTTFVVAHRLSTI-RSADRIL 563
Cdd:PRK11022 150 yphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD----VTIQAQIIELLLelqqkeNMALVLITHDLALVaEAAHKII 225
|
250
....*....|....
gi 499192068 564 VMDAGRVVADGTHE 577
Cdd:PRK11022 226 VMYAGQVVETGKAH 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
363-574 |
5.53e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH--DVRAYALADLRRQVGLVPQ- 439
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 -ETLLFSGTVAENILYG--RPGASQAEVEAAAHAAHaheficeleggygAVVGERGVK------LSGGQRQRVAIARAIL 510
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlrNLGVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG 574
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
494-582 |
6.65e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTIRS-ADRILVMDAGRV 570
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
90
....*....|..
gi 499192068 571 VADGTHEGLMAA 582
Cdd:PRK15134 236 VEQNRAATLFSA 247
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
384-569 |
8.99e-11 |
|
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: 60.46 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVNLIPRFWDVTAGRV-EVDGHDVRAYALADLRrqvglvpqetllfsgtvaenilygrpgasqa 462
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 463 eveaaahaahaheficeleggyGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM- 541
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499192068 542 ------VGRTTFVVAHRLSTIRSA------DRILVMDAGR 569
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
374-568 |
1.23e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVN-LIPRfwdVTAGRVEVDGHDVRAYAL-ADLRRQVGLVPQETL-LFSGTVAE 450
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER---VTTGVITGGDRLVNGRPLdSSFQRSIGYVQQQDLhLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYG----RPgaSQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILI-LDEATSAL 525
Cdd:TIGR00956 856 SLRFSaylrQP--KSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499192068 526 DNESEALVQAALERLM-VGRTTFVVAHRLSTIRSA--DRILVMDAG 568
Cdd:TIGR00956 934 DSQTAWSICKLMRKLAdHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
496-575 |
1.71e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 496 SGGQRQRVAIARAILKDPRILILDEATSALDneseALVQAALERLM------VGRTTFVVAHRLSTIR-SADRILVMDAG 568
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALD----VTVQAQIMTLLnelkreFNTAIIMITHDLGVVAgICDKVLVMYAG 238
|
....*..
gi 499192068 569 RVVADGT 575
Cdd:PRK09473 239 RTMEYGN 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
360-584 |
2.47e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 360 RFVDvgFTyagapALQDITFDVPAGQVVALVGPSGAGKTT----LVNLIPrfwdVTAGRVEVDGHDVRAYALAdLRRQVG 435
Cdd:NF033858 275 RFGD--FT-----AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWLFGQPVDAGDIA-TRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 436 LVPQETLLFSG-TVAENI-----LYGRPGASQAEVeaaahaahahefICELEGGYG--AVVGERGVKLSGGQRQRVAIAR 507
Cdd:NF033858 343 YMSQAFSLYGElTVRQNLelharLFHLPAAEIAAR------------VAEMLERFDlaDVADALPDSLPLGIRQRLSLAV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 508 AILKDPRILILDEATS-----ALDNESEALVQAALERlmvGRTTFVVAHRLSTIRSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:NF033858 411 AVIHKPELLILDEPTSgvdpvARDMFWRLLIELSRED---GVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
..
gi 499192068 583 GG 584
Cdd:NF033858 488 RG 489
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
359-582 |
2.48e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAP--ALQDITFDVPAGQVVALVGPSGAGKTTLVNLI----PRFWDVTAGRVEVDGHDVRAYALADLRR 432
Cdd:PRK15093 6 IRNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 433 QVG-------LVPQETLLFSGTVAENILYGRPGASQAEVEAAAHAAHAHEFIcELEGGYG-----AVVGERGVKLSGGQR 500
Cdd:PRK15093 86 LVGhnvsmifQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAI-ELLHRVGikdhkDAMRSFPYELTEGEC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 501 QRVAIARAILKDPRILILDEATSALdnesEALVQAALERLMV------GRTTFVVAHRLSTIRS-ADRILVMDAGRVVAD 573
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAM----EPTTQAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVET 240
|
....*....
gi 499192068 574 GTHEGLMAA 582
Cdd:PRK15093 241 APSKELVTT 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
384-566 |
3.26e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVrayaLADLRrqVGLVPQE-TLLFSGTVAENIlygrpgASQA 462
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEV----DPELK--ISYKPQYiKPDYDGTVEDLL------RSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 463 EVEAAAHAAHAHEFICELEGGYgavvgERGVK-LSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLM 541
Cdd:PRK13409 426 DDLGSSYYKSEIIKPLQLERLL-----DKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIA 500
|
170 180
....*....|....*....|....*...
gi 499192068 542 VGR--TTFVVAHRLSTIRS-ADRILVMD 566
Cdd:PRK13409 501 EEReaTALVVDHDIYMIDYiSDRLMVFE 528
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
370-538 |
3.42e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.68 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdvrayALADLRRQvglvPQETLLFSG--- 446
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-----PLAEQRDE----PHENILYLGhlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 ------TVAENIlygrpgasqaeveaaahaahahEFICELEGGYG-------AVVGERGVK------LSGGQRQRVAIAR 507
Cdd:TIGR01189 83 glkpelSALENL----------------------HFWAAIHGGAQrtiedalAAVGLTGFEdlpaaqLSAGQQRRLALAR 140
|
170 180 190
....*....|....*....|....*....|.
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALE 538
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-566 |
4.50e-10 |
|
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: 62.49 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVRAyalaDLRrqVGLVPQE-TLLFSGTVAENilygrpgasqa 462
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDE----DLK--ISYKPQYiSPDYDGTVEEF----------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 463 eveaaahaahaheficeLEGGYGAVVG------------------ERGVK-LSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:COG1245 422 -----------------LRSANTDDFGssyykteiikplglekllDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499192068 524 ALDNESEALVQAALERLMVGR--TTFVVAHRLSTIRS-ADRILVMD 566
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
373-574 |
4.97e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV---RAYALADLRRQV---------GLVPQE 440
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIqfifqdpyaSLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 TLLFS---GTVAENILYGRPGASQaeveaaahaahaHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILI 517
Cdd:PRK10261 419 TVGDSimePLRVHGLLPGKAAAAR------------VAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 518 LDEATSALDNESEALVQAALERLM--VGRTTFVVAHRLSTI-RSADRILVMDAGRVVADG 574
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQrdFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
359-526 |
6.41e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHdvrayaladLRrqVGLVP 438
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSG---TVaENILYGRPGASQAEVEAAAHAAHAheficeleggyGAVVGERGVKLSGGQRQRVAIARAILKDPRI 515
Cdd:PRK09544 74 QKLYLDTTlplTV-NRFLRLRPGTKKEDILPALKRVQA-----------GHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 499192068 516 LILDEATSALD 526
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
374-580 |
6.51e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLI---------PRFWDVTaGRVEVDGHDVRAYALADLRRQVGLVPQETL-L 443
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARVT-GDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 444 FSGTVAENILYGRPGASQAEVEAAAHAAHAHEFICELEGGyGAVVGERGVKLSGGQRQRVAIARAILK---------DPR 514
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 515 ILILDEATSALDNESEALVQAALERLM----VGRTTFVVAHRLSTiRSADRILVMDAGRVVADGTHEGLM 580
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLArdwnLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
349-570 |
7.34e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 349 PRPLSRAEGRV-RFVDVGFTYAGAPAL-QDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRV----------- 415
Cdd:PLN03073 498 PTPDDRPGPPIiSFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavf 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 416 ---EVDGHDVRAYALADLRRQVGLVPQETL---LFSGTVAENIlygrpgasqaeveaaahaahaheficELEGGYgavvg 489
Cdd:PLN03073 578 sqhHVDGLDLSSNPLLYMMRCFPGVPEQKLrahLGSFGVTGNL--------------------------ALQPMY----- 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 490 ergvKLSGGQRQRVAIARAILKDPRILILDEATSALDNES-EALVQAALerLMVGrTTFVVAHRLSTIR-SADRILVMDA 567
Cdd:PLN03073 627 ----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISgSVDELWVVSE 699
|
...
gi 499192068 568 GRV 570
Cdd:PLN03073 700 GKV 702
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
43-221 |
7.41e-10 |
|
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: 60.12 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDASFLKVGSTDtgPLDRTVLSLLGIFALSACFGAAQAYLLARVGAGVVADLRRALFSH 122
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGAGLA--ALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 123 LLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASqgfTLIGSVLLLVQTSPR--LSLLTLAI-IPLVIGTAVT 199
Cdd:cd18584 80 LLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVL---AAIVPLLILVAVFPLdwVSALILLVtAPLIPLFMIL 156
|
170 180
....*....|....*....|..
gi 499192068 200 IGRRIRRVSREVQDAVAAANGQ 221
Cdd:cd18584 157 IGKAAQAASRRQWAALSRLSGH 178
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
377-537 |
7.74e-10 |
|
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: 59.04 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 377 ITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDG------HDVRAYALADLRRQVGLvpqETLLfsgTVAE 450
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYLGHAPGI---KTTL---SVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NILYGRPgasqaeveaaahaahahefICELEGGYGAV--VGERGVK------LSGGQRQRVAIARAILKDPRILILDEAT 522
Cdd:cd03231 93 NLRFWHA-------------------DHSDEQVEEALarVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170
....*....|....*
gi 499192068 523 SALDNESEALVQAAL 537
Cdd:cd03231 154 TALDKAGVARFAEAM 168
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
374-529 |
1.11e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAY---ALADLR-RQVGLVPQETLLFSGTVA 449
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 450 -ENI-----LYGRPGASQAEVEAAAHAAHaheficelegGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATS 523
Cdd:PRK10584 106 lENVelpalLRGESSRQSRNGAKALLEQL----------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
....*.
gi 499192068 524 ALDNES 529
Cdd:PRK10584 176 NLDRQT 181
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
83-333 |
1.81e-09 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 59.15 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 83 VLSLLGIFALSACFGAAQ--AYLLARVGAGVVADLRRALFSHLLSLSPRFfgnhRTGDLTSRLTSDVGTV-QAVTSTALA 159
Cdd:cd18586 43 GLTLGMVVLLAFDGLLRQvrSRILQRVGLRLDVELGRRVFRAVLELPLES----RPSGYWQQLLRDLDTLrNFLTGPSLF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 160 QLASQGFTLIGSVLLLVqTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFTAEG 239
Cdd:cd18586 119 AFFDLPWAPLFLAVIFL-IHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 240 LEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGV 319
Cdd:cd18586 198 NLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGA 277
|
250
....*....|....
gi 499192068 320 FNQFQEALGASSRI 333
Cdd:cd18586 278 WKQLSAARQAYERL 291
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
372-550 |
1.86e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPR--FWDVTAGRVEVDGHDV-RAYALADLRRQVGLVPQET-LLFSGT 447
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFgREASLIDAIGRKGDFKDAVeLLNAVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 448 VAENILYGRPGAsqaeveaaahaahaheficeleggygavvgergvKLSGGQRQRVAIARAILKDPRILILDEATSALDN 527
Cdd:COG2401 124 LSDAVLWLRRFK----------------------------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....
gi 499192068 528 ESEALVQAALERLM-VGRTTFVVA 550
Cdd:COG2401 170 QTAKRVARNLQKLArRAGITLVVA 193
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
374-575 |
2.07e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVnliprfwDVTAGRvevdghDVRAYALADLRRQVGLVPQETLL-FSG------ 446
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGR------KTGGYIEGDIRISGFPKKQETFArISGyceqnd 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 ------TVAENILYgrpgASQAEVEAAAHAAHAHEFI------CELEGGYGAVVGERGVK-LSGGQRQRVAIARAILKDP 513
Cdd:PLN03140 963 ihspqvTVRESLIY----SAFLRLPKEVSKEEKMMFVdevmelVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANP 1038
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 514 RILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLS--TIRSADRILVMD-AGRVVADGT 575
Cdd:PLN03140 1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSidIFEAFDELLLMKrGGQVIYSGP 1104
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
384-582 |
2.58e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.15 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKT----TLVNLIPRFWDVTAGRVEVDGHDVRAYALADLR----RQVGLV---PQETLLFSGTVAENI 452
Cdd:COG4170 33 GEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRkiigREIAMIfqePSSCLDPSAKIGDQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 LYGRPGAsqaeveaaahaahaheficELEGGYGAVVGER-----------GVK------------LSGGQRQRVAIARAI 509
Cdd:COG4170 113 IEAIPSW-------------------TFKGKWWQRFKWRkkraiellhrvGIKdhkdimnsypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 510 LKDPRILILDEATSALdnesEALVQAALERLMV------GRTTFVVAHRLSTI-RSADRILVMDAGRVVADGTHEGLMAA 582
Cdd:COG4170 174 ANQPRLLIADEPTNAM----ESTTQAQIFRLLArlnqlqGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
348-577 |
5.07e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 348 APRPLsraeGRVRFVDVGFTyagAPAL-QDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYA 426
Cdd:PRK11288 249 RPRPL----GEVRLRLDGLK---GPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 427 LAD-LRRQVGLVP----QETLLFSGTVAENI-LYGRPGASqaeveaaahaahahEFICELEGGYGAVVGERGVK------ 494
Cdd:PRK11288 322 PRDaIRAGIMLCPedrkAEGIIPVHSVADNInISARRHHL--------------RAGCLINNRWEAENADRFIRslnikt 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 ---------LSGGQRQRVAIARAILKDPRILILDEATSALD----NESEALVQAALERlmvGRTTFVVAHRLSTIRS-AD 560
Cdd:PRK11288 388 psreqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgakHEIYNVIYELAAQ---GVAVLFVSSDLPEVLGvAD 464
|
250
....*....|....*..
gi 499192068 561 RILVMDAGRVVADGTHE 577
Cdd:PRK11288 465 RIVVMREGRIAGELARE 481
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
375-539 |
5.77e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 375 QDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlADLRRQvglvpqetLLFSG-------- 446
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQD--------LLYLGhqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 447 -TVAENIlygrpgasqaeveaaahaahahEFICELEGGYG--------AVVGERGVK------LSGGQRQRVAIARAILK 511
Cdd:PRK13538 89 lTALENL----------------------RFYQRLHGPGDdealwealAQVGLAGFEdvpvrqLSAGQQRRVALARLWLT 146
|
170 180
....*....|....*....|....*...
gi 499192068 512 DPRILILDEATSALDNESEALVQAALER 539
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-570 |
6.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKT----TLVNLIPrfwdVTAGRVEVDGHDVRAYALADlRRQVGLV------PQETLLFS 445
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTelaeTLYGLRP----ARGGRIMLNGKEINALSTAQ-RLARGLVylpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 446 GTVAENI---LYGRPGASqaeveaaahaahaheficeLEGGYGAVVGER-----GVK----------LSGGQRQRVAIAR 507
Cdd:PRK15439 356 APLAWNVcalTHNRRGFW-------------------IKPARENAVLERyrralNIKfnhaeqaartLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 508 AILKDPRILILDEATSALDNESEALVQAALERLMVGRTT--FVVAHRLSTIRSADRILVMDAGRV 570
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAvlFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
365-553 |
6.71e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 365 GFTYAGAPALQDitfdvpaGQVVALVGPSGAGKTTLVN-----LIPRFWDVTAgrvEVDGHDV-RAYA-------LADLR 431
Cdd:PRK13409 87 GFKLYGLPIPKE-------GKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEE---EPSWDEVlKRFRgtelqnyFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 432 ----------RQVGLVPQetlLFSGTVAEnilygrpgasqaeveaaahaahaheficELEGgygavVGERGV-------- 493
Cdd:PRK13409 157 ngeikvvhkpQYVDLIPK---VFKGKVRE----------------------------LLKK-----VDERGKldevverl 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 494 -----------KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFVVAHRL 553
Cdd:PRK13409 201 glenildrdisELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
372-582 |
1.28e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 372 PALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGH----------DVRAYALADLRRQVG----LV 437
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETL-----LFsgTVAENI---LYGRPGASQAEVEAAAHAAHAHEFICELEggygAVVGERGVKLSGGQRQRVAIARAI 509
Cdd:PRK10261 110 FQEPMtslnpVF--TVGEQIaesIRLHQGASREEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499192068 510 LKDPRILILDEATSALDNESEALVQ---AALERLMVGRTTFvVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMSMGVIF-ITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-582 |
1.40e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 349 PRpLSRAEGRVRFVDVGFTyagAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI----PRfwdvTAGRVEVDGHDVR- 423
Cdd:PRK10762 247 PR-LDKAPGEVRLKVDNLS---GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLygalPR----TSGYVTLDGHEVVt 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 424 -----------AYALADlRRQVGLVpqetLLFSgtVAENI-------LYGRPGASQAEVEAAAHAAHAHEFICELEGgYG 485
Cdd:PRK10762 319 rspqdglangiVYISED-RKRDGLV----LGMS--VKENMsltalryFSRAGGSLKHADEQQAVSDFIRLFNIKTPS-ME 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 486 AVVGergvKLSGGQRQRVAIARAILKDPRILILDEATSALDnesealVQAALERLMV-------GRTTFVVAHRLSTIRS 558
Cdd:PRK10762 391 QAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD------VGAKKEIYQLinqfkaeGLSIILVSSEMPEVLG 460
|
250 260 270
....*....|....*....|....*....|
gi 499192068 559 -ADRILVMDAGRV-----VADGTHEGLMAA 582
Cdd:PRK10762 461 mSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
41-333 |
1.73e-08 |
|
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: 55.95 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 41 LGVLATLISSGLGLVFPRLFGTLIDAsflkVGSTDTGPLDRTVLSLLGIFA---LSACFGAAQAYLLARVGAGVVADLRR 117
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISY----LSSYPDEPLSEGYLLALALFLvslLQSLLLHQYFFLSFRLGMRVRSALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 118 ALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVtSTALAQLASQGFTLIGSVLLLVQT---SprlSLLTLAIIPLVI 194
Cdd:cd18579 77 LIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDF-FLFLHYLWSAPLQIIVALYLLYRLlgwA---ALAGLGVLLLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 195 GTAVTIGRRIRRVSREVQDA----VAAANgqaeEAISGVRVVQSFtaeGLEEerygqgvlaSFRAALRRARLQ------- 263
Cdd:cd18579 153 PLQAFLAKLISKLRKKLMKAtderVKLTN----EILSGIKVIKLY---AWEK---------PFLKRIEELRKKelkalrk 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 264 -ALMTGVMSFLTFGA--LALVLWFGGRQVMSGALTPGNLVT--FLFYALQVggTVAALTGVFNQFQEALGASSRI 333
Cdd:cd18579 217 fGYLRALNSFLFFSTpvLVSLATFATYVLLGNPLTAAKVFTalSLFNLLRF--PLLMLPQAISSLIEALVSLKRI 289
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-555 |
1.95e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 384 GQVVALVGPSGAGKTTLVN-----LIPRFWDVTAgrvEVDGHDV-RAYA-------LADLR----------RQVGLVPQe 440
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKilsgeLKPNLGDYDE---EPSWDEVlKRFRgtelqdyFKKLAngeikvahkpQYVDLIPK- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 441 tlLFSGTVAEniLygrpgasqaeveaaahaahaheficeLEGgygavVGERGV-------------------KLSGGQRQ 501
Cdd:COG1245 175 --VFKGTVRE--L--------------------------LEK-----VDERGKldelaeklglenildrdisELSGGELQ 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 502 RVAIARAILKDPRILILDEATSALD-NESEALVQAALERLMVGRTTFVVAHRLST 555
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
376-582 |
1.97e-08 |
|
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: 57.14 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWD-VTAGRVEVDGH--DVRAYALAdLRRQVGLVPQET----LLFSGTV 448
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNPAQA-IRAGIAMVPEDRkrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 449 AENI----LYGRPGASQAEVEAAahaahaheficelEGGYGAVVGERGVK----------LSGGQRQRVAIARAILKDPR 514
Cdd:TIGR02633 357 GKNItlsvLKSFCFKMRIDAAAE-------------LQIIGSAIQRLKVKtaspflpigrLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 515 ILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADG-----THEGLMAA 582
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFvnhalTQEQVLAA 498
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
495-582 |
3.64e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKDPRILILDEATSALDnesealVQAALE--RLM-----VGRTTFVVAHRLSTIRS-ADRILVMD 566
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGID------VGAKYEiyKLInqlvqQGVAIIVISSELPEVLGlSDRVLVMH 479
|
90 100
....*....|....*....|.
gi 499192068 567 AGRVVAD-----GTHEGLMAA 582
Cdd:PRK13549 480 EGKLKGDlinhnLTQEQVMEA 500
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
154-329 |
4.37e-08 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 54.75 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 154 TSTALAQLASQGFTLIgSVLLLVQTSPRLSLLTLAIIPLVIGTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQ 233
Cdd:cd18587 115 TSATLTALIDLPFVLL-FLAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 234 SFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTV 313
Cdd:cd18587 194 ALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPL 273
|
170
....*....|....*.
gi 499192068 314 AALTGVFNQFQEALGA 329
Cdd:cd18587 274 GQIAGLLTRYQQARTA 289
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
493-564 |
7.25e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 7.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 493 VKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV--GRTTFVVAHRLSTIRS-ADRILV 564
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHV 144
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
86-335 |
1.21e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 53.69 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 86 LLGIFALSACFGAAQAYLLARvgAGVVADLR--RALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLAS 163
Cdd:cd18605 48 YGFLAGLNSLFTLLRAFLFAY--GGLRAARRlhNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 164 QGFTLIGSVLLLVQTSPrlsLLTLAIIPLVIgTAVTIGRRIRRVSREVQDAVAAANGQA----EEAISGVRVVQSFTAEG 239
Cdd:cd18605 126 QLFGLLGYLVVICYQLP---WLLLLLLPLAF-IYYRIQRYYRATSRELKRLNSVNLSPLythfSETLKGLVTIRAFRKQE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 240 LEEERYGQGVLASFRA--ALRRA------RLQALmtGVMSFLTFGALALVLWFGGRQVmsgalTPGNLVTFLFYALQVGG 311
Cdd:cd18605 202 RFLKEYLEKLENNQRAqlASQAAsqwlsiRLQLL--GVLIVTFVALTAVVQHFFGLSI-----DAGLIGLALSYALPITG 274
|
250 260
....*....|....*....|....
gi 499192068 312 TVAALTGVFNQFQEALGASSRIFE 335
Cdd:cd18605 275 LLSGLLNSFTETEKEMVSVERVRQ 298
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
350-551 |
1.24e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 350 RPLSRAEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDV----RAY 425
Cdd:PRK13543 3 EPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 426 ALADLRRQVGLVPQETLLfsgtvaENIlygrpgasqaeveaaahaahahEFICELEGGYG--------AVVGERGV---- 493
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTL------ENL----------------------HFLCGLHGRRAkqmpgsalAIVGLAGYedtl 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 494 --KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALE-RLMVGRTTFVVAH 551
Cdd:PRK13543 135 vrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
359-538 |
1.64e-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: 54.17 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 359 VRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVdGHDVrayaladlrrQVGLVP 438
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 Q--ETLLFSGTVAENILYGRPgasqaeveaaahaahahefICELeGGYG----AVVGERGVK----------LSGGQRQR 502
Cdd:TIGR03719 392 QsrDALDPNKTVWEEISGGLD-------------------IIKL-GKREipsrAYVGRFNFKgsdqqkkvgqLSGGERNR 451
|
170 180 190
....*....|....*....|....*....|....*..
gi 499192068 503 VAIARAILKDPRILILDEATSALDNES-EALVQAALE 538
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETlRALEEALLN 488
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
373-582 |
2.48e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVrAYALADLRRQ-VGLVPQEtllfsgtvAEN 451
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSQrIRMIFQD--------PST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 452 ILYGRPGASQAEVEAAAHAAHAHEfiCELEGGYGAVVGERGVK----------LSGGQRQRVAIARAILKDPRILILDEA 521
Cdd:PRK15112 99 SLNPRQRISQILDFPLRLNTDLEP--EQREKQIIETLRQVGLLpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 522 TSALDNEsealVQAALERLMV------GRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAA 582
Cdd:PRK15112 177 LASLDMS----MRSQLINLMLelqekqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
373-557 |
2.99e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGhDVRAYALadlrrQVGLVPQETLLfsgtvaENI 452
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAI-----SAGLSGQLTGI------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 453 LYGRPGASQAEVEAAAHAAHAHEFiCELeggyGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDnesEAL 532
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEF-SEL----GEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTF 178
|
170 180
....*....|....*....|....*....
gi 499192068 533 VQAALERLM----VGRTTFVVAHRLSTIR 557
Cdd:PRK13546 179 AQKCLDKIYefkeQNKTIFFVSHNLGQVR 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
494-539 |
4.03e-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: 53.02 E-value: 4.03e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALER 539
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
343-556 |
4.16e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 343 LPGPAAPR---PLSRAEGRVRFVDVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLI----PRFW--DVTA- 412
Cdd:PRK10938 242 LPEPDEPSarhALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhPQGYsnDLTLf 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 413 GRVEVDGHdvrayALADLRRQVGLVPQETLL---FSGTVAENILYG---RPGASQAEVEAAAHAAHAHEFICelegGYGA 486
Cdd:PRK10938 322 GRRRGSGE-----TIWDIKKHIGYVSSSLHLdyrVSTSVRNVILSGffdSIGIYQAVSDRQQKLAQQWLDIL----GIDK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 487 VVGERGVK-LSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMV-GRTT--FV----------VAHR 552
Cdd:PRK10938 393 RTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQllFVshhaedapacITHR 472
|
....
gi 499192068 553 LSTI 556
Cdd:PRK10938 473 LEFV 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
375-582 |
4.65e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 375 QDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALAD-LRRQVGLVPQ---ETLLFSG-TVA 449
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 450 ENI-------LYGRPGA-----SQAEVEAAAHAAHAHEFICeleggygAVVGERGVKLSGGQRQRVAIARAILKDPRILI 517
Cdd:PRK09700 360 QNMaisrslkDGGYKGAmglfhEVDEQRTAENQRELLALKC-------HSVNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 518 LDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSA-DRILVMDAGRVVA------DGTHEGLMAA 582
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQiltnrdDMSEEEIMAW 505
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
363-585 |
7.30e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtAGRVEVDGHDVRAYALAdlrrQVGLVPQET- 441
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVKWSENA----NIGYYAQDHa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 --------------------------------LLFSGtvaENIlygrpgasqaeveaaahaahaheficeleggygavvg 489
Cdd:PRK15064 393 ydfendltlfdwmsqwrqegddeqavrgtlgrLLFSQ---DDI------------------------------------- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 490 ERGVK-LSGGQRQRVAIARAILKDPRILILDEATSALDNES-EALvQAALErlMVGRTTFVVAHRLSTIRS-ADRILVMD 566
Cdd:PRK15064 433 KKSVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiESL-NMALE--KYEGTLIFVSHDREFVSSlATRIIEIT 509
|
250 260
....*....|....*....|
gi 499192068 567 AGRVVA-DGTHEGLMAAGGL 585
Cdd:PRK15064 510 PDGVVDfSGTYEEYLRSQGI 529
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
374-582 |
7.55e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTL-VNLIPRFWDV-TAGRVEVDGHDVR------------AYALADlRRQVGLVPQ 439
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDvstvsdaidaglAYVTED-RKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 440 ETllfsgtVAENI-LYGRPGASQAEveaaahaahaheFICELEGGYGAV------------VGERGVKLSGGQRQRVAIA 506
Cdd:NF040905 355 DD------IKRNItLANLGKVSRRG------------VIDENEEIKVAEeyrkkmniktpsVFQKVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 507 RAILKDPRILILDEATSALDnesealVQAALE------RLMV-GRTTFVVAHRL-STIRSADRILVMDAGRVV-----AD 573
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID------VGAKYEiytiinELAAeGKGVIVISSELpELLGMCDRIYVMNEGRITgelprEE 490
|
....*....
gi 499192068 574 GTHEGLMAA 582
Cdd:NF040905 491 ASQERIMRL 499
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
40-301 |
8.18e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 51.01 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 40 VLGVLAtLISSGLGLVFPRLFGTLIDasFLKVGSTdtgPLDRTVLSLLGIFA---LSACFGAAQAYLLARVGAGVVADLR 116
Cdd:cd18598 1 PLGLLK-LLADVLGFAGPLLLNKLVE--FLEDSSE---PLSDGYLYALGLVLsslLGALLSSHYNFQMNKVSLKVRAALV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 117 RALFSHLLSLSPRFFGNHRTGDLTSRLTSDVGTVQAVTSTaLAQLASQGFTLIGSVLLLVQtspRLSL-------LTLAI 189
Cdd:cd18598 75 TAVYRKALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPS-FHDLWSLPLQIIVALYLLYQ---QVGVaflaglvFALVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 190 IPLVIgtavTIGRRIRRVSREVQ---DA-VAAANgqaeEAISGVRVVQSFTAEGLEEERygqgVLASFRAALRRARLQAL 265
Cdd:cd18598 151 IPINK----WIAKRIGALSEKMMkhkDArVKLMT----EILSGIRVIKLLAWERIFKQK----IEELRAKELKALKGRKY 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499192068 266 MTGV-----------MSFLTFGALALvlwfggrqvMSGALTPGNLVT 301
Cdd:cd18598 219 LDALcvyfwattpvlISILTFATYVL---------MGNTLTAAKVFT 256
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
373-598 |
9.43e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 373 ALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYALADLRRQVGLVPQETL--LFSGTVAE 450
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELkgLMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 451 NIlygrpgasQAEVEAAAHAAHAHEFICELEGGYgavvgergvklSGGQRQRVAIARAILKDPRILILDEATSALDnesE 530
Cdd:PRK13545 119 KI--------KEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 531 ALVQAALERL----MVGRTTFVVAHRLSTIRS-ADRILVMDAGRV--------VADGTHEGLMAAGGLYRELYElQFRQQ 597
Cdd:PRK13545 177 TFTKKCLDKMnefkEQGKTIFFISHSLSQVKSfCTKALWLHYGQVkeygdikeVVDHYDEFLKKYNQMSVEERK-DFREE 255
|
.
gi 499192068 598 Q 598
Cdd:PRK13545 256 Q 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
363-551 |
2.19e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 363 DVGFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAYAlaDLRRQVgLVPQETl 442
Cdd:PRK11147 324 NVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYF--DQHRAE-LDPEKT- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 443 lfsgtVAENILYGRpgasQAEveaaahaahaheficELEGGYGAVVG---------ERG---VK-LSGGQRQRVAIARAI 509
Cdd:PRK11147 400 -----VMDNLAEGK----QEV---------------MVNGRPRHVLGylqdflfhpKRAmtpVKaLSGGERNRLLLARLF 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499192068 510 LKDPRILILDEATSALDNESEALvqaaLERLMVGR--TTFVVAH 551
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLEL----LEELLDSYqgTVLLVSH 495
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
494-529 |
2.41e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 2.41e-06
10 20 30
....*....|....*....|....*....|....*.
gi 499192068 494 KLSGGQRQRVAIARAILKDPRILILDEATSALDNES 529
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
57-308 |
3.27e-06 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, 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. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 49.17 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 57 PRLFGTLIDAsfLKVGSTDTGPLDRTVLSLLGIFAL---------SACFGAAQAYLLARVGAGVVADLRRALFSHLLSLS 127
Cdd:cd18581 16 PILYKKIVDS--LTPDSADSPLAFPWALILLYVFLKflqgggsgsVGLLSNLRSFLWIPVQQFTTREISVKLFAHLHSLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 128 PRFFGNHRTGDLTSRLTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQT-SPRLSL---LTLAI-IPLVIgtAVTIGR 202
Cdd:cd18581 94 LRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAfNPWFGLivfVTMALyLILTI--IITEWR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 203 -RIRRVSREvQDavAAANGQAEEAISGVRVVQSFTAEGLEEERYGQGVLASFRAALRRARLQALMTGVMSFLTFGALALV 281
Cdd:cd18581 172 tKFRREMNK-LD--NEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLIITIGLLAG 248
|
250 260
....*....|....*....|....*..
gi 499192068 282 LWFGGRQVMSGALTPGNLVTFLFYALQ 308
Cdd:cd18581 249 SLLCAYFVVEGKLTVGDFVLFLTYIIQ 275
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
495-574 |
3.34e-06 |
|
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: 47.70 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKDPR--ILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVM------ 565
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgk 167
|
....*....
gi 499192068 566 DAGRVVADG 574
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
381-554 |
4.84e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.52 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 381 VPA-GQVVALVGPSGAGKTTLVN-----LIPRF--------WD--VTAGRvevdGHDVRAYaLADLR----------RQV 434
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKilagkLKPNLgkfddppdWDeiLDEFR----GSELQNY-FTKLLegdvkvivkpQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 435 GLVPQEtllFSGTVAENIlygrpgasqaeveAAAHAAHAHEFIC---ELEGgygavVGERGV-KLSGGQRQRVAIARAIL 510
Cdd:cd03236 97 DLIPKA---VKGKVGELL-------------KKKDERGKLDELVdqlELRH-----VLDRNIdQLSGGELQRVAIAAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499192068 511 KDPRILILDEATSALDNESEALVQAALERLMV-GRTTFVVAHRLS 554
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
495-571 |
5.31e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499192068 495 LSGGQRQRVAIARAILKDPRILILDEATSALDNES-EALVQAALErlMVGRTTFvVAHRLSTIRS-ADRILVMDAGRVV 571
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWLEGFLKT--FQGSIIF-ISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
383-571 |
6.01e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 383 AGQVVALVGPSGAGKTTLVNLIP----RFWDVTAGRVEVDGHDvrayaLADLRRQV---------------GLVPQETLL 443
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT-----PEEIKKHYrgdvvynaetdvhfpHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 444 FSG---TVAEnilygRP-GASQAEVEAAAHAAHAHEFicELEGGYGAVVGE---RGVklSGGQRQRVAIARAILKDPRIL 516
Cdd:TIGR00956 161 FAArckTPQN-----RPdGVSREEYAKHIADVYMATY--GLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 517 ILDEATSALDNeSEAL--VQAALERLMVGRTT-FVVAHRLS--TIRSADRILVMDAGRVV 571
Cdd:TIGR00956 232 CWDNATRGLDS-ATALefIRALKTSANILDTTpLVAIYQCSqdAYELFDKVIVLYEGYQI 290
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
365-570 |
6.70e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 365 GFTYAGAPALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVR----------AYAL-ADLRRQ 433
Cdd:PRK10982 255 NLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhGFALvTEERRS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 434 VGLVPQETLLFSGTVAENILY-GRPGASQAEveaaahaahaheficELEGGYGAVVGERGVK----------LSGGQRQR 502
Cdd:PRK10982 335 TGIYAYLDIGFNSLISNIRNYkNKVGLLDNS---------------RMKSDTQWVIDSMRVKtpghrtqigsLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 503 VAIARAILKDPRILILDEATSALDNESE-ALVQAALERLMVGRTTFVVAHRLSTIRS-ADRILVMDAGRV 570
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
495-577 |
9.63e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKD---PRILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVM----- 565
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|...
gi 499192068 566 -DAGRVVADGTHE 577
Cdd:TIGR00630 910 dGGGTVVASGTPE 922
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
368-584 |
1.06e-05 |
|
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: 48.86 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 368 YAG--APALQDITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVDGHDVRAyALADLRRQVGLVPQ----ET 441
Cdd:TIGR01257 1947 YSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 442 LLfsgTVAENI-LYGR----PGAS-QAEVEAAAHAAHAHEFICELEGGYgavvgergvklSGGQRQRVAIARAILKDPRI 515
Cdd:TIGR01257 2026 LL---TGREHLyLYARlrgvPAEEiEKVANWSIQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 516 LILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRS-ADRILVMDAGRVVADGTHEGLMAAGG 584
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
489-574 |
1.13e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 489 GERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALeRLMV--GRTTFVVAHRLSTIRS-ADRILVM 565
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEAEQlAHELTVI 217
|
....*....
gi 499192068 566 DAGRVVADG 574
Cdd:NF000106 218 DRGRVIADG 226
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
73-337 |
1.27e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 47.46 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 73 STDTGPLDRTVLSLLGIFAL----SACFGAAQAYLLARVGagvvadLR--RALFSHLLS--LS--PRFFGNHRTGDLTSR 142
Cdd:cd18604 32 SSALPPSEVSVLYYLGIYALisllSVLLGTLRYLLFFFGS------LRasRKLHERLLHsvLRapLRWLDTTPVGRILNR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 143 LTSDVGTVQAVTSTALAQLASQGFTLIGSVLLLVQTSPrlSLLTLAIIPLVIGtaVTIGRRIRRVSREVQDAVAAAN--- 219
Cdd:cd18604 106 FSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSP--AFLLPAVVLAALY--VYIGRLYLRASRELKRLESVARspi 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 220 -GQAEEAISGVRVVQSFTAegleEERYGQGVLASFRAALRRARLQALM-------TGVMSFLTFGALALVLwfggrqVMS 291
Cdd:cd18604 182 lSHFGETLAGLVTIRAFGA----EERFIEEMLRRIDRYSRAFRYLWNLnrwlsvrIDLLGALFSFATAALL------VYG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499192068 292 GALTPGnLVTF-LFYALQVGGTVAALTGVFNQFQEALGASSRIFELL 337
Cdd:cd18604 252 PGIDAG-LAGFsLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
43-326 |
1.87e-05 |
|
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: 46.85 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 43 VLATLISSGLGLVFPRLFGTLIDAsfLKVGstdtgpldRTVLSLLGIFALSACFGAAQAYLLARvGAGVVADLRR----- 117
Cdd:cd18562 5 ALANVALAGVQFAEPVLFGRVVDA--LSSG--------GDAFPLLALWAALGLFSILAGVLVAL-LADRLAHRRRlavma 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 118 ALFSHLLSLSPRFFGNHRTGDLTSRLTSdvGTvQAVTSTALAQLASQGFTLIGSVLLL---VQTSPRLSLLTLAIIPLVI 194
Cdd:cd18562 74 SYFEHVITLPLSFHSQRGSGRLLRIMLR--GT-DALFGLWLGFFREHLAALVSLIVLLpvaLWMNWRLALLLVVLAAVYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 195 GTAVTIGRRIRRVSREVQDAVAAANGQAEEAISGVRVVQSFT---AEGLEEERYGQGVLASFRAALRRARLQALMTGVMS 271
Cdd:cd18562 151 ALNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTrlaAETSALRGITRRLLAAQYPVLNWWALASVLTRAAS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 272 FLTfgaLALVLWFGGRQVMSGALTPGNLVTFLFYALQVGGTVAALTGVFNQ-FQEA 326
Cdd:cd18562 231 TLT---MVAIFALGAWLVQRGELTVGEIVSFVGFATLLIGRLDQLSGFINRlFMQA 283
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
82-212 |
3.32e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 46.06 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 82 TVLSLLGIFALSACFGAAQAyllarvgAGVVAdlRRALFSHLL---SLSP-RFFGNHRTGDLTSRLTSDVGTVQAVTSTA 157
Cdd:cd18602 57 AGLSLGAVILSLVTNLAGEL-------AGLRA--ARRLHDRMLrniVRAPmRFFDTTPIGRILNRFSSDTNVIDQKLPTT 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 158 LAQLASQGFTLIGSVLLLVQTSPrlsLLTLAIIPLVIgTAVTIGRRIRRVSREVQ 212
Cdd:cd18602 128 LERLLRFLLLCLSAIIVNAIVTP---YFLIALIPIII-VYYFLQKFYRASSRELQ 178
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
495-581 |
4.61e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAI---LKDPrILILDEATSAL---DNESeaLVQAaLERLM-VGRTTFVVAHRLSTIRSADRILVM-- 565
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLhqrDNRR--LINT-LKRLRdLGNTLIVVEHDEDTIRAADYVIDIgp 564
|
90 100
....*....|....*....|
gi 499192068 566 ----DAGRVVADGTHEGLMA 581
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILA 584
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
495-575 |
4.92e-05 |
|
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: 45.30 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILKDPR---ILILDEATSALDNESEALVQAALERLM-VGRTTFVVAHRLSTIRSADRILVM----- 565
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWIIDLgpegg 249
|
90
....*....|.
gi 499192068 566 -DAGRVVADGT 575
Cdd:cd03271 250 dGGGQVVASGT 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
376-538 |
6.98e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 376 DITFDVPAGQVVALVGPSGAGKTTLVNLIPRFWDVTAGRVEVdGHDVrayaladlrrQVGLVPQ--ETLLFSGTVAENIL 453
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQsrDALDPNKTVWEEIS 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 454 YGRPgasqaeveaaahaahahefICELeGGYG----AVVGERGVK----------LSGGQRQRVAIARAILKDPRILILD 519
Cdd:PRK11819 411 GGLD-------------------IIKV-GNREipsrAYVGRFNFKggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLD 470
|
170 180
....*....|....*....|
gi 499192068 520 EATSALDNES-EALVQAALE 538
Cdd:PRK11819 471 EPTNDLDVETlRALEEALLE 490
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
374-577 |
7.84e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.63 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLI---PRFwDVTAGRVEVDGHDVrAYALADLRRQVGL------------VP 438
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPAY-KILEGDILFKGESI-LDLEPEERAHLGIflafqypieipgVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSGTVAENILYGRPGASqaeveaaahAAHAHEFICE-LEggygaVVG------ERGVK--LSGGQRQRVAIARAI 509
Cdd:CHL00131 101 NADFLRLAYNSKRKFQGLPELD---------PLEFLEIINEkLK-----LVGmdpsflSRNVNegFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 510 LKDPRILILDEATSALDNESEALVQAALERLMVGRTTFV-VAH--RLSTIRSADRILVMDAGRVVADGTHE 577
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
374-574 |
8.01e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.17 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLV-NLI---------------PRFWDVTAGRVEVDGHDVRAYALADLRRQVGLV 437
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIyaegqrryveslsayARQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 438 PQETLlfsGTVAE-----NILYGRPGASQAEVeaaahaahaheFICELEGGYgAVVGERGVKLSGGQRQRVAIARAILK- 511
Cdd:cd03270 91 PRSTV---GTVTEiydylRLLFARVGIRERLG-----------FLVDVGLGY-LTLSRSAPTLSGGEAQRIRLATQIGSg 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499192068 512 -DPRILILDEATSAL---DNESealVQAALERLM-VGRTTFVVAHRLSTIRSADRILVM------DAGRVVADG 574
Cdd:cd03270 156 lTGVLYVLDEPSIGLhprDNDR---LIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
495-582 |
8.16e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAI---LKDprIL-ILDEATSAL---DNEseaLVQAALERLM-VGRTTFVVAHRLSTIRSADRILVM- 565
Cdd:COG0178 486 LSGGEAQRIRLATQIgsgLVG--VLyVLDEPSIGLhqrDND---RLIETLKRLRdLGNTVIVVEHDEDTIRAADYIIDIg 560
|
90 100
....*....|....*....|..
gi 499192068 566 -DA----GRVVADGTHEGLMAA 582
Cdd:COG0178 561 pGAgehgGEVVAQGTPEEILKN 582
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
370-576 |
3.50e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 370 GAPALQDITFDVPAGQVVALVGPSGAGKTTL-VNLIPRF-WDVTAGRVEVDGHDVRAYALADlRRQVGL---------VP 438
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypveIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 439 QETLLFSGTVAENILygRPGASQAEVEAAAHAAHAHEFICELEGGYGAVVGERGVKLSGGQRQRVAIARAILKDPRILIL 518
Cdd:PRK09580 92 GVSNQFFLQTALNAV--RSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499192068 519 DEATSALDNESEALVQAALERLMVGRTTF-VVAH--RLSTIRSADRILVMDAGRVVADGTH 576
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGKRSFiIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
493-565 |
3.75e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.58 E-value: 3.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499192068 493 VKLSGGQRQRVAIARAI---LKDPRIL-ILDEATSALDNES-EALVQAALERLMVGRTTFVVAHRLSTIRSADRILVM 565
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
383-419 |
4.19e-04 |
|
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: 42.00 E-value: 4.19e-04
10 20 30
....*....|....*....|....*....|....*...
gi 499192068 383 AGQVVALVGPSGAGKTTLVN-LIPRFWDVTAGRVEVDG 419
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNaLLPELVLATGEISEKLG 121
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
313-570 |
4.30e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 313 VAALTGVFNQFQ----EALGASSRIFELldERSDLPGPA---------------APRPLSRAEgrvrfvDVGFTYAGAPA 373
Cdd:PRK10636 256 VAHLQSYIDRFRakatKAKQAQSRIKML--ERMELIAPAhvdnpfhfsfrapesLPNPLLKME------KVSAGYGDRII 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVNLIprfwdvtagrvevdghdvrAYALADLRRQVGLVPQETLlfsGTVAENIL 453
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-------------------AGELAPVSGEIGLAKGIKL---GYFAQHQL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 454 -YGRPGASQAEVEAAAHAAHAHEFICELEGGYG---AVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALD-NE 528
Cdd:PRK10636 386 eFLRADESPLQHLARLAPQELEQKLRDYLGGFGfqgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDlDM 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499192068 529 SEALVQAAL--ERLMVgrttfVVAHRLSTIRSA--DRILVMDaGRV 570
Cdd:PRK10636 466 RQALTEALIdfEGALV-----VVSHDRHLLRSTtdDLYLVHD-GKV 505
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
495-563 |
1.22e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499192068 495 LSGGQRQRVAIARAIL---KDPRILILDEATSAL-DNESEALVQAALERLMVGRTTFVVAHRLSTIRSADRIL 563
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
374-402 |
1.24e-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: 41.92 E-value: 1.24e-03
10 20
....*....|....*....|....*....
gi 499192068 374 LQDITFDVPAGQVVALVGPSGAGKTTLVN 402
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
386-407 |
2.18e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 39.01 E-value: 2.18e-03
10 20
....*....|....*....|...
gi 499192068 386 VVALVGPSGAGKTTLV-NLIPRF 407
Cdd:COG1763 3 VLGIVGYSGSGKTTLLeKLIPEL 25
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
496-551 |
2.31e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499192068 496 SGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALerLMVGRTTFVVAH 551
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
383-404 |
3.82e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 3.82e-03
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
40-309 |
3.88e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 39.54 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 40 VLGVLAtLISSGLGLVFPRLFGTLIdASFlkvgsTDTGPLDRTVLSLLGIfALSACFGAAQA------YLLARVGAGVVA 113
Cdd:cd18594 1 LLGILL-FLEESLKIVQPLLLGRLV-AYF-----VPDSTVTKTEAYLYAL-GLSLCAFLRVLlhhpyfFGLHRYGMQLRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 114 DLRRALFSHLLSLSPRFFGNHRTGDLTSRLTSDV---------------GTVQAVTSTALAQLASQGFTLIGSVLLLVQT 178
Cdd:cd18594 73 ALSSLIYKKTLKLSSSALSKITTGHIVNLLSNDVqkfdevlvylhflwiAPLQVIVLTGLLWREIGPSSLAGLGVLLLLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 179 sPRLSLLTLAIIPLVIGTAVTIGRRIRRVSrevqdavaaangqaeEAISGVRVVQSFTAegleEERYGQGVLASFRAALR 258
Cdd:cd18594 153 -PLQAYLGKLFAKYRRKTAGLTDERVKIMN---------------EIISGMRVIKMYTW----EESFAKLIENIRKKELK 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499192068 259 RARLQALMTGV-MSFLTF-GALALVLWFGGRQVMSGALTPGNLVTF--LFYALQV 309
Cdd:cd18594 213 LIRKAAYIRAFnMAFFFFsPTLVSFATFVPYVLTGNTLTARKVFTVisLLNALRM 267
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
483-581 |
4.00e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 483 GYGAVVGERGVKLSGGQRQRVAIARAILKDPRILILDEATSALDNESEALVQAALERLMVGRTTFV-VAHRLSTIRS-AD 560
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQ 203
|
90 100
....*....|....*....|.
gi 499192068 561 RILVMDAGRVVADGTHEGLMA 581
Cdd:PRK10938 204 FAGVLADCTLAETGEREEILQ 224
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
384-402 |
8.03e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 8.03e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
495-581 |
9.96e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499192068 495 LSGGQRQRVAIARAILK---DPRILILDEATSALDNESEALVQAALERLmV--GRTTFVVAHRLSTIRSADRILVM---- 565
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRL-VdkGNTVVVIEHNLDVIKTADWIIDLgpeg 905
|
90
....*....|....*...
gi 499192068 566 --DAGRVVADGTHEGLMA 581
Cdd:COG0178 906 gdGGGEIVAEGTPEEVAK 923
|
|
| |
