|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-558 |
8.34e-176 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 514.66 E-value: 8.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRASDWVARE---DELA-AILPMVLLGLSSAVTELVCDVTFVGTL 83
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDkgpPALAsAIFFMCLLSIASSVSAGLRGGSFNYTM 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 SRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTAL 163
Cdd:TIGR00958 230 ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 164 ALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLW 243
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLW 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 244 TSGFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPSGT 323
Cdd:TIGR00958 390 TTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGT 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 324 MAPTDLQGHLQLEDVWFSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQ 402
Cdd:TIGR00958 470 LAPLNLEGLIEFQDVSFSYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 403 HSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIA 482
Cdd:TIGR00958 550 HHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIA 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQeilAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGpPHEVLR 558
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG-THKQLM 701
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
24-308 |
6.33e-158 |
|
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: 453.08 E-value: 6.33e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 24 VMGLMAASALGEMAVPYYMGRASDWV----AREDELAAILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVL 99
Cdd:cd18589 1 VLGLVVLSSLGEMAIPYYTGRMTDWImnkdAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 100 RQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFR 179
Cdd:cd18589 81 RQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 180 QALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYY 259
Cdd:cd18589 161 QSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2099372369 260 GGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18589 241 GGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-569 |
2.19e-144 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 429.58 E-value: 2.19e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 3 TMGAGRRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILP----MVLLGLSSAVTELVCDVT 78
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLllllLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 79 FVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMA 158
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 159 LLTALALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALY 238
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 239 TASLWTSGFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQV 318
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 319 A-PSGTMAPTDLQGHLQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP 397
Cdd:COG1132 325 PdPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 398 LPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQ 477
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALI-QEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|...
gi 2099372369 558 RPGSLLRD-WGQQ 569
Cdd:COG1132 563 ARGGLYARlYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-569 |
4.14e-110 |
|
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: 345.28 E-value: 4.14e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILP----MVLLGLSSAVTELVCDVTFVGTL 83
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVlaigLLLALLFEGLLRLLRSYLLLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 SRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVtRDAEDVREAL-GEALSLLLwYLARGLCLFATMAWLSPRMALLTA 162
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLtGSLLTALL-DLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 163 LALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKK-DVALYTAS 241
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 242 LWTSGFSALALkMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPS 321
Cdd:COG2274 383 TLSGLLQQLAT-VALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 322 GTMAPTD-LQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA 400
Cdd:COG2274 462 RSKLSLPrLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 401 YQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVA 480
Cdd:COG2274 542 IDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL-RP 559
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAII-LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLaRK 700
|
570
....*....|
gi 2099372369 560 GSLLRDWGQQ 569
Cdd:COG2274 701 GLYAELVQQQ 710
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
322-547 |
8.45e-94 |
|
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: 286.67 E-value: 8.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 322 GTMAPTDLQGHLQLEDVWFSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA 400
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 401 YQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVA 480
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEQeILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEV 547
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQ-ALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-558 |
5.00e-83 |
|
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: 270.48 E-value: 5.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRC--AAVMGLMA-ASALGEMAVpyymgraSDW-VARedelAAILPMVL-----------LGLSSAVT- 71
Cdd:COG4987 4 LRLLRLLRPHRGRLllGVLLGLLTlLAGIGLLAL-------SGWlIAA----AALAPPILnlfvpivgvraFAIGRTVFr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 72 --ELVC--DVTFvgtlsRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLF 147
Cdd:COG4987 73 ylERLVshDATL-----RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 148 ATMAWLSPRMALLTALALPLLLALPRAVGHfRQALAPQMQKAQARA--SEVAVETFQAMATVRSFANEDGAAAHYRQRLQ 225
Cdd:COG4987 148 AFLAFFSPALALVLALGLLLAGLLLPLLAA-RLGRRAGRRLAAARAalRARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 226 QSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSS 305
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 306 EKIFEFLDREPQVAPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ 385
Cdd:COG4987 307 RRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 386 PTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVG 465
Cdd:COG4987 387 PQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 466 ELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAkGSGRAVLMVTGRAALAARAQRVVVLEGG 545
Cdd:COG4987 467 EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDG 545
|
570
....*....|...
gi 2099372369 546 EVRQEGPPHEVLR 558
Cdd:COG4987 546 RIVEQGTHEELLA 558
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-557 |
6.21e-83 |
|
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: 270.05 E-value: 6.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRASD--WVAREDELAAILPMVLLGLssAVTELVCDVT---FVGT 82
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDdgFGGRDRSVLWWVPLVVIGL--AVLRGICSFVstyLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 83 LSR-TQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLT 161
Cdd:TIGR02203 81 VSNkVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 162 ALALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDV---ALY 238
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTsagSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 239 TASLWTSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQV 318
Cdd:TIGR02203 241 SPITQLIASLALAV---VLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 319 aPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL 398
Cdd:TIGR02203 318 -DTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 399 PAYQHSYLCRQVAVVPQEPLLFARSLHANISYG-LGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQ 477
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-560 |
2.29e-80 |
|
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: 263.16 E-value: 2.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRA-SDWVAREDELAAILPMVLLGLSSAVTELVCdvTFVGTL--- 83
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLlAGLIIGGAPLSALLPLLGLLLAVLLLRALL--AWLRERaaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 ---SRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALS-LLLWYLARgLCLFATMAWLSPR--- 156
Cdd:COG4988 84 raaARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPqLFLAALVP-LLILVAVFPLDWLsgl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 157 ------------MalltalalplllalpRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFanedGAAAHYRQRL 224
Cdd:COG4988 163 illvtapliplfM---------------ILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLF----GRAKAEAERI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 225 QQ-SHRLEKKD-----VALyTASLWTSGFSALALKMGILYYGGQLVAaGTVSTGDLVTFLL-----YQiqftdVLRVLLD 293
Cdd:COG4988 224 AEaSEDFRKRTmkvlrVAF-LSSAVLEFFASLSIALVAVYIGFRLLG-GSLTLFAALFVLLlapefFL-----PLRDLGS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 294 YFPTLMKAVGSSEKIFEFLDREPQVAPSGTMAPTDLQG-HLQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAG 372
Cdd:COG4988 297 FYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 373 KSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDF 452
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 453 ITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGsGRAVLMVTGRAAL 532
Cdd:COG4988 456 VAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLAL 534
|
570 580
....*....|....*....|....*...
gi 2099372369 533 AARAQRVVVLEGGEVRQEGPPHEVLRPG 560
Cdd:COG4988 535 LAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-565 |
9.38e-77 |
|
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: 242.91 E-value: 9.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 493 ILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRD 565
Cdd:cd03251 161 ILDEATSALDTESERLV-QAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-557 |
9.21e-75 |
|
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: 237.82 E-value: 9.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 335 LEDVWFSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:cd03249 3 FKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILI 493
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 494 LDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03249 163 LDEATSALDAESEKLV-QEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
185-516 |
1.31e-72 |
|
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: 243.57 E-value: 1.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 185 QMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQqshRLEKKDVALYTaSLWTSGFS-----ALALkMGILYY 259
Cdd:COG5265 209 EMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALA---RYERAAVKSQT-SLALLNFGqaliiALGL-TAMMLM 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 260 GGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPSGTMAPTDL-QGHLQLEDV 338
Cdd:COG5265 284 AAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 339 WFSY-PGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEP 417
Cdd:COG5265 364 SFGYdPER--PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEH 497
Cdd:COG5265 442 VLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
330
....*....|....*....
gi 2099372369 498 TSALDTESqqqvEQEILAA 516
Cdd:COG5265 522 TSALDSRT----ERAIQAA 536
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-569 |
4.19e-72 |
|
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: 230.97 E-value: 4.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSY-PGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVA 411
Cdd:cd03253 1 IEFENVTFAYdPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRI 491
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 492 LILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRD-WGQQ 569
Cdd:cd03253 159 LLLDEATSALDTHTEREI-QAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEmWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
331-557 |
7.93e-72 |
|
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: 229.80 E-value: 7.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYpGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQV 410
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 491 ILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03254 160 ILILDEATSNIDTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
79-569 |
2.80e-67 |
|
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: 231.56 E-value: 2.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 79 FVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVtRDAEDVREAL-GEALSLLLwYLARGLCLFATMAWLSPRM 157
Cdd:TIGR01846 203 FAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARV-RELEQIRNFLtGSALTVVL-DLLFVVVFLAVMFFYSPTL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 158 ALLTALALPLLLALPRAVG-HFRQALAPQMQKAqARASEVAVETFQAMATVRSFANEDGAAAHYRQRL-QQSHRLEKKDV 235
Cdd:TIGR01846 281 TGVVIGSLVCYALLSVFVGpILRKRVEDKFERS-AAATSFLVESVTGIETIKATATEPQFQNRWDRQLaAYVAASFRVTN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 236 ALYTASLWTSGFSALALKMgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTD-VLRvLLDYFPTLMKAVGSSEKIFEFLDR 314
Cdd:TIGR01846 360 LGNIAGQAIELIQKLTFAI-LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQpVLR-LAQLWQDFQQTGIALERLGDILNS 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 315 EPQVAPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLD 394
Cdd:TIGR01846 438 PTEPRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVD 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 395 GHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGG 474
Cdd:TIGR01846 518 GVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 475 QRQAVAIARALLRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPH 554
Cdd:TIGR01846 598 QRQRIAIARALVGNPRILIFDEATSALDYESEALI-MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHE 676
|
490
....*....|....*.
gi 2099372369 555 EVLRPGSLLRD-WGQQ 569
Cdd:TIGR01846 677 ELLALQGLYARlWQQQ 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-546 |
3.28e-65 |
|
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: 210.32 E-value: 3.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANIsyglggcswaqvtaaarrvgahdfitrlpqgydtevgelggqLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGsGRAVLMVTGRAALAARAQRVVVLEGGE 546
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-564 |
7.10e-63 |
|
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: 206.95 E-value: 7.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQ---QQVEQEILAakgsGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:cd03252 161 IFDEATSALDYESEhaiMRNMHDICA----GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
254-513 |
3.31e-62 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 215.60 E-value: 3.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 254 MGILYYGGQLVAAGTVSTGDLVTFllyqIQFTDVLRVLLD----YFPTLMKAVGSSEKIFEFLDREPQVA-PSGTMAPTD 328
Cdd:PRK13657 255 LAILVLGAALVQKGQLRVGEVVAF----VGFATLLIGRLDqvvaFINQVFMAAPKLEEFFEVEDAVPDVRdPPGAIDLGR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 329 LQGHLQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCR 408
Cdd:PRK13657 331 VKGAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRD 488
Cdd:PRK13657 410 NIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
250 260
....*....|....*....|....*
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEI 513
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAAL 514
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
84-558 |
7.54e-62 |
|
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: 213.84 E-value: 7.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 SRTQSRLQRRVFAAVLRQSiteLRADGAGdvAMRVTRDAEDVREAL-GEALSLLL-----------------WY----LA 141
Cdd:COG4618 89 ARLDRRLGPRVFDAAFRAA---LRGGGGA--AAQALRDLDTLRQFLtGPGLFALFdlpwapiflavlflfhpLLgllaLV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 142 RGLCLFAtMAWLSPRMAlltalalplllalpravghfRQALApQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYR 221
Cdd:COG4618 164 GALVLVA-LALLNERLT--------------------RKPLK-EANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 222 QRLQQSHRLEKKdvalytASLWTSGFSA------LALKMGILYYGGQLVAAGTVSTGDLV--TFLLYqiqftdvlRVL-- 291
Cdd:COG4618 222 RANARALALQAR------ASDRAGGFSAlskflrLLLQSAVLGLGAYLVIQGEITPGAMIaaSILMG--------RALap 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 292 LDYF----PTLMKAVGSSEKIFEFLDREPqvAPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLG 367
Cdd:COG4618 288 IEQAiggwKQFVSARQAYRRLNELLAAVP--AEPERMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 368 PPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISyGLGGCSWAQVTAAARRV 447
Cdd:COG4618 366 PSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLA 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 448 GAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG4618 445 GVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVIT 524
|
490 500 510
....*....|....*....|....*....|.
gi 2099372369 528 GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG4618 525 HRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
331-547 |
1.75e-59 |
|
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: 197.43 E-value: 1.75e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQV 410
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 491 ILILDEHTSALDTESQQQVEQEiLAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEV 547
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
308-557 |
5.66e-59 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 206.41 E-value: 5.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 308 IFEFLDREPQvAPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPT 387
Cdd:PRK11176 318 LFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 388 AGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGG-CSWAQVTAAARRVGAHDFITRLPQGYDTEVGE 466
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 467 LGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGE 546
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
250
....*....|.
gi 2099372369 547 VRQEGpPHEVL 557
Cdd:PRK11176 556 IVERG-THAEL 565
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-527 |
3.17e-58 |
|
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: 203.36 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 8 RRLLLSLSPERRRCAAVM---GLMAASALGEMAVP-YYMGRASDWVAREDELAAILPMVLLGLSSAV----TELVC-DVT 78
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVllgALALGSAVALLGVSaWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVfrylERLVGhDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 79 FvgtlsRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMA 158
Cdd:TIGR02868 82 L-----RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 159 LLTALALPLL-----LALPRAVGHFRQALAPQmqkaQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKK 233
Cdd:TIGR02868 157 LILAAGLLLAgfvapLVSLRAARAAEQALARL----RGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 234 DVAlytASLWTSGFSALALK---MGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFE 310
Cdd:TIGR02868 233 AAA---ATALGAALTLLAAGlavLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 311 FLDREPQVA-PSGTMAPTDLQGH--LQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPT 387
Cdd:TIGR02868 310 VLDAAGPVAeGSAPAAGAVGLGKptLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 388 AGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGEL 467
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 468 GGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAkGSGRAVLMVT 527
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLIT 527
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-542 |
5.93e-58 |
|
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: 202.52 E-value: 5.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 18 RRRCAAVMGLMAASALGEMAVPYYMGRA-SDWVAREDELAAILP----MVLLGLSSAVTELVCDVTFVGTLSRTQSRLQR 92
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVvDGLISAGEPLAELLPalgaLALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 93 RVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALP 172
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 173 RAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAA-------HYRQRLQQSHRlekkdVA-LYTASLwt 244
Cdd:TIGR02857 162 ILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAairrsseEYRERTMRVLR-----IAfLSSAVL-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 245 SGFSALALKMGILYYGGQLVAAG-TVSTGDLVtfLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPSGT 323
Cdd:TIGR02857 235 ELFATLSVALVAVYIGFRLLAGDlDLATGLFV--LLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 324 MAPTDLQGHLQLEDVWFSYPGRqEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQH 403
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 404 SYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIAR 483
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEqEILAAKGSGRAVLMVTGRAALAARAQRVVVL 542
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVL-EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
25-308 |
9.27e-54 |
|
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: 184.67 E-value: 9.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 25 MGLMAASALGEMAVPYYMGRASDWVAREDELA----AILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLR 100
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREafyrAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 101 QSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQ 180
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 181 ALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYG 260
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2099372369 261 GQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
245-557 |
3.22e-51 |
|
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: 184.47 E-value: 3.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 245 SGFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYqiqftdVLRVL------LDYFPTLMKAVGSSEKIFEFLDREPQV 318
Cdd:TIGR01842 231 SKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSIL------VGRALapidgaIGGWKQFSGARQAYKRLNELLANYPSR 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 319 APSgtMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL 398
Cdd:TIGR01842 305 DPA--MPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 399 PAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQA 478
Cdd:TIGR01842 383 KQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 479 VAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
28-308 |
3.07e-50 |
|
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: 175.19 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 28 MAASALGEMAVPYYMGRASDWVAREDELA----AILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSI 103
Cdd:cd18784 5 LLAAAVGEIFIPYYTGQVIDGIVIEKSQDkfsrAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 104 TELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQALA 183
Cdd:cd18784 85 GFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 184 PQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQL 263
Cdd:cd18784 165 KAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2099372369 264 VAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18784 245 VITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
260-557 |
8.28e-50 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 181.06 E-value: 8.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 260 GGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVApSGTMAPTDLQGHLQLEDVW 339
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPVPEGRGELDVNIRQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLL 419
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 FARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 500 ALDTESQQQVEQEiLAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGpPHEVL 557
Cdd:PRK10789 481 AVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG-NHDQL 536
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
27-308 |
9.09e-50 |
|
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: 173.90 E-value: 9.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 27 LMAASALGEMAVPYYMGRASDWVAREDELAAI----LPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQS 102
Cdd:cd18557 4 FLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLnelaLILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 103 ITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQAL 182
Cdd:cd18557 84 IAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 183 APQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQ 262
Cdd:cd18557 164 SKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2099372369 263 LVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18557 244 LVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-557 |
7.17e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 178.48 E-value: 7.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 295 FPTLMKAVGSSEKIFEFLDREPQVAPSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKS 374
Cdd:PRK11160 301 FQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 375 TLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFIT 454
Cdd:PRK11160 381 TLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 455 RlPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQeILAAKGSGRAVLMVTGRAALAA 534
Cdd:PRK11160 461 D-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILE-LLAEHAQNKTVLMITHRLTGLE 538
|
250 260
....*....|....*....|...
gi 2099372369 535 RAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK11160 539 QFDRICVMDNGQIIEQGTHQELL 561
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
254-567 |
9.08e-49 |
|
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: 178.54 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 254 MGILYYGGQLVAAGTVSTGDLVTFllyqIQFTDVLRVLLDYFPTLM-KAVGSSEKIFEFLDREPQV----APSGTMAPTD 328
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAF----IGFANLLIGRLDQMSGFItQIFEARAKLEDFFDLEDSVfqreEPADAPELPN 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 329 LQGHLQLEDVWFSYPGRQEPVlKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCR 408
Cdd:TIGR01192 331 VKGAVEFRHITFEFANSSQGV-FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRD 488
Cdd:TIGR01192 410 SIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKN 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEILAAKgSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPG----SLLR 564
Cdd:TIGR01192 490 APILVLDEATSALDVETEARVKNAIDALR-KNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDgrfyKLLR 568
|
...
gi 2099372369 565 DWG 567
Cdd:TIGR01192 569 RSG 571
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
331-553 |
1.97e-47 |
|
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: 165.36 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQV 410
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFARSLHANISyGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 491 ILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPP 553
Cdd:cd03244 160 ILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
333-562 |
2.34e-47 |
|
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: 165.99 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEP-----------LLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLpqgYDTevgelggqLSGGQRQAVAI 481
Cdd:COG1120 80 VPQEPpapfgltvrelVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALDTESQQQVeQEILA--AKGSGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEV-LELLRrlARERGRTVVMVLhdlnlaaryadrLVLLKDGRIVAQGPPEEVLT 227
|
....
gi 2099372369 559 PGSL 562
Cdd:COG1120 228 PELL 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-565 |
3.57e-47 |
|
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: 164.81 E-value: 3.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPL--LFARSLHANISYGLG--GCS----WAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARA 484
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPEnlGLPreeiRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLL 563
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVThDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
..
gi 2099372369 564 RD 565
Cdd:COG1122 229 EE 230
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-563 |
8.75e-47 |
|
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: 174.76 E-value: 8.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 5 GAGRRLLLSLSPERRRCAAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCDVTFVGTLS 84
Cdd:TIGR03797 122 GLRDLLRFALRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 85 RTQSRLQRRVFAAV----LRQSITELRADGAGDVAMRVTRDAEdVREALGEALSLLLWYLARGLCLFATMAWLSPRMALL 160
Cdd:TIGR03797 202 RLETRMDASLQAAVwdrlLRLPVSFFRQYSTGDLASRAMGISQ-IRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 161 TALALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLE-KKDVALYT 239
Cdd:TIGR03797 281 AVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLElSAQRIENL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 240 ASLWTSGFSALAlkMGILYY-GGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQV 318
Cdd:TIGR03797 361 LTVFNAVLPVLT--SAALFAaAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEV 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 319 ApSGTMAPTDLQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL 398
Cdd:TIGR03797 439 D-EAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 399 PAYQHSYLCRQVAVVPQEPLLFARSLHANIsyglggCSWAQVT-----AAARRVGAHDFITRLPQGYDTEVGELGGQLSG 473
Cdd:TIGR03797 518 AGLDVQAVRRQLGVVLQNGRLMSGSIFENI------AGGAPLTldeawEAARMAGLAEDIRAMPMGMHTVISEGGGTLSG 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 474 GQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSgRAVlmVTGRAALAARAQRVVVLEGGEVRQEGPP 553
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVT-RIV--IAHRLSTIRNADRIYVLDAGRVVQQGTY 668
|
570
....*....|
gi 2099372369 554 HEVLRPGSLL 563
Cdd:TIGR03797 669 DELMAREGLF 678
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
324-527 |
2.21e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.63 E-value: 2.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 324 MAPTDlqGHLQLEDVWFSYPGRQE--PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAy 401
Cdd:COG1116 1 MSAAA--PALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 402 qhsyLCRQVAVVPQEPLLFA-RSLHANISYGL--GGCSWAQVTAAARR----VGAHDFITRLPqgydtevgelgGQLSGG 474
Cdd:COG1116 78 ----PGPDRGVVFQEPALLPwLTVLDNVALGLelRGVPKAERRERAREllelVGLAGFEDAYP-----------HQLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 475 QRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVT 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-547 |
3.45e-43 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 151.99 E-value: 3.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANIsyglggcswaqvtaaarrvgahdfitrlpqgydtevgelggqLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEV 547
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-527 |
3.60e-43 |
|
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: 153.78 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEP--VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQhsylcRQV 410
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFA-RSLHANISYGL--GGCSWAQVTAAARR----VGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIAR 483
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLelQGVPKAEARERAEEllelVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVT 527
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVT 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-499 |
4.42e-43 |
|
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: 150.88 E-value: 4.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFAR-SLHANI 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 429 SYGLGGCSWAQVTAAARrvgAHDFITRLPQGY--DTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR---AEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
89-511 |
4.90e-43 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 162.58 E-value: 4.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 89 RLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLL 168
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 169 LALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANE--------DGAAAHYRQRLQqSHRLekkDVALYTA 240
Cdd:PRK10790 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQarfgermgEASRSHYMARMQ-TLRL---DGFLLRP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 241 SLwtSGFSALALKMGILYYGgqLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQvaP 320
Cdd:PRK10790 255 LL--SLFSALILCGLLMLFG--FSASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQ--Q 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 321 SGTMAPTDLQGHLQLEDVWFSYpGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA 400
Cdd:PRK10790 329 YGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 401 YQHSYLCRQVAVVPQEPLLFARSLHANISYGLgGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVA 480
Cdd:PRK10790 408 LSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLA 486
|
410 420 430
....*....|....*....|....*....|.
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEQ 511
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
185-557 |
6.54e-43 |
|
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: 163.76 E-value: 6.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 185 QMQKAQARASEVaVETFQAMATVRSFANEDGAAAHYRQR----LQQSHRLEKKDV---ALYTASlwtsgfsALALKMGIL 257
Cdd:TIGR01193 326 AMQANAVLNSSI-IEDLNGIETIKSLTSEAERYSKIDSEfgdyLNKSFKYQKADQgqqAIKAVT-------KLILNVVIL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 258 YYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPSGTM-APTDLQGHLQLE 336
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRtELNNLNGDIVIN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 337 DVWFSYpGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQE 416
Cdd:TIGR01193 478 DVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 PLLFARSLHANISYGLG-GCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:TIGR01193 557 PYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKgsGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQ--DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-527 |
2.84e-41 |
|
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: 148.38 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEP--LLFARSLHANISYGLGGCSWAQ------VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARAL 485
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEeeieerVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVT 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
246-551 |
2.94e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 157.31 E-value: 2.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 246 GFSAL-ALKMGilYYGGQLvaagTVSTGDLVTFL---LYQiqftdVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPS 321
Cdd:PRK11174 269 GFSYLgELNFG--HYGTGV----TLFAGFFVLILapeFYQ-----PLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQ 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 322 GTmAPTDLQGHLQLE--DVW-FSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLhqPTAGRLLLDGHP 397
Cdd:PRK11174 338 GE-KELASNDPVTIEaeDLEiLSPDGK--TLAGPLNFTLPAGQRIALVGPSGAGKTSLLnALLGFL--PYQGSLKINGIE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 398 LPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQ 477
Cdd:PRK11174 413 LRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKgSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEG 551
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-558 |
1.08e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 147.52 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLcRQVAV 412
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFAR-SLHANISY--GLGGCSWAQVTAAA----RRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARAL 485
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFfaRLYGLPRKEARERIdellELFGLTDAADRKV-----------GTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSThyleeaerlcdrVAIIDKGRIVADGTPDELKA 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-527 |
1.40e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANISYGLG----GCSWAQVTAAARRVGahdfitrLPQGY-DTEVGELggqlSGGQRQAVAIARALLR 487
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQlrerKFDRERALELLERLG-------LPPDIlDKPVERL----SGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVS 188
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-567 |
2.35e-40 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.77 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHsylcrQVAV 412
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARR-----RIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQ-------------EPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLpqgydteVGELggqlSGGQRQAV 479
Cdd:COG1121 80 VPQraevdwdfpitvrDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRP-------IGEL----SGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 480 AIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRqEGPPHEVLR 558
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVThDLGAVREYFDRVLLLNRGLVA-HGPPEEVLT 227
|
....*....
gi 2099372369 559 PGSLLRDWG 567
Cdd:COG1121 228 PENLSRAYG 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-527 |
2.08e-39 |
|
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: 142.19 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQepllfarslhanisyglggcswaqvtaAARRVGAHDFITRlpqGYDTevgelggqLSGGQRQAVAIARALLRDPRILI 493
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 494 LDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlARERGKTVVMVL 155
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-551 |
3.13e-39 |
|
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: 141.68 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSyLCRQVAV 412
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANisyglggcswaqvtaaarrvgahdfitrlpqgydtevgeLGGQLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03247 80 LNQRPYLFDTTLRNN---------------------------------------LGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 493 ILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEG 551
Cdd:cd03247 121 LLDEPTVGLDPITERQL-LSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-527 |
7.27e-39 |
|
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: 140.23 E-value: 7.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYlCRQVAV 412
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV-KRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPllfarSLHANISyglggcswaqvtaaarrvgAHDFItrlpqgydtevgelggQLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03230 78 LPEEP-----SLYENLT-------------------VRENL----------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSS 152
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
338-527 |
8.65e-39 |
|
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: 142.63 E-value: 8.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 338 VWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEP 417
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLfarSLHANIS-----------YGLGGcSWAQVTAAARRVG-AHDFITRLPQgydtevgelggQLSGGQRQAVAIARAL 485
Cdd:COG1124 89 YA---SLHPRHTvdrilaeplriHGLPD-REERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVEQEILAAKG-SGRAVLMVT 527
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVS 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-564 |
9.71e-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: 149.28 E-value: 9.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTA---GRLLLDGHPLPAYQHSYLCRQ 409
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPL--LFARSLHANISYGL--GGCSWAQ----VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAI 481
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALenLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEGPPHEVLRP 559
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
....*
gi 2099372369 560 GSLLR 564
Cdd:COG1123 234 PQALA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
303-558 |
1.11e-37 |
|
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: 146.20 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 303 GSSEKIFE---FLDREPQVAPSGTMAPTDLQGH---LQLEDVWFSYPGRQE---PVLKGVSLELRPGEVLALLGPPGAGK 373
Cdd:COG1123 225 GPPEEILAapqALAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 374 STLVALVSRLHQPTAGRLLLDGHPLPAYQHS---YLCRQVAVVPQEPL--LFAR-SLHANISYGL---GGCS----WAQV 440
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYssLNPRmTVGDIIAEPLrlhGLLSraerRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 441 TAAARRVG-AHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKG 518
Cdd:COG1123 385 AELLERVGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRE 453
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2099372369 519 SGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG1123 454 LGLTYLFIShdlavvryiadrVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-527 |
1.19e-37 |
|
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: 138.79 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLED--VWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH---PLPAYQHSYLC 407
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 408 RQVAVVPQ-----------------EPLLFARSLHANISYglggcsWAQVTAAARRVG-AHDFITRLPQgydtevgelgg 469
Cdd:cd03257 82 KEIQMVFQdpmsslnprmtigeqiaEPLRIHGKLSKKEAR------KEAVLLLLVGVGlPEEVLNRYPH----------- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 470 QLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEIL-AAKGSGRAVLMVT 527
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKkLQEELGLTLLFIT 203
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-558 |
1.28e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.54 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsylcRQ 409
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtgLPPEK-----RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFA-RSLHANISYGLGGCSW------AQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIA 482
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGLRMRGVpkaeirARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVThdqeealaladrIAVMNDGRIEQVGTPEEIYE 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-527 |
1.30e-37 |
|
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: 138.39 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQE--PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY----QHSYL 406
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 CRQVAVVPQE---------------PLLFARSLHANISyglggcswAQVTAAARRVGAHDFITRLPqgydtevgelgGQL 471
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGVPKKERR--------ERAEELLERVGLGDRLNHYP-----------SEL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 472 SGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVT 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-527 |
1.46e-37 |
|
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: 136.22 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQepllfarslhanisyglggcswaqvtaaarrvgahdfitrlpqgydtevgelggqLSGGQRQAVAIARALLRDPRILI 493
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190
....*....|....*....|....*....|....
gi 2099372369 494 LDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVT 137
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
333-527 |
2.51e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.87 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYP-GRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYL---- 406
Cdd:COG1136 5 LELRNLTKSYGtGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 CRQVAVVPQEPLLFAR-SLHANISYGL--GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAV 479
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALPLllAGVSRKERRERARelleRVGLGDRLDHRP-----------SQLSGGQQQRV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099372369 480 AIARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVT 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-527 |
3.79e-37 |
|
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: 136.89 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHsylcrQVAVV 413
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQ-------------EPLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVA 480
Cdd:cd03235 74 PQrrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQI-----------GELSGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVT 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-556 |
1.80e-36 |
|
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: 135.77 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLH-----QPTAGRLLLDGHPLPAYQHS--Y 405
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQEPLLFARSLHANISYG--LGGCSWAQ-----VTAAARRVGAHDfitrlpqgydtEVGE--LGGQLSGGQR 476
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrLHGIKLKEelderVEEALRKAALWD-----------EVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSgRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHE 555
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVThNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2099372369 556 V 556
Cdd:cd03260 227 I 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
333-557 |
1.87e-36 |
|
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: 136.14 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPlPAYQHSYLCRQVAV 412
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFAR-SLHANISYglggcswaqvTAAARRVGAHDFITR---------LPQGYDTEVGELggqlSGGQRQAVAIA 482
Cdd:COG4555 79 LPDERGLYDRlTVRENIRY----------FAELYGLFDEELKKRieeliellgLEEFLDRRVGEL----STGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEGPPHEVL 557
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELR 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
333-557 |
6.21e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.35 E-value: 6.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL--PAYQHSYLCRQV 410
Cdd:COG1126 2 IEIENLHKSF-GDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFArslHA----NISYGL---GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAV 479
Cdd:COG1126 80 GMVFQQFNLFP---HLtvleNVTLAPikvKKMSKAEAEERAMelleRVGLADKADAYP-----------AQLSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 480 AIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVL 557
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVThemgfarevadrVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-551 |
5.87e-35 |
|
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: 131.10 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrqEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsylcRQ 409
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFA-RSLHANISYGLGGCSW------AQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIA 482
Cdd:cd03259 74 IGMVFQDYALFPhLTVAENIAFGLKLRGVpkaeirARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEG 551
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVThDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
333-527 |
1.42e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQHSYLCRQ 409
Cdd:COG2884 2 IRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQE-PLLFARSLHANISYGL--GGCSWAQ----VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENVALPLrvTGKSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAT 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
333-509 |
1.55e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.95 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQ 409
Cdd:COG3638 3 LELRNLSKRYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFARS------LHANISYGLGGCSWAQVTAAARRVGAHDFITRlpqgydteVGELG------GQLSGGQRQ 477
Cdd:COG3638 82 IGMIFQQFNLVPRLsvltnvLAGRLGRTSTWRSLLGLFPPEDRERALEALER--------VGLADkayqraDQLSGGQQQ 153
|
170 180 190
....*....|....*....|....*....|..
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQV 185
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
333-527 |
1.57e-34 |
|
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: 129.52 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYlCRQVAV 412
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFAR-SLHANISY--GLGGCSW--AQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLR 487
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaALYGLRAdrEAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTT 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
272-519 |
1.59e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 140.16 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 272 GDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQVAPSGTMAPTDLQGHLQLEDVWFSYPGRQE-PVL 350
Cdd:PTZ00265 322 GSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDvEIY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 351 KGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLL-DGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANIS 429
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 430 YGL-------------------------------GGCSW--------------------------AQVTAAARRVGAHDF 452
Cdd:PTZ00265 482 YSLyslkdlealsnyynedgndsqenknkrnscrAKCAGdlndmsnttdsneliemrknyqtikdSEVVDVSKKVLIHDF 561
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 453 ITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS 519
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
333-527 |
5.00e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.15 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLP------AYQHSyl 406
Cdd:COG1129 5 LEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 crqVAVVPQEPLLFA-RSLHANISYG-----LGGCSWAQVTAAARRVgahdfITRLpqGYDTEVGELGGQLSGGQRQAVA 480
Cdd:COG1129 81 ---IAIIHQELNLVPnLSVAENIFLGreprrGGLIDWRAMRRRAREL-----LARL--GLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2099372369 481 IARALLRDPRILILDEHTSALdteSQQQVEQ--EILAA-KGSGRAVLMVT 527
Cdd:COG1129 151 IARALSRDARVLILDEPTASL---TEREVERlfRIIRRlKAQGVAIIYIS 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-558 |
1.32e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.95 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqepvLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG---HPLPAYQhsylcRQ 409
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdlTALPPAE-----RP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANISYGLG-GCS-----WAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIA 482
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNIGLGLRpGLKltaeqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 483 RALLRDPRILILDEHTSALDtesqQQVEQEILA-----AKGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEGPPHEV 556
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALD----PALRQEMLDlvdelCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAAL 217
|
..
gi 2099372369 557 LR 558
Cdd:COG3840 218 LD 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
199-557 |
1.77e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 136.70 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 199 ETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVaLYTASLWtsGFSALA---LKMGILYYGGQLVAAGTVSTGD-- 273
Cdd:PTZ00265 1027 EAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKT-LVNSMLW--GFSQSAqlfINSFAYWFGSFLIRRGTILVDDfm 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 274 --LVTFLlyqiqFTDvlrvllDYFPTLMKAVGSSE-------KIFEFLDREP--QVAPSGTMA---PTDLQGHLQLEDVW 339
Cdd:PTZ00265 1104 ksLFTFL-----FTG------SYAGKLMSLKGDSEnaklsfeKYYPLIIRKSniDVRDNGGIRiknKNDIKGKIEIMDVN 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ--------------------------------- 385
Cdd:PTZ00265 1173 FRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgm 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 386 ---------------------PTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSWAQVTAAA 444
Cdd:PTZ00265 1253 knvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRAC 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 445 RRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSG-RAV 523
Cdd:PTZ00265 1333 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1412
|
410 420 430
....*....|....*....|....*....|....*....
gi 2099372369 524 LMVTGRAALAARAQRVVVLE-----GGEVRQEGPPHEVL 557
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELL 1451
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-527 |
2.35e-33 |
|
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: 126.49 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA-YQHSYLCRQ-V 410
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQkV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFA-RSLHANISYGL---GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIA 482
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITLAPikvKGMSKAEAEERALelleKVGLADKADAYP-----------AQLSGGQQQRVAIA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVT 192
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
333-566 |
3.64e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.54 E-value: 3.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:COG4559 2 LEAENLSVRLGGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQE-PLLFARSLHANIsyGLGGCSWAQ--------VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIAR 483
Cdd:COG4559 80 LPQHsSLAFPFTVEEVV--ALGRAPHGSsaaqdrqiVREALALVGLAHLAGRSYQ-----------TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 484 ALL-------RDPRILILDEHTSALDTESQQQVEQEI--LAAKGSGraVLMV------------TgraalaaraqrVVVL 542
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLArqLARRGGG--VVAVlhdlnlaaqyadR-----------ILLL 213
|
250 260
....*....|....*....|....
gi 2099372369 543 EGGEVRQEGPPHEVLRPgSLLRDW 566
Cdd:COG4559 214 HQGRLVAQGTPEEVLTD-ELLERV 236
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
28-308 |
3.85e-33 |
|
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: 128.22 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 28 MAASALGEMAVPYYMGRASDWVAREDE----LAAILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSI 103
Cdd:cd18590 5 LTLAVICETFIPYYTGRVIDILGGEYQhnafTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 104 TELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQALA 183
Cdd:cd18590 85 GFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 184 PQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQL 263
Cdd:cd18590 165 QAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2099372369 264 VAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18590 245 IQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-562 |
1.74e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.96 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLcRQVAV 412
Cdd:COG1118 3 IEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRE-RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFArslH----ANISYGL--GGCSWAQVTAAARR----VGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIA 482
Cdd:COG1118 80 VFQHYALFP---HmtvaENIAFGLrvRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQ---EILaaKGSGRAVLMVTgraala-araqrVVVLEGGEVRQEGPPHEVL- 557
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRwlrRLH--DELGGTTVFVThdqeealeladrVVVMNQGRIEQVGTPDEVYd 223
|
....*
gi 2099372369 558 RPGSL 562
Cdd:COG1118 224 RPATP 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
333-567 |
2.26e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.27 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK13548 3 LEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLL-FARSLHANIsyGLGGCSWAQ--------VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIAR 483
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVV--AMGRAPHGLsraeddalVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 484 ALLR------DPRILILDEHTSALDTESQQQVEQeiLA---AKGSGRAVLMV------TgraalAARAQRVVVLEGGEVR 548
Cdd:PRK13548 148 VLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLR--LArqlAHERGLAVIVVlhdlnlA-----ARYADRIVLLHQGRLV 220
|
250
....*....|....*....
gi 2099372369 549 QEGPPHEVLRPGSLLRDWG 567
Cdd:PRK13548 221 ADGTPAEVLTPETLRRVYG 239
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
29-285 |
2.33e-32 |
|
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: 125.83 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 29 AASALGEMAVPYYMGRASDWV----AREDELAAILPMVL--LGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQS 102
Cdd:pfam00664 9 ILSGAISPAFPLVLGRILDVLlpdgDPETQALNVYSLALllLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 103 ITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQAL 182
Cdd:pfam00664 89 MSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 183 APQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQ 262
Cdd:pfam00664 169 SRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAY 248
|
250 260
....*....|....*....|...
gi 2099372369 263 LVAAGTVSTGDLVTFLLYQIQFT 285
Cdd:pfam00664 249 LVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-527 |
3.97e-32 |
|
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: 121.38 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrqEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPlpayqhsylcrqvaV 412
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPllfarslhanisyglggcswaqvtAAARRVGahdfITRLPQgydtevgelggqLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03216 65 SFASP------------------------RDARRAG----IAMVYQ------------LSVGERQMVEIARALARNARLL 104
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFIS 139
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-556 |
7.88e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 7.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsylcRQ 409
Cdd:COG3839 4 LELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPKD-----RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLF-ARSLHANISYGLggcSWA---------QVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAV 479
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPL---KLRkvpkaeidrRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 480 AIARALLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVT---------GraalaaraQRVVVLEGGEVRQ 549
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVThdqveamtlA--------DRIAVMNDGRIQQ 214
|
....*..
gi 2099372369 550 EGPPHEV 556
Cdd:COG3839 215 VGTPEEL 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
340-557 |
8.73e-32 |
|
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: 122.69 E-value: 8.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQVAVVPQE 416
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRkarRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 -PLLFARSLHANISYGL--GGCSWAQVTAAARR----VGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDP 489
Cdd:cd03258 91 fNLLSSRTVFENVALPLeiAGVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 490 RILILDEHTSALDTESQQQveqeILA-----AKGSGRAVLMVTGRAALAARA-QRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03258 160 KVLLCDEATSALDPETTQS----ILAllrdiNRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
334-527 |
1.31e-31 |
|
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: 121.60 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSylcRQVAVV 413
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEP--LLFARSLHANISYGLGGCSWAQVTAAA--RRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDP 489
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQAETvlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGK 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIT 183
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
348-557 |
9.24e-31 |
|
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: 119.46 E-value: 9.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VAVVPQEPLLFAR-SLH 425
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYGLGGCSWAQVTAAARRVgaHDFITRLPQGYDTevgeLGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:cd03224 94 ENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 506 QQQVEQEILAAKGSGRAVLMV-TGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03224 168 VEEIFEAIRELRDEGVTILLVeQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-527 |
1.10e-30 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 118.06 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL--PAYQHSYLCRQV 410
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFAR-SLHANISYGLggcswaqvtaaarrvgahdfitrlpqgydtevgelggqlSGGQRQAVAIARALLRDP 489
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMDP 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVT 158
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
346-556 |
2.39e-30 |
|
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: 118.88 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG---HPLPAYQhsylcRQVAVVPQEPLLFAR 422
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPHK-----RPVNTVFQNYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 -SLHANISYGL------GGCSWAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:cd03300 87 lTVFENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 496 EHTSALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEV 556
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRlQKELGITFVFVThDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-558 |
2.90e-30 |
|
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: 118.94 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFA-RSLHANISYGLGGCSWAQVTAAAR--------RVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIAR 483
Cdd:cd03295 80 VIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERadellalvGLDPAEFADRYP-----------HELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRlQQELGKTIVFVThDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
333-558 |
3.23e-30 |
|
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: 118.55 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsyLCRQ 409
Cdd:COG0410 4 LEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHR---IARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 -VAVVPQEPLLFAR-SLHANIsyglggcswaqVTAAARRVGAHDFITRLPQGYDT--EVGE----LGGQLSGGQRQAVAI 481
Cdd:COG0410 79 gIGYVPEGRRIFPSlTVEENL-----------LLGAYARRDRAEVRADLERVYELfpRLKErrrqRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALdtesQQQVEQEILAA----KGSGRAVLMV------------TGraalaaraqrvVVLEGG 545
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGL----APLIVEEIFEIirrlNREGVTILLVeqnarfaleiadRA-----------YVLERG 212
|
250
....*....|...
gi 2099372369 546 EVRQEGPPHEVLR 558
Cdd:COG0410 213 RIVLEGTAAELLA 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-567 |
6.46e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEP--LLFARSLHANISYGLGGCSWA------QVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARA 484
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGLENIGVPreemveRVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRA-VLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLL 563
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
....
gi 2099372369 564 RDWG 567
Cdd:PRK13635 235 QEIG 238
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
28-308 |
6.52e-30 |
|
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: 119.28 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 28 MAASALGEMAVPYYMGRASDWV----------AREDELAAILPMVLLGLSSAVTELVcdVTFVGTLS--RTQSRLQRRVF 95
Cdd:cd18780 5 LLVSSGTNLALPYFFGQVIDAVtnhsgsggeeALRALNQAVLILLGVVLIGSIATFL--RSWLFTLAgeRVVARLRKRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 96 AAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAV 175
Cdd:cd18780 83 SAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 176 GHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKdVALYTAslWTSGFSALALKMG 255
Cdd:cd18780 163 GKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKK-LARASG--GFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 256 I---LYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18780 240 IvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-526 |
7.16e-30 |
|
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: 117.67 E-value: 7.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQ 409
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANIsygLGGcswaqvtaaarRVGAHDFITRLPQGYDTE-----------VGELG------GQL 471
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENV---LSG-----------RLGRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 472 SGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEIL-AAKGSGRAVLMV 526
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrINREEGITVIVS 201
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
25-308 |
7.73e-30 |
|
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: 119.16 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 25 MGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVC--------DVTFVGTLS-RTQSRLQRRVF 95
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVvgaaanfgRVYLLRIAGeRIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 96 AAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAV 175
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 176 GHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKdVALYTASLWTS-GFSALALKM 254
Cdd:cd18573 162 GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKK-EALASGLFFGStGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 255 GILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
332-509 |
8.12e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.18 E-value: 8.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 332 HLQLEDVWFSYPGRQEPV--LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC-- 407
Cdd:COG1135 1 MIELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 408 -RQVAVVPQEP-LLFARSLHANISYGLggcSWAQVTAAARR---------VGAHDFITRLPqgydtevgelgGQLSGGQR 476
Cdd:COG1135 81 rRKIGMIFQHFnLLSSRTVAENVALPL---EIAGVPKAEIRkrvaellelVGLSDKADAYP-----------SQLSGGQK 146
|
170 180 190
....*....|....*....|....*....|...
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSI 179
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-558 |
8.43e-30 |
|
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: 117.22 E-value: 8.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQ 409
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLF-ARSLHANISYGL---GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAI 481
Cdd:cd03261 79 MGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREIVLekleAVGLRGAEDLYP-----------AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 482 ARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS-GRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVThDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
347-557 |
3.66e-29 |
|
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: 115.51 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 347 EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH---PLPAYQhsylcRQVAVVPQEPLLFAR- 422
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGLGGCSW------AQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:cd03299 87 TVYKNIAYGLKKRKVdkkeieRKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 497 HTSALDTESQQQVEQEI-LAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03299 156 PFSALDVRTKEKLREELkKIRKEFGVTVLHVThDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
280-557 |
4.43e-29 |
|
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: 123.13 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 280 YQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDREPQvAP---SGTMAPTDL--QGHLQLEDVWFSYPGRQEPVLKGVS 354
Cdd:TIGR00957 1228 YSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE-APwqiQETAPPSGWppRGRVEFRNYCLRYREDLDLVLRHIN 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 355 LELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISyGLGG 434
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQ 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 435 CSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVeQEIL 514
Cdd:TIGR00957 1386 YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI-QSTI 1464
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2099372369 515 AAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-551 |
6.38e-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: 114.21 E-value: 6.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGeVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAyQHSYLCRQVAV 412
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFAR-SLHANISY--GLGGCSWAQVTAAARR----VGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARAL 485
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYiaWLKGIPSKEVKARVDEvlelVNLGDRAKKKI-----------GSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEG 551
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRF-RNLLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-575 |
2.61e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 120.85 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 58 ILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSL-- 135
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMfm 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 136 -LLWYLARGLCLFATMAWLSprmalltALALPLLLALPRAVGHFRQALAPQMQKAQA--RASEVAV--ETFQAMATVRSF 210
Cdd:PLN03232 1033 nQLWQLLSTFALIGTVSTIS-------LWAIMPLLILFYAAYLYYQSTSREVRRLDSvtRSPIYAQfgEALNGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 211 ANEDGAAAHYRQRLQQSHR-----------LEKKDVALYTASLW-TSGFSalalkmgILYYGGQLVAAGTVSTGDLVtfL 278
Cdd:PLN03232 1106 KAYDRMAKINGKSMDNNIRftlantssnrwLTIRLETLGGVMIWlTATFA-------VLRNGNAENQAGFASTMGLL--L 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 279 LYQIQFTDVLRVLLDYFPTLMKAVGSSEKIFEFLDRePQVAPS---GTMAPTD--LQGHLQLEDVWFSYPGRQEPVLKGV 353
Cdd:PLN03232 1177 SYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDL-PSEATAiieNNRPVSGwpSRGSIKFEDVHLRYRPGLPPVLHGL 1255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 354 SLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISyGLG 433
Cdd:PLN03232 1256 SFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFS 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 434 GCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI 1414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 514 LAAKGSGrAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL-RPGSLLRDWGQQGAPGEG 575
Cdd:PLN03232 1415 REEFKSC-TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANA 1476
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
326-553 |
2.62e-28 |
|
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: 112.12 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 326 PTDlqGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY 405
Cdd:cd03369 2 PEH--GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQEPLLFARSLHANISYgLGGCSWAQVTAAARrvgahdfitrlpqgydteVGELGGQLSGGQRQAVAIARAL 485
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVeQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPP 553
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALI-QKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
21-308 |
4.40e-28 |
|
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: 114.18 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 21 CAAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILP----MVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFA 96
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWiallLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 97 AVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVG 176
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 177 HFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVAL-YTASLWTSGFSALALkMG 255
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLsALFSPLIGLLTALGT-AL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 256 ILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-527 |
4.68e-28 |
|
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: 114.77 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPV--LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP---TAGRLLLDGHPL----PAYQH 403
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 404 SYLCRQVAVVPQEPL-----------LFARSLHANisyglGGCSWAQVTAAA----RRVG---AHDFITRLPqgydtevg 465
Cdd:COG0444 82 KIRGREIQMIFQDPMtslnpvmtvgdQIAEPLRIH-----GGLSKAEARERAiellERVGlpdPERRLDRYP-------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 466 elgGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI--LAAKgSGRAVLMVT 527
Cdd:COG0444 149 ---HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRE-LGLAILFIT 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-558 |
7.77e-28 |
|
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: 112.00 E-value: 7.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHS---YLCRQ 409
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLF-ARSLHANISYGL---GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAI 481
Cdd:COG1127 84 IGMLFQGGALFdSLTVFENVAFPLrehTDLSEAEIRELVLekleLVGLPGAADKMP-----------SELSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 482 ARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS-GRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVThDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-558 |
1.15e-27 |
|
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: 111.37 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsyLCRQ-VAVVPQEPLLFAR-- 422
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHE---IARLgIGRTFQIPRLFPElt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 -------SLHANISYGLGGCSWAQVTAAARRVgAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:cd03219 92 vlenvmvAAQARTGSGLLLARARREEREARER-AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGSGRAVLM-------VTGraalaaRAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLvehdmdvVMS------LADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-546 |
1.34e-27 |
|
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: 110.25 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQE---PVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHqptagrlLLDGHplpayqhSYLCR 408
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLGELE-------KLSGS-------VSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHANIsygLGGCSWAQ------VTAAARRVgahDfITRLPQGYDTEVGELGGQLSGGQRQAVAIA 482
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENI---LFGKPFDEeryekvIKACALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 483 RALLRDPRILILDEHTSALDTE-SQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGE 546
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-556 |
1.64e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.27 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsylcRQ 409
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithVPAEN-----RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANISYGL--GGCSWAQVTA----AARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:PRK09452 88 VNTVFQSYALFPHmTVFENVAFGLrmQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEV 556
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKAlQRKLGITFVFVThDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
353-571 |
2.65e-27 |
|
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: 113.27 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---------LPAYQhsylcRQVAVVPQEPLLFA-R 422
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargifLPPHR-----RRIGYVFQEARLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGlggcsWAQVTAAARRVGAHDFITRLpqgydtEVGEL----GGQLSGGQRQAVAIARALLRDPRILILDEHT 498
Cdd:COG4148 93 SVRGNLLYG-----RKRAPRAERRISFDEVVELL------GIGHLldrrPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 499 SALDTESQqqveQEILA-----AKGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDWGQQGA 571
Cdd:COG4148 162 AALDLARK----AEILPylerlRDELDIPILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEA 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-527 |
6.61e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 332 HLQLEDVWFSYPGR--QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL--PAYQHsylc 407
Cdd:COG4525 3 MLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 408 rqvAVVPQ-EPLLFARSLHANISYGL--GGCSWAQVTAAARR----VGAHDFITRLPQgydtevgelggQLSGGQRQAVA 480
Cdd:COG4525 79 ---GVVFQkDALLPWLNVLDNVAFGLrlRGVPKAERRARAEEllalVGLADFARRRIW-----------QLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVeQEIL--AAKGSGRAVLMVT 527
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQM-QELLldVWQRTGKGVFLIT 192
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-557 |
9.09e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEP--LLFARSLHANISYGL------GGCSWAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARAL 485
Cdd:PRK13632 89 FQNPdnQFIGATVEDDIAFGLenkkvpPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVEQEI--LAAKGSgRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMvdLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-502 |
1.51e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 354 SLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG----HPLPAYqhsylcRQVAVVPQEPLLFAR-SLHANI 428
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhtTTPPSR------RPVSMLFQENNLFSHlTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 429 SYG------LGGCSWAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:PRK10771 93 GLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
333-527 |
2.12e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 108.25 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL--PAYQhsylcRQV 410
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----RGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 aVVPQEPLLFARSLHANISYGLggcSWAQVTAAARRVGAHDFITRlpqgydteVGELGG------QLSGGQRQAVAIARA 484
Cdd:PRK11248 75 -VFQNEGLLPWRNVQDNVAFGL---QLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVT 527
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLIT 186
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-527 |
3.26e-26 |
|
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: 106.82 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpaYQHSYLCRQ-VA 411
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQsLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEPLLF----ARSlHANISYGLGGCSW----AQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIAR 483
Cdd:cd03263 79 YCPQFDALFdeltVRE-HLRFYARLKGLPKseikEEVELLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILAAKgSGRAVLMVT 527
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTT 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
341-527 |
3.82e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 341 SYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY--QHSYLCRQVAVVPQEPL 418
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYvpQRSEVPDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LFARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRlpqgydtEVGELggqlSGGQRQAVAIARALLRDPRILILDEHT 498
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGR-------QLGEL----SGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180
....*....|....*....|....*....
gi 2099372369 499 SALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVT 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-513 |
5.10e-26 |
|
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: 105.80 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH---PLPAYQhsylcRQ 409
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANISYGLGGCSW------AQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:cd03301 74 IAMVFQNYALYPHmTVYDNIAFGLKLRKVpkdeidERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALG 142
|
170 180 190
....*....|....*....|....*....|.
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAEL 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
333-527 |
6.71e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP---TAGRLLLDGH---PLPAYQhsyl 406
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltALPAEQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 cRQVAVVPQEPLLFAR-SLHANISYGL-----GGCSWAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVA 480
Cdd:COG4136 76 -RRIGILFQDDLLFPHlSVGENLAFALpptigRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVT 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
350-513 |
6.80e-26 |
|
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: 105.45 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELR---PGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---------LPAYQhsylcRQVAVVPQEP 417
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinLPPQQ-----RKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFAR-SLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDtevgelgGQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:cd03297 85 ALFPHlNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
|
170
....*....|....*..
gi 2099372369 497 HTSALDTESQQQVEQEI 513
Cdd:cd03297 158 PFSALDRALRLQLLPEL 174
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
349-558 |
9.79e-26 |
|
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: 106.28 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQhsyLCRQ--------VAVVPQ-- 415
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHR---IARLgiartfqnPRLFPElt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 --EPLLFARSLHANISY---GLGGCSWAQVTAAARRVgAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:COG0411 96 vlENVLVAAHARLGRGLlaaLLRLPRARREEREARER-AEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 491 ILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMV------------TgraalaaraqrVVVLEGGEVRQEGPPHEVL 557
Cdd:COG0411 173 LLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIehdmdlvmgladR-----------IVVLDFGRVIAEGTPAEVR 241
|
.
gi 2099372369 558 R 558
Cdd:COG0411 242 A 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-527 |
1.04e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 106.27 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 323 TMAPTDLQGHLQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLH--QPTA---GRLLLDGHP 397
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 398 LpaYQHSY----LCRQVAVVPQEPLLFARSLHANISYGL---GGCSWAQ----VTAAARRVGAHDfitrlpqgydtEV-- 464
Cdd:COG1117 80 I--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhGIKSKSEldeiVEESLRKAALWD-----------EVkd 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 465 --GELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSgRAVLMVT 527
Cdd:COG1117 147 rlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVT 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
344-509 |
1.18e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.90 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 344 GRQEPVLK---GVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYL---CRQVAVVPQEP 417
Cdd:COG4608 25 GRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 llFArSLH------ANISYGL---GGCSWAQVTAAAR----RVG-AHDFITRLPQgydtevgelggQLSGGQRQAVAIAR 483
Cdd:COG4608 105 --YA-SLNprmtvgDIIAEPLrihGLASKAERRERVAelleLVGlRPEHADRYPH-----------EFSGGQRQRIGIAR 170
|
170 180
....*....|....*....|....*.
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVSIQAQV 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
333-564 |
1.40e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYL-CRQ-V 410
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKtV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEP--LLFARSLHANISYG---LGGCS---WAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGplnLGLSKeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGS 561
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISThDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
...
gi 2099372369 562 LLR 564
Cdd:PRK13639 230 TIR 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
353-558 |
1.65e-25 |
|
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: 106.19 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLcRQV-----AVVPQEPLLFA-RSLHA 426
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKEL-RELrrkkiSMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGL--GGCSWAQVTAAAR----RVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDEHTSA 500
Cdd:cd03294 122 NVAFGLevQGVPRAEREERAAealeLVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 501 LDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:cd03294 191 LDPLIRREMQDELLRlQAELQKTIVFIThDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
347-565 |
2.26e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 347 EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLL------- 419
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpegitvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 ----FARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:PRK11231 95 elvaYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGsLLRD 565
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLhDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG-LLRT 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-527 |
4.65e-25 |
|
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: 103.26 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHS---YLCRQ 409
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQE-PLLFARSLHANISYGL-----GGCSWAQ-VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:cd03292 80 IGVVFQDfRLLPDRNVYENVAFALevtgvPPREIRKrVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAT 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-501 |
4.78e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.98 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 324 MAPTDLqghLQLEDVWFSYPGrqEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL----P 399
Cdd:PRK15439 6 TTAPPL---LCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 400 AYQHS---YLcrqvavVPQEPLLFAR-SLHANISYGLggcswAQVTAAARRVGAhdFITRLPQGYDTEVgeLGGQLSGGQ 475
Cdd:PRK15439 81 AKAHQlgiYL------VPQEPLLFPNlSVKENILFGL-----PKRQASMQKMKQ--LLAALGCQLDLDS--SAGSLEVAD 145
|
170 180
....*....|....*....|....*.
gi 2099372369 476 RQAVAIARALLRDPRILILDEHTSAL 501
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASL 171
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
346-568 |
6.22e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 6.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL--PAYQHSYLCRQVAVVPQEPLLFARs 423
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPH- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHA--NISYG---LGGCSwaqvTAAARRVgAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHT 498
Cdd:PRK09493 92 LTAleNVMFGplrVRGAS----KEEAEKQ-ARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 499 SALDTESQQQVEQEILAAKGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEGPPHEVLR--PGSLLRDWGQ 568
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKnpPSQRLQEFLQ 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-527 |
6.59e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.26 E-value: 6.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK10247 8 LQLQNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANISYglggcSWAQVTAAARRVGAHDFITR--LPqgyDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIF-----PWQIRNQQPDPAIFLDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2099372369 491 ILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT 527
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLWVT 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
340-509 |
6.70e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.04 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQVAVVPQE 416
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 -PLLFARSLHANISYGL--GGCSWAQVTAAA----RRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDP 489
Cdd:PRK11153 91 fNLLSSRTVFDNVALPLelAGTPKAEIKARVtellELVGLSDKADRYP-----------AQLSGGQKQRVAIARALASNP 159
|
170 180
....*....|....*....|
gi 2099372369 490 RILILDEHTSALDTESQQQV 509
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSI 179
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-527 |
9.91e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAYQHSylcRQVAVVPQEPLL------ 419
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRA---KYIGRVFQDPMMgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 -----FARSLHANISYGLGgcsWAqVTAAaRRVGAHDFITRLPQGY----DTEVGelggQLSGGQRQAVAIARALLRDPR 490
Cdd:COG1101 98 tieenLALAYRRGKRRGLR---RG-LTKK-RRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 491 ILILDEHTSALDTESQQQVEQ---EILAAKgsGRAVLMVT 527
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLElteKIVEEN--NLTTLMVT 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
331-502 |
1.34e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.44 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQV 410
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFARSLHANISyGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPR 490
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|..
gi 2099372369 491 ILILDEHTSALD 502
Cdd:PLN03130 1395 ILVLDEATAAVD 1406
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-562 |
1.43e-24 |
|
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: 102.86 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAG---RLLldGHPL----------- 398
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRggedvwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 399 -----PAYQHSYL----CRQVAVvpqepllfarS-LHANIsyGLggcsWAQVTAAARRVgAHDFITRLpqgydtEVGELG 468
Cdd:COG1119 80 iglvsPALQLRFPrdetVLDVVL----------SgFFDSI--GL----YREPTDEQRER-ARELLELL------GLAHLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 469 ----GQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQ--EILAAKGSgRAVLMVT--------Graalaa 534
Cdd:COG1119 137 drpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAllDKLAAEGA-PTLVLVThhveeippG------ 209
|
250 260
....*....|....*....|....*...
gi 2099372369 535 rAQRVVVLEGGEVRQEGPPHEVLRPGSL 562
Cdd:COG1119 210 -ITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
61-308 |
1.50e-24 |
|
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: 104.09 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 61 MVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYL 140
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 141 ARGLCLFAT-----------MAWLSPRMALLTAlalplllalprAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRS 209
Cdd:cd18577 133 STFIAGFIIafiyswkltlvLLATLPLIAIVGG-----------IMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 210 FANEDGAAAHYRQRLQQSHRLEKKdVALYTA----SLWTSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFT 285
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGIK-KGLVSGlglgLLFFIIFAMYAL---AFWYGSRLVRDGEISPGDVLTVFFAVLIGA 277
|
250 260
....*....|....*....|...
gi 2099372369 286 DVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18577 278 FSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-527 |
2.11e-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: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL-PAYQHS--YLCRQ 409
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNRigYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVP----QEPLLFARSLHanisyGLGgcswaqVTAAARRVgaHDFITRLpqgydtevgELGG-------QLSGGQRQA 478
Cdd:cd03269 79 RGLYPkmkvIDQLVYLAQLK-----GLK------KEEARRRI--DEWLERL---------ELSEyankrveELSKGNQQK 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099372369 479 VAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILST 185
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
348-556 |
4.54e-24 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 101.26 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHplPAYQHSYLCRQVAVVPQEPLLFAR-SLHA 426
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGL------GGCSWAQVTAAARR----VGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:cd03296 94 NVAFGLrvkprsERPPEAEIRAKVHEllklVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 497 HTSALDTesqqQVEQEI------LAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEV 556
Cdd:cd03296 163 PFGALDA----KVRKELrrwlrrLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
241-516 |
4.92e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 241 SLWTSGFSALALkmgILYYggqLVAA-----GTVSTGDLVtfllyQI-----QFTDVLRVLLDYFPTLMKAVGSSEKIFE 310
Cdd:COG4178 269 TFFTTGYGQLAV---IFPI---LVAApryfaGEITLGGLM-----QAasafgQVQGALSWFVDNYQSLAEWRATVDRLAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 311 FLD-----REPQVAPSGTMAPTDlqGHLQLEDVWFSYPgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ 385
Cdd:COG4178 338 FEEaleaaDALPEAASRIETSED--GALALEDLTLRTP-DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWP 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 386 PTAGRLLLdghplPAYQHsylcrqVAVVPQEPLLFARSLHANISYGLGGCSW--AQVTAAARRVGAHDFITRLpqgyDTE 463
Cdd:COG4178 415 YGSGRIAR-----PAGAR------VLFLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERL----DEE 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 464 VgELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAA 516
Cdd:COG4178 480 A-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
316-556 |
5.21e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.15 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 316 PQVAPSGTMAPTdlqghLQLEDVWFSYPGrqEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG 395
Cdd:PRK11607 8 PQAKTRKALTPL-----LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 396 HPL---PAYQhsylcRQVAVVPQEPLLFAR-SLHANISYGLGGCSWAQVTAAAR------RVGAHDFITRLPQgydtevg 465
Cdd:PRK11607 81 VDLshvPPYQ-----RPINMMFQSYALFPHmTVEQNIAFGLKQDKLPKAEIASRvnemlgLVHMQEFAKRKPH------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 466 elggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEIL-AAKGSGRAVLMVT-GRAALAARAQRVVVLE 543
Cdd:PRK11607 149 ----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVdILERVGVTCVMVThDQEEAMTMAGRIAIMN 224
|
250
....*....|...
gi 2099372369 544 GGEVRQEGPPHEV 556
Cdd:PRK11607 225 RGKFVQIGEPEEI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-527 |
1.31e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLP------AYQHSylcrqVAVVPQEPLLFaRS 423
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALG-----IGMVHQHFMLV-PN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHA--NISYGLGGCSWAQV-TAAARRVgahdfITRLPQGY------DTEVgelgGQLSGGQRQAVAIARALLRDPRILIL 494
Cdd:COG3845 95 LTVaeNIVLGLEPTKGGRLdRKAARAR-----IRELSERYgldvdpDAKV----EDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 495 DEHTSALdteSQQQVEQ--EILAA-KGSGRAVLMVT 527
Cdd:COG3845 166 DEPTAVL---TPQEADElfEILRRlAAEGKSIIFIT 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-551 |
1.57e-23 |
|
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: 98.72 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpgrQEPVLKgVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYlcRQVAV 412
Cdd:cd03298 1 VRLDKIRFSY---GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFAR-SLHANISYG------LGGCSWAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARAL 485
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGlspglkLTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 486 LRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEG 551
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
333-526 |
1.76e-23 |
|
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: 99.14 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQ-HSYLCRQVA 411
Cdd:TIGR03410 1 LEVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEPLLFAR-SLHANISYGLggcswaqvtAAARRVGAH--DFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRD 488
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLLTGL---------AALPRRSRKipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEI--LAAKGsGRAVLMV 526
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIrrLRAEG-GMAILLV 188
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
23-308 |
2.87e-23 |
|
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: 100.25 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 23 AVMGLMAASALGeMAVPYYMGRASD------WVAREDELAAILpMVLLGLSsAVTELVCDVTFVGTLSRTQSRLQRRVFA 96
Cdd:cd18576 1 GLILLLLSSAIG-LVFPLLAGQLIDaalgggDTASLNQIALLL-LGLFLLQ-AVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 97 AVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVG 176
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 177 HFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDV---ALYTASLWTSGFSALALk 253
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRArirALFSSFIIFLLFGAIVA- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 254 mgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18576 237 --VLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
340-551 |
6.35e-23 |
|
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: 97.44 E-value: 6.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG-----HPLPAYqhsylcRQVAVVP 414
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEAR------RRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 415 QEPLLFAR-SLHANISY--GLGGCSWAQVTAA----ARRVGAHDFITRLpqgydtevgelGGQLSGGQRQAVAIARALLR 487
Cdd:cd03266 85 DSTGLYDRlTARENLEYfaGLYGLKGDELTARleelADRLGMEELLDRR-----------VGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEG 551
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCdRVVVLHRGRVVYEG 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
333-496 |
7.13e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.79 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKST----LVALVsrlhQPTAGRLLLDGH---PLPAYQH-- 403
Cdd:COG1137 4 LEAENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLV----KPDSGRIFLDGEditHLPMHKRar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 404 ---SYLcrqvavvPQEPLLFaRSLHA--NIsyglggcsWA-----QVTAAAR--RVGA--HDF-ITRLpqgYDTevgeLG 468
Cdd:COG1137 78 lgiGYL-------PQEASIF-RKLTVedNI--------LAvlelrKLSKKEReeRLEEllEEFgITHL---RKS----KA 134
|
170 180
....*....|....*....|....*...
gi 2099372369 469 GQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-509 |
1.00e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.27 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY---LCRQVAVVPQ----------- 415
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 ------EPLLFARSLhanisyglggcswaqvTAAARRVGAHDFITRL---PQGYDtevgELGGQLSGGQRQAVAIARALL 486
Cdd:PRK11308 111 vgqileEPLLINTSL----------------SAAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALM 170
|
170 180
....*....|....*....|...
gi 2099372369 487 RDPRILILDEHTSALDTESQQQV 509
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQV 193
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
286-583 |
1.27e-22 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 103.10 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 286 DVLRVLLDYFP----TLMKAVGSSEKIFEFLDRE---PQVAPSGTMAPTDLQGhLQLEDVWFSYPGRQEPVLKGVSLELR 358
Cdd:TIGR00957 584 NILRFPLNILPmvisSIVQASVSLKRLRIFLSHEelePDSIERRTIKPGEGNS-ITVHNATFTWARDLPPTLNGITFSIP 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 359 PGEVLALLGPPGAGKSTLV-ALVSRLHQptagrllLDGHplpayqhSYLCRQVAVVPQEPLLFARSLHANISYG--LGGC 435
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLsALLAEMDK-------VEGH-------VHMKGSVAYVPQQAWIQNDSLRENILFGkaLNEK 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 436 SWAQVTAAARRVGAHDFitrLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILA 515
Cdd:TIGR00957 729 YYQQVLEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 516 AKG--SGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL-RPGS---LLRDWG----QQGAPGEGDRGSGGEG 583
Cdd:TIGR00957 806 PEGvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLqRDGAfaeFLRTYApdeqQGHLEDSWTALVSGEG 883
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-527 |
1.29e-22 |
|
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: 95.19 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSypgrqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VA 411
Cdd:cd03215 5 LEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEP----LLFARSLHANISyglggcswaqvtaaarrvgahdfitrlpqgydtevgeLGGQLSGGQRQAVAIARALLR 487
Cdd:cd03215 79 YVPEDRkregLVLDLSVAENIA-------------------------------------LSSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLIS 161
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
348-562 |
2.21e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLL-------- 419
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfefdvrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 ---FARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRlpqGYDTevgelggqLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK09536 97 vveMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 497 HTSALDTESQQQVEQEILAAKGSGRAVL-MVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSL 562
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGKTAVaAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
320-509 |
2.30e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 100.91 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 320 PSGTMAPTDLQGH--LQLEDVWFSYPGRQ-------EPV--LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHqPTA 388
Cdd:COG4172 261 PRGDPRPVPPDAPplLEARDLKVWFPIKRglfrrtvGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 389 GRLLLDGHPLPAYQHSY---LCRQVAVVPQEPllFArSLhaN--------ISYGLG----GCS----WAQVTAAARRVG- 448
Cdd:COG4172 340 GEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--FG-SL--SprmtvgqiIAEGLRvhgpGLSaaerRARVAEALEEVGl 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 449 AHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG4172 415 DPAARHRYPH-----------EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQI 464
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
333-527 |
2.50e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH------PLPAYQHSYL 406
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 CRQVAVVPQEPLLFArslHANISYGL-------GGCSWAQVTAAAR----RVGAHDFITRLPQgydtevgelggQLSGGQ 475
Cdd:COG4161 81 RQKVGMVFQQYNLWP---HLTVMENLieapckvLGLSKEQAREKAMkllaRLRLTDKADRFPL-----------HLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 476 RQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVT 198
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
333-509 |
3.01e-22 |
|
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: 95.58 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPV--LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCR-- 408
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 --QVAVVPQEPLLFArSLHA--NISYG--LGGCSWAQVTAAA--RRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVA 480
Cdd:COG4181 89 arHVGFVFQSFQLLP-TLTAleNVMLPleLAGRRDARARARAllERVGLGHRLDHYP-----------AQLSGGEQQRVA 156
|
170 180
....*....|....*....|....*....
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQI 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-567 |
4.45e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC--RQV 410
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEP--LLFARSLHANISYGLGGCSWAQvTAAARRVgaHDFITRL-PQGYDTEVGELggqLSGGQRQAVAIARALLR 487
Cdd:PRK13638 80 ATVFQDPeqQIFYTDIDSDIAFSLRNLGVPE-AEITRRV--DEALTLVdAQHFRHQPIQC---LSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDW 566
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISShDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
.
gi 2099372369 567 G 567
Cdd:PRK13638 234 G 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
333-567 |
5.61e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VA 411
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEP--LLFARSLHANISYGLGGCSW------AQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIAR 483
Cdd:PRK13644 81 IVFQNPetQFVGRTVEEDLAFGPENLCLppieirKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSlL 563
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS-L 228
|
....
gi 2099372369 564 RDWG 567
Cdd:PRK13644 229 QTLG 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
61-564 |
6.81e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 61 MVLLGLSSAVtelVCDVTFVGTLSRTQSRLQRRVFAAVLRQSIT---ELRAD-GAGDVAMRVTRDAeDVREALGEALSLL 136
Cdd:PLN03232 346 LIFFGVTFGV---LCESQYFQNVGRVGFRLRSTLVAAIFHKSLRlthEARKNfASGKVTNMITTDA-NALQQIAEQLHGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 137 lWylARGLCLFATMAWLSPRMALLT----ALALPLLLALPRAVGHFRQALAPQMQKAQARASeVAVETFQAMATVRSFAN 212
Cdd:PLN03232 422 -W--SAPFRIIVSMVLLYQQLGVASlfgsLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVG-IINEILASMDTVKCYAW 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 213 EDGaaahYRQRLQQshrLEKKDVALYTASLWTSGFSALALK-----MGILYYGGQLVAAGTVSTGDLVTFL-LYQiqftd 286
Cdd:PLN03232 498 EKS----FESRIQG---IRNEELSWFRKAQLLSAFNSFILNsipvvVTLVSFGVFVLLGGDLTPARAFTSLsLFA----- 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 287 VLRVLLDYFPTLMKAVG----SSEKIFE-FLDREPQVAPSGTMAPTdlQGHLQLEDVWFSYPGRQE-PVLKGVSLELRPG 360
Cdd:PLN03232 566 VLRSPLNMLPNLLSQVVnanvSLQRIEElLLSEERILAQNPPLQPG--APAISIKNGYFSWDSKTSkPTLSDINLEIPVG 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 361 EVLALLGPPGAGKSTLV-ALVSRLHQPTAGRLLLDGhplpayqhsylcrQVAVVPQEPLLFARSLHANISYGLGGCS--- 436
Cdd:PLN03232 644 SLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFESery 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 437 WAQVTAAARRvgaHDFitRLPQGYD-TEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILA 515
Cdd:PLN03232 711 WRAIDVTALQ---HDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK 785
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2099372369 516 AKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:PLN03232 786 DELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
333-517 |
7.15e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.23 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ-----PTAGRLLLDGHPL--PAYQHSY 405
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQEPLLFARSLHANISYGL--GGCSWAQVTAAARR---VGA---HDFITRLpqgYDTEVGelggqLSGGQRQ 477
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGLrlKGIKDKQVLDEAVEkslKGAsiwDEVKDRL---HDSALG-----LSGGQQQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAK 517
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
334-567 |
8.66e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:PRK10575 13 ALRNVSFRVPGRT--LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEpLLFARSLHANISYGLGGCSW------------AQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAI 481
Cdd:PRK10575 91 PQQ-LPAAEGMTVRELVAIGRYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALDTesQQQVEQEILAAKGSGRAVLMVTGRAALAARAQR----VVVLEGGEVRQEGPPHEVL 557
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDI--AHQVDVLALVHRLSQERGLTVIAVLHDINMAARycdyLVALRGGEMIAQGTPAELM 236
|
250
....*....|
gi 2099372369 558 RPGSLLRDWG 567
Cdd:PRK10575 237 RGETLEQIYG 246
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
333-567 |
9.06e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 9.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVA 411
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEP--LLFARSLHANISYGL--GGCSWAQ----VTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIAR 483
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLenKGIPHEEmkerVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS-GRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSL 562
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
....*
gi 2099372369 563 LRDWG 567
Cdd:PRK13650 234 LLQLG 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
334-562 |
1.54e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVV 413
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEPLL-----------FARSLHaniSYG-LGGCSWAQVTAAARRVG----AHDFITrlpqgydtevgelggQLSGGQRQ 477
Cdd:COG4604 81 RQENHInsrltvrelvaFGRFPY---SKGrLTAEDREIIDEAIAYLDledlADRYLD---------------ELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQeIL--AAKGSGRAVLMV------------TgraalaaraqrVVVLE 543
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMK-LLrrLADELGKTVVIVlhdinfascyadH-----------IVAMK 210
|
250
....*....|....*....
gi 2099372369 544 GGEVRQEGPPHEVLRPGSL 562
Cdd:COG4604 211 DGRVVAQGTPEEIITPEVL 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-524 |
1.72e-21 |
|
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: 93.38 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH---PLPAYQH-----S 404
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditKLPMHKRarlgiG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 405 YLcrqvavvPQEPLLFaRSLHA--NISYGLGGcswAQVTAAARRVGA----HDF-ITRLPQgydtevgELGGQLSGGQRQ 477
Cdd:cd03218 79 YL-------PQEASIF-RKLTVeeNILAVLEI---RGLSKKEREEKLeellEEFhITHLRK-------SKASSLSGGERR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVL 524
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVL 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
349-557 |
2.42e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPayQHSYLCRQ-VAVVPQ----EP------ 417
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRARHARQrVGVVPQfdnlDPdftvre 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 --LLFARSLhanisyglgGCSWAQvtAAARRVGAHDFiTRLPQGYDTEVGElggqLSGGQRQAVAIARALLRDPRILILD 495
Cdd:PRK13537 100 nlLVFGRYF---------GLSAAA--ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARA-QRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-527 |
2.64e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 2.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA--YQH-SYLcrq 409
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedRRRiGYL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 vavvPQEPLL------------FARsLHanisyGLGGcswaqvtAAARRVgAHDFITRLpqgydtEVGELGG----QLSG 473
Cdd:COG4152 77 ----PEERGLypkmkvgeqlvyLAR-LK-----GLSK-------AEAKRR-ADEWLERL------GLGDRANkkveELSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 474 GQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSS 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
315-564 |
4.44e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 315 EPqVAPSGTmAPTDLQ-GHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLL 393
Cdd:PTZ00243 1292 EP-ASPTSA-APHPVQaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 394 DGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANISYGLGGCSwAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSG 473
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS-AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 474 GQRQAVAIARALL-RDPRILILDEHTSALDTESQQQVEQEILAAKgSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGP 552
Cdd:PTZ00243 1449 GQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAF-SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
250
....*....|...
gi 2099372369 553 PHE-VLRPGSLLR 564
Cdd:PTZ00243 1528 PRElVMNRQSIFH 1540
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
350-555 |
6.56e-21 |
|
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: 91.66 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGhplpayqHSYLC------RQVAVVPQEPL----L 419
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-------HDVVReprevrRRIGIVFQDLSvddeL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 FARS---LHANIsYGLGGCSWAQVTAAA-RRVGAHDFITRLPQGYdtevgelggqlSGGQRQAVAIARALLRDPRILILD 495
Cdd:cd03265 89 TGWEnlyIHARL-YGVPGAERRERIDELlDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGS-GRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEGPPHE 555
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCdRVAIIDHGRIIAEGTPEE 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
346-527 |
7.50e-21 |
|
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: 90.69 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQP-TAGRLLLDGHPLpaYQHSYLCRqVAVVPQEPLLFAR- 422
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnALAGRRTGLgVSGEVLINGRPL--DKRSFRKI-IGYVPQDDILHPTl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYglggcswaqvtAAARRvgahdfitrlpqgydtevgelggQLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:cd03213 98 TVRETLMF-----------AAKLR-----------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*
gi 2099372369 503 TESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSI 168
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
347-527 |
7.53e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 347 EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH----PLPAYQHSYLCRQVAVVP----QEPL 418
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYLGHRNAMKPaltvAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LFARSLHANISYGlggcswaqVTAAARRVGAHDfITRLPQGYdtevgelggqLSGGQRQAVAIARALLRDPRILILDEHT 498
Cdd:PRK13539 95 EFWAAFLGGEELD--------IAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*....
gi 2099372369 499 SALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAAT 184
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
344-527 |
1.25e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.70 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 344 GRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHS---YLCRQVAVVPQE-PLL 419
Cdd:PRK10908 14 GRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDhHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 FARSLHANISYGL--GGCSWA----QVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILI 493
Cdd:PRK10908 92 MDRTVYDNVAIPLiiAGASGDdirrRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 2099372369 494 LDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAT 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-524 |
1.26e-20 |
|
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: 90.35 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGhplPAYQHSYLC-RQVA 411
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEAlRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEPLLF-ARSLHANISYG--LGGCSWAQVTAAARRVGAHDfitrlpqgydtEVGELGGQLSGGQRQAVAIARALLRD 488
Cdd:cd03268 76 ALIEAPGFYpNLTARENLRLLarLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEILAAKGSGRAVL 524
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVL 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
349-527 |
1.33e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 91.35 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLL------DGHPLPAYQH--SYLCRQVAVVPQEPLLF 420
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 421 A-RSLHANISYG---LGGCSWAQVTAAAR----RVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRIL 492
Cdd:PRK11264 98 PhRTVLENIIEGpviVKGEPKEEATARARellaKVGLAGKETSYPR-----------RLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVT 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
344-526 |
1.96e-20 |
|
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: 90.19 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 344 GRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLldghplpaYQHSYlcRQVAVVPQEPllfaRS 423
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDG--GWVDLAQASP----RE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHANISYGLGGCSwaQVTAAARRVGAHDFITR--LPQGYDTEV-----GELGGQL--------------SGGQRQAVAIA 482
Cdd:COG4778 87 ILALRRRTIGYVS--QFLRVIPRVSALDVVAEplLERGVDREEararaRELLARLnlperlwdlppatfSGGEQQRVNIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMV 526
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-527 |
2.16e-20 |
|
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: 90.22 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSylcRQVaVVPQEPLLFARSLHANIS 429
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD---RMV-VFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 430 YGLgGCSWAQVTAAARR--VGAHDFITRLPQGYDTEVgelgGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQ 507
Cdd:TIGR01184 77 LAV-DRVLPDLSKSERRaiVEEHIALVGLTEAADKRP----GQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|.
gi 2099372369 508 QVEQEILA-AKGSGRAVLMVT 527
Cdd:TIGR01184 152 NLQEELMQiWEEHRVTVLMVT 172
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-527 |
3.16e-20 |
|
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: 87.12 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYqhsylcrqvav 412
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 vpqepllFArslhanisyglggcswaqvtaaarrvgahdfitrlpqgydtevgelggQLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03221 68 -------FE------------------------------------------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVS 124
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-527 |
3.25e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 335 LEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHplpayqhsylCRqVAVVP 414
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LR-IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 415 QEPLLFA-RSLHANISYGLGG------------CSWAQVTAAARRVG-AHDFITRLpQGYDTE------VGELG------ 468
Cdd:COG0488 68 QEPPLDDdLTVLDTVLDGDAElraleaeleeleAKLAEPDEDLERLAeLQEEFEAL-GGWEAEaraeeiLSGLGfpeedl 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 469 ----GQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG---TVLVVS 206
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
329-557 |
4.93e-20 |
|
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: 89.97 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 329 LQGHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCR 408
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHANISYGLGgCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRD 488
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 489 PRILILDEHTSALDTESqQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:cd03288 175 SSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
333-527 |
5.47e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH------PLPAYQHSYL 406
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 407 CRQVAVVPQEPLLFArslHANISYGL-------GGCSWAQVTAAAR----RVGAHDFITRLPQgydtevgelggQLSGGQ 475
Cdd:PRK11124 81 RRNVGMVFQQYNLWP---HLTVQQNLieapcrvLGLSKDQALARAEklleRLRLKPYADRFPL-----------HLSGGQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 476 RQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVT 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
349-562 |
6.31e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.32 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPayQHSYLCRQVAVVPQEPLLFAR-SLHAN 427
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 428 ISYGLggcSWAQVTAAARRvgahdfiTRLPQGYdtEVGELGG-------QLSGGQRQAVAIARALLRDPRILILDEHTSA 500
Cdd:PRK11432 99 VGYGL---KMLGVPKEERK-------QRVKEAL--ELVDLAGfedryvdQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 501 LDT-----------ESQQQVeqeilaakgsGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEV-LRPGSL 562
Cdd:PRK11432 167 LDAnlrrsmrekirELQQQF----------NITSLYVThDQSEAFAVSDTVIVMNKGKIMQIGSPQELyRQPASR 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-557 |
8.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ--PTA---GRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFAR- 422
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGLGGCSWAQVTAA-ARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSAL 501
Cdd:PRK14247 98 SIFENVALGLKLNRLVKSKKElQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 502 DTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK14247 178 DPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
330-502 |
9.10e-20 |
|
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: 88.48 E-value: 9.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 330 QGHLQLEDV--WFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRL---HQPTAGRLLLDGHPLPAYQHS 404
Cdd:cd03234 1 QRVLPWWDVglKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 405 YlcrQVAVVPQE----PLLFAR-SLHANISYGLGGCSwaqvTAAARRVGAHDFitRLPQGYDTEVG-ELGGQLSGGQRQA 478
Cdd:cd03234 81 K---CVAYVRQDdillPGLTVReTLTYTAILRLPRKS----SDAIRKKRVEDV--LLRDLALTRIGgNLVKGISGGERRR 151
|
170 180
....*....|....*....|....
gi 2099372369 479 VAIARALLRDPRILILDEHTSALD 502
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-496 |
9.38e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 92.94 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 9 RLLLSLSPERRRCAAVMGLmaASALGEMAVPYYMGRAsdwVAREDELAAILPMVLLGLSSA--VTELVCDVTFVGTLSRT 86
Cdd:COG4615 5 RLLLRESRWLLLLALLLGL--LSGLANAGLIALINQA---LNATGAALARLLLLFAGLLVLllLSRLASQLLLTRLGQHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 87 QSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALgEALSLLLWYLARGLCLFATMAWLSPRM-----ALLT 161
Cdd:COG4615 80 VARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLflltlVLLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 162 ALALPLLLALPRAVGHFRQAlapqmqkaqaRASEVAV-ETFQAMatVRSFA----NEDGAAAHYRQRLQQS---HRLEKK 233
Cdd:COG4615 159 LGVAGYRLLVRRARRHLRRA----------REAEDRLfKHFRAL--LEGFKelklNRRRRRAFFDEDLQPTaerYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 234 DVALYTASLWTSGFSALALKMGILYYGgqLVAAGTVSTGDLVTF---LLYQIQftdVLRVLLDYFPTLMKAVGSSEKIFE 310
Cdd:COG4615 227 RADTIFALANNWGNLLFFALIGLILFL--LPALGWADPAVLSGFvlvLLFLRG---PLSQLVGALPTLSRANVALRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 311 FLDREPQVAPSGTMAPTDLQ----GHLQLEDVWFSYPGRQEP---VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRL 383
Cdd:COG4615 302 LELALAAAEPAAADAAAPPApadfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 384 HQPTAGRLLLDGHPLPAYQ-HSYlcRQ-VAVVPQEPLLFARsLhanisYGLGGcswaqVTAAARrvgAHDFITRLpqGYD 461
Cdd:COG4615 382 YRPESGEILLDGQPVTADNrEAY--RQlFSAVFSDFHLFDR-L-----LGLDG-----EADPAR---ARELLERL--ELD 443
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2099372369 462 TEVGELGG-----QLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:COG4615 444 HKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-562 |
1.06e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.67 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL----PAYqhsylcR 408
Cdd:PRK11650 4 LKLQAVRKSYDGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelePAD------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFAR-SLHANISYGLG--GCSWAQ----VTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAI 481
Cdd:PRK11650 77 DIAMVFQNYALYPHmSVRENMAYGLKirGMPKAEieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALDT--------ESQQ---------------QVEQEILAAKgsgravlmvtgraalaaraqr 538
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvqmrlEIQRlhrrlkttslyvthdQVEAMTLADR--------------------- 204
|
250 260
....*....|....*....|....*
gi 2099372369 539 VVVLEGGEVRQEGPPHEVL-RPGSL 562
Cdd:PRK11650 205 VVVMNGGVAEQIGTPVEVYeKPAST 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
324-509 |
1.89e-19 |
|
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: 91.67 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 324 MAPTDLqghLQLED--VWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKS-TLVALVSRLHQPTA---GRLLLDGHP 397
Cdd:COG4172 1 MMSMPL---LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 398 LPAYQHSYLCR----QVAVVPQEPL-----LF--------ARSLHANISyglGGCSWAQVTAAARRVGAHDFITRL---P 457
Cdd:COG4172 78 LLGLSERELRRirgnRIAMIFQEPMtslnpLHtigkqiaeVLRLHRGLS---GAAARARALELLERVGIPDPERRLdayP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 458 QgydtevgelggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG4172 155 H-----------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQI 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-558 |
2.58e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 344 GRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpayqhSYLC---RQVAVVPQEPLLF 420
Cdd:PRK10851 13 GRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHardRKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 421 AR-SLHANISYGLggcswaQVTAAARRVGAHDFITRLPQGYD-TEVGELGG----QLSGGQRQAVAIARALLRDPRILIL 494
Cdd:PRK10851 87 RHmTVFDNIAFGL------TVLPRRERPNAAAIKAKVTQLLEmVQLAHLADrypaQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 495 DEHTSALDTesqqQVEQEI------LAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:PRK10851 161 DEPFGALDA----QVRKELrrwlrqLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-567 |
2.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.32 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTA---GRLLLDGHPLPAYQHSYLCRQ 409
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEP--LLFARSLHANISYGLG--GCSWAQVTAAARR----VGAHDFITRLPQgydtevgelggQLSGGQRQAVAI 481
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGLEnrAVPRPEMIKIVRDvladVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPG 560
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
....*..
gi 2099372369 561 SLLRDWG 567
Cdd:PRK13640 235 EMLKEIG 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-557 |
4.07e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 319 APSGTMAPTdlqgHLQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL 398
Cdd:PRK13536 32 SIPGSMSTV----AIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 399 PAYQHSYLCRqVAVVPQ-EPLLFARSLHAN-ISYG-LGGCSWAQVTAAARRVgaHDFiTRLPQGYDTEVGELggqlSGGQ 475
Cdd:PRK13536 106 PARARLARAR-IGVVPQfDNLDLEFTVRENlLVFGrYFGMSTREIEAVIPSL--LEF-ARLESKADARVSDL----SGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 476 RQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARA-QRVVVLEGGEVRQEGPPH 554
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPH 257
|
...
gi 2099372369 555 EVL 557
Cdd:PRK13536 258 ALI 260
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
312-509 |
4.47e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 312 LDREPQVAPsgTMAPTDLQGHLQLEDVWFSYPGRQ---------EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSR 382
Cdd:PRK15134 257 LNSEPSGDP--VPLPEPASPLLDVEQLQVAFPIRKgilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 383 LhQPTAGRLLLDGHPLPAYQHSYLC---RQVAVVPQEP--LLFAR-SLHANISYGL--------GGCSWAQVTAAARRVG 448
Cdd:PRK15134 335 L-INSQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDPnsSLNPRlNVLQIIEEGLrvhqptlsAAQREQQVIAVMEEVG 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 449 AhDFITRlpQGYDTEvgelggqLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:PRK15134 414 L-DPETR--HRYPAE-------FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
333-527 |
6.27e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.27 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLvALV---SRLHQPTAGRLLLDGHPL----P------ 399
Cdd:COG0396 1 LEIKNLHVSVEGK--EILKGVNLTIKPGEVHAIMGPNGSGKSTL-AKVlmgHPKYEVTSGSILLDGEDIlelsPderara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 400 ----AYQH---------SYLCRQVAVVPQEPLLFARSLHAnisyglggcswaQVTAAARRVG-AHDFITRlpqgydtevg 465
Cdd:COG0396 78 giflAFQYpveipgvsvSNFLRTALNARRGEELSAREFLK------------LLKEKMKELGlDEDFLDR---------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 466 ELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG0396 136 YVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIIT 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-557 |
6.36e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.32 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYL----CRQVAVVPQE-PLLFARSL 424
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 425 HANISYGLggcSWAQVTAAARRVGAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTE 504
Cdd:PRK10070 124 LDNTAFGM---ELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 505 SQQQVEQEI--LAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK10070 199 IRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
333-526 |
9.49e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSyPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAyqHSYLCRQ--- 409
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG--LSPRERRrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFARSLHANIS------------YGLGG-CSWAQVTAAARRVgahdfITRL---PQGYDTEVgelgGQLSG 473
Cdd:COG3845 335 VAYIPEDRLGRGLVPDMSVAenlilgryrrppFSRGGfLDRKAIRAFAEEL-----IEEFdvrTPGPDTPA----RSLSG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 474 GQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMV 526
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
333-564 |
9.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYL-CRQ-V 410
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMkLREsV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEP--LLFARSLHANISYGLG--GCSWAQVTAAARRVGAHDFITRLPQgydtevgELGGQLSGGQRQAVAIARALL 486
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAVnlKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEmQKELGLTIIIAThDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
349-558 |
9.88e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 9.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGhplpayqhsylcrQVAvvpqePLL-FARSLHAN 427
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVS-----ALLeLGAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 428 IS-----------YGLggcSWAQVTAAARRV----GAHDFItrlpqgyDTEVgelgGQLSGGQ--RQAVAIARALlrDPR 490
Cdd:COG1134 103 LTgreniylngrlLGL---SRKEIDEKFDEIvefaELGDFI-------DQPV----KTYSSGMraRLAFAVATAV--DPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 491 ILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVShSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-527 |
1.18e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 335 LEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDghplPAYQHSYLCRQVAVVP 414
Cdd:PRK09544 7 LENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 415 QEPLLFARSLHANisyglGGCSWAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILIL 494
Cdd:PRK09544 81 TLPLTVNRFLRLR-----PGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 495 DEHTSALDTESQ-------QQVEQEIlaakgsGRAVLMVT 527
Cdd:PRK09544 145 DEPTQGVDVNGQvalydliDQLRREL------DCAVLMVS 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-527 |
1.19e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 341 SYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpAYQHSY--LCRQVAVVPQE-- 416
Cdd:PRK11288 13 TFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 --PLLfarSLHANISYG-----LGgcsWAQVTAAARRVGAHdfITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDP 489
Cdd:PRK11288 90 lvPEM---TVAENLYLGqlphkGG---IVNRRLLNYEAREQ--LEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVS 197
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
22-308 |
1.27e-18 |
|
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: 86.33 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWV-AREDELAAILPMVLLGLSSAVtelvcdVTFVGT--LSRTQSR----LQRRV 94
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALsAGGSSGGLLALLVALFLLQAV------LSALSSylLGRTGERvvldLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 95 FAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRA 174
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 175 VGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKdVALYTASLWT-SGFSALALK 253
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLK-AAKIEALIGPlMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 254 MGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18551 235 LVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-527 |
2.05e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLP------AYQHSylcrqVAVVP----QEP 417
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFARSLHANISYG-LGGCSWAQV--TAAARRVgAHDFITRL---PQGYDTEVgelgGQLSGGQRQAVAIARALLRDPRI 491
Cdd:COG1129 341 LVLDLSIRENITLAsLDRLSRGGLldRRRERAL-AEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 492 LILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS 451
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-555 |
3.03e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEP--VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGhplpayqhsylcRQV 410
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG------------QDV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEPLLFARSLHANISYG----LGGCSWAQ----------VTAAARRVGAHDFITRLpqGYDTEVGELGGQLSGGQR 476
Cdd:PRK10535 73 ATLDADALAQLRREHFGFIFQryhlLSHLTAAQnvevpavyagLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHE 555
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
336-567 |
3.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.14 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 336 EDVWFSY----PGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVA 411
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 -VVPQEP--LLFARSLHANISYG---LGGCS---WAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:PRK13633 88 gMVFQNPdnQIVATIVEEDVAFGpenLGIPPeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGS 561
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
....*.
gi 2099372369 562 LLRDWG 567
Cdd:PRK13633 237 MMKKIG 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-567 |
3.15e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPL-LFARSLHA-NISYGLGGCS------WAQVTAAARRVGAHDFITRLPQGydtevgelggqLSGGQRQAVAIARA 484
Cdd:PRK13648 88 VFQNPDnQFVGSIVKyDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGR-AVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLL 563
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
....
gi 2099372369 564 RDWG 567
Cdd:PRK13648 237 TRIG 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
350-526 |
3.31e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.18 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQPT--AGRLLLDGHPLPAYQHSYLCRQVavvpQEPLLFARSL-- 424
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMnALAFRSPKGVkgSGSVLLNGMPIDAKEMRAISAYV----QQDDLFIPTLtv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 425 --HANIS--YGLGgcswAQVTAAARRVGAHDFITR--LPQGYDTEVGELGGQ--LSGGQRQAVAIARALLRDPRILILDE 496
Cdd:TIGR00955 117 reHLMFQahLRMP----RRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190
....*....|....*....|....*....|
gi 2099372369 497 HTSALDTESQQQVEQEILAAKGSGRAVLMV 526
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
347-527 |
6.68e-18 |
|
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: 82.16 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 347 EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpAYQHSYLCRQVAVVPQEPLLFAR-SLH 425
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYGLGGCSWAQVTAAARRVGAHDFITRlpqgydtevgeLGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGFEDR-----------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|..
gi 2099372369 506 QQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTT 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-557 |
6.86e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVA 411
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEP--LLFARSLHANISYGLGGCS------WAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIAR 483
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGipreemIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGR-AVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
287-564 |
7.24e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.87 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 287 VLRVLLDYFPTLMKAV---GSSEKIFE--FLDREPQVAPSGTMAPTdlQGHLQLEDVWFSYPGRQE-PVLKGVSLELRPG 360
Cdd:PLN03130 566 VLRFPLFMLPNLITQAvnaNVSLKRLEelLLAEERVLLPNPPLEPG--LPAISIKNGYFSWDSKAErPTLSNINLDVPVG 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 361 EVLALLGPPGAGKSTLV-ALVSRLHQPTAGRLLLDGhplpayqhsylcrQVAVVPQEPLLFARSLHANISYGLGGCS--- 436
Cdd:PLN03130 644 SLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATVRDNILFGSPFDPery 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 437 WAQVTAAARRvgaHDfITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAA 516
Cdd:PLN03130 711 ERAIDVTALQ---HD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKD 786
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2099372369 517 KGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:PLN03130 787 ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQ 834
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
346-557 |
1.21e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.09 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLH 425
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYGLggcsWAQVTA----------------AARRVGAHDFITRLpqGYDTEV-GELGGQLSGGQRQAVAIARALLRD 488
Cdd:PRK10619 97 VFQHFNL----WSHMTVlenvmeapiqvlglskQEARERAVKYLAKV--GIDERAqGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-513 |
2.27e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQpTAGRLLLDGHPLPAYQHSY--------LCRQVA 411
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYerrvnlnrLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVPQEPLLFARSLHANISYGLGGCSWAQ-------VTAAARRVGAHDFITRlpqgydtEVGELGGQLSGGQRQAVAIARA 484
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVAYGVKIVGWRPkleiddiVESALKDADLWDEIKH-------KIHKSALDLSGGQQQRLCIARA 164
|
170 180
....*....|....*....|....*....
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLI 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
345-509 |
2.42e-17 |
|
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: 81.61 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 345 RQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHpLPAYQHSYLCRQVAVVPQE-------- 416
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFGQktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 PLLFARSLHANIsYGLggcSWAQVTAAARRVGAHDFITRLpqgYDTEVgelgGQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:cd03267 111 PVIDSFYLLAAI-YDL---PPARFKKRLDELSELLDLEEL---LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170
....*....|...
gi 2099372369 497 HTSALDTESQQQV 509
Cdd:cd03267 180 PTIGLDVVAQENI 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-527 |
2.61e-17 |
|
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: 79.51 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLlldghplpayqHSYLCRQVAV 412
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLFARSLHANISYglggcSWAQVtaaarrvgahdfitrlpqgydtevgelggqLSGGQRQAVAIARALLRDPRIL 492
Cdd:cd03223 69 LPQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 493 ILDEHTSALDTESQQQVEQeilAAKGSGRAVLMVT 527
Cdd:cd03223 114 FLDEATSALDEESEDRLYQ---LLKELGITVISVG 145
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
89-318 |
2.84e-17 |
|
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: 82.88 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 89 RLQRRVFAAVLRQSIT--ELRADGAGDVAMRVTRDAEDVREALGEALSLLL-----------------WYLArgLCLFAT 149
Cdd:cd18578 86 RLRKLAFRAILRQDIAwfDDPENSTGALTSRLSTDASDVRGLVGDRLGLILqaivtlvagliiafvygWKLA--LVGLAT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 150 MawlsPRMAlltalalplllalprAVGHFRQAL----APQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQ 225
Cdd:cd18578 164 V----PLLL---------------LAGYLRMRLlsgfEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 226 QSHRLEKKdvalytASLWTS---GFS------ALALkmgILYYGGQLVAAGTVStgdlvtfllyqiqFTDVLRVL----- 291
Cdd:cd18578 225 EPLKKGLR------RALISGlgfGLSqsltffAYAL---AFWYGGRLVANGEYT-------------FEQFFIVFmalif 282
|
250 260 270
....*....|....*....|....*....|....*
gi 2099372369 292 --------LDYFPTLMKAVGSSEKIFEFLDREPQV 318
Cdd:cd18578 283 gaqsagqaFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
333-562 |
3.21e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVwfSYPGRqepvLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHqPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:COG4138 1 LQLNDV--AVAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQE-PLLFARSLHANISYGL-GGCSWAQVTAA----ARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALL 486
Cdd:COG4138 74 LSQQqSPPFAMPVFQYLALHQpAGASSEAVEQLlaqlAEALGLEDKLSRPLT-----------QLSGGEWQRVRLAAVLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 487 R-------DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:COG4138 143 QvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSShDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
....
gi 2099372369 559 PGSL 562
Cdd:COG4138 223 PENL 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
333-527 |
3.75e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQH--------S 404
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaaqlgiG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 405 YLCRQVAVVP----QEPLLFARSLHANIsYGLGGCSWAQVtaaarRVGAHDFITRLpqGYDTEVGELGGQLSGGQRQAVA 480
Cdd:PRK09700 84 IIYQELSVIDeltvLENLYIGRHLTKKV-CGVNIIDWREM-----RVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIS 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
333-559 |
3.84e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEP--LLFARSLHANISYG-----LGGCSW-AQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARA 484
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVeRRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVeQEILAA-KGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRP 559
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETL-MEILDRlHNQGKTVIVAThDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
351-555 |
3.86e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 351 KGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL----PAYqhsylcRQVAVVPQEPLLFAR-SLH 425
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMndvpPAE------RGVGMVFQSYALYPHlSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYG--LGGCSWAQ----VTAAARRVGAHDFITRLPQGydtevgelggqLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:PRK11000 94 ENMSFGlkLAGAKKEEinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 500 ALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHE 555
Cdd:PRK11000 163 NLDAALRVQMRIEISRlHKRLGRTMIYVThDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
350-567 |
5.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQ--HSYLCRQVAVVPQEP--LLFARSLH 425
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvkLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYGLG--GCSWAQVTaaaRRVGAHDFITRLPqgYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDT 503
Cdd:PRK13637 103 KDIAFGPInlGLSEEEIE---NRVKRAMNIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 504 ESQQQVEQEI--LAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDWG 567
Cdd:PRK13637 178 KGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIG 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
352-513 |
6.97e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 352 GVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPA-----------YQHSYLCRQVAVVpqEP 417
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGhqiarmgvvrtFQHVRLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFA--RSLHANISYGL---GGCSWAQVTAAAR------RVGAHDFITRlpqgydtevgeLGGQLSGGQRQAVAIARALL 486
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLlktPAFRRAESEALDRaatwleRVGLLEHANR-----------QAGNLAYGQQRRLEIARCMV 169
|
170 180
....*....|....*....|....*..
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELI 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-557 |
9.61e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.48 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY------LCRQVAVVPQEPLLFAR 422
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaikLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 -SLHANISYGLGGCSWAQ-------VTAAARRVGAHDFItrlpqgYDtEVGELGGQLSGGQRQAVAIARALLRDPRILIL 494
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEV------YD-RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 495 DEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
333-525 |
1.02e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP---LPAyqHSYLCRQ 409
Cdd:PRK10895 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDislLPL--HARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANISYGLGgcSWAQVTAAARRVGAHDFITRLPQGYDTEvgELGGQLSGGQRQAVAIARALLRD 488
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAAN 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLM 525
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI 192
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-527 |
1.02e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.11 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 323 TMAPTDL-QGH-LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA 400
Cdd:PRK11247 1 MMNTARLnQGTpLLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 401 YQH-SYLCRQVAvvpqePLLFARSLHANISYGLGGCSWAQVTAAARRVGAHDfitrlpqgydtEVGELGGQLSGGQRQAV 479
Cdd:PRK11247 79 AREdTRLMFQDA-----RLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 480 AIARALLRDPRILILDEHTSALDT----ESQQQVE---QEilaakgSGRAVLMVT 527
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDAltriEMQDLIEslwQQ------HGFTVLLVT 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
333-558 |
1.70e-16 |
|
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: 78.34 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLH--QPTAGRLLLDGHPLpayqhsylcrqV 410
Cdd:cd03217 1 LEIKDLHVSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI-----------T 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQEpllfaRSLhanisygLG-GCSWaQVTAAARRVGAHDFITRLPQGydtevgelggqLSGGQRQAVAIARALLRDP 489
Cdd:cd03217 68 DLPPEE-----RAR-------LGiFLAF-QYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT--GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIIThyQRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-527 |
2.09e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLdGHPLpayqhsylcrQVAV 412
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEPLLF--ARSLHANISYGLGGcswAQVTAAARRVGAHDFitrlpQGYD--TEVGElggqLSGGQRQAVAIARALLRD 488
Cdd:COG0488 383 FDQHQEELdpDKTVLDELRDGAPG---GTEQEVRGYLGRFLF-----SGDDafKPVGV----LSGGEKARLALAKLLLSP 450
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 489 PRILILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDFPG---TVLLVS 486
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
349-509 |
2.77e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.96 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY---QHSYLCRQVAVVPQEPLLFA---R 422
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSISAVnprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPqgyDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:PRK10419 107 TVREIIREPLRHLLSLDKAERLARASEMLRAVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
....*..
gi 2099372369 503 TESQQQV 509
Cdd:PRK10419 184 LVLQAGV 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
350-514 |
2.96e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRL--HQPTAGRLLLDGHPLPA--------------YQhsylcrQVAVV 413
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQAsnirdteragiaiiHQ------ELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 414 PQEPLLFARSLHANISYGlGGCSWAQVTAAARRVGAHdfiTRLPQGYDTEVGELGGqlsgGQRQAVAIARALLRDPRILI 493
Cdd:PRK13549 95 KELSVLENIFLGNEITPG-GIMDYDAMYLRAQKLLAQ---LKLDINPATPVGNLGL----GQQQLVEIAKALNKQARLLI 166
|
170 180
....*....|....*....|.
gi 2099372369 494 LDEHTSALdTESQQQVEQEIL 514
Cdd:PRK13549 167 LDEPTASL-TESETAVLLDII 186
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
349-551 |
3.98e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.57 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDG--HPLPAYQHSYlcrqvavvpqEPLLFARSlha 426
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGGF----------NPELTGRE--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGLG--GCSWAQVTAAARRVgaHDFiTRLPQGYDTEVGElggqLSGGQ--RQAVAIARALlrDPRILILDEHTSALD 502
Cdd:cd03220 104 NIYLNGRllGLSRKEIDEKIDEI--IEF-SELGDFIDLPVKT----YSSGMkaRLAFAIATAL--EPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2099372369 503 TESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEG 551
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVShDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-557 |
4.00e-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: 78.69 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY---QHSYLCRQVAVVPQ--------- 415
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQdspsavnpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 --------EPLLFARSLHANISYglggcswAQVTAAARRVGAHDFIT-RLPQgydtevgelggQLSGGQRQAVAIARALL 486
Cdd:TIGR02769 105 mtvrqiigEPLRHLTSLDESEQK-------ARIAELLDMVGLRSEDAdKLPR-----------QLSGGQLQRINIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEILAAKG-SGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRKLQQaFGTAYLFIThDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
298-564 |
4.00e-16 |
|
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: 82.27 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 298 LMKAVgssEKIFEFLDREPQVA-PSGTMAPTDL-----------------QGHLQLEDVWFSYPGRQEPVLKGVSLELRP 359
Cdd:TIGR01271 1168 LMRSV---SRVFKFIDLPQEEPrPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKYTEAGRAVLQDLSFSVEG 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 360 GEVLALLGPPGAGKSTLVALVSRLHQpTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSLHANIS-YGlggcSWA 438
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYE----QWS 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 439 --QVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESqQQVEQEILAA 516
Cdd:TIGR01271 1320 deEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT-LQIIRKTLKQ 1398
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2099372369 517 KGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:TIGR01271 1399 SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFK 1446
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
352-527 |
7.91e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 352 GVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL----PAYQHS--YLCRQVAV----VPQEPLLFA 421
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrDEYHQDllYLGHQPGIktelTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 422 RSLHANISYglggcswAQVTAAARRVGAHDFiTRLPqgydtevgelGGQLSGGQRQAVAIARALLRDPRILILDEHTSAL 501
Cdd:PRK13538 99 QRLHGPGDD-------EALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*.
gi 2099372369 502 DTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVILTT 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
333-525 |
8.38e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVwfSYPGRQEPVlkgvSLELRPGEVLALLGPPGAGKSTLVALVSRLhQPTAGRLLLDGHPLPAYQHS-------Y 405
Cdd:PRK03695 1 MQLNDV--AVSTRLGPL----SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelarhraY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQEPLL--FARSLHANISYglgGCSWAQVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIAR 483
Cdd:PRK03695 74 LSQQQTPPFAMPVFqyLTLHQPDKTRT---EAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099372369 484 ALLR-DPRI------LILDEHTSALDTESQQQVEQEILAAKGSGRAVLM 525
Cdd:PRK03695 140 VVLQvWPDInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVM 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
345-567 |
9.30e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 77.56 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 345 RQEPVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQPTA-------GRLLLDGHPLPAYQHSYLCRQVAVVPQ- 415
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 ----------EPLLFARSLHAN----ISYGLGGCSWAQVTAAarrvgahdfitrlpqGYDTEVGELGGQLSGGQRQAVAI 481
Cdd:PRK13547 92 aqpafafsarEIVLLGRYPHARragaLTHRDGEIAWQALALA---------------GATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 482 ARAL---------LRDPRILILDEHTSALDTESQQQVEQEI--LAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQE 550
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|....*..
gi 2099372369 551 GPPHEVLRPGSLLRDWG 567
Cdd:PRK13547 237 GAPADVLTPAHIARCYG 253
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-527 |
9.72e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 9.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpayqHSYLCRQVAVVPQEPLLFARSLH--- 425
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM----SKLSSAAKAELRNQKLGFIYQFHhll 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ------ANISYGL--GGCSWAQVTAAARRVGAhdfitrlPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEH 497
Cdd:PRK11629 100 pdftalENVAMPLliGKKKPAEINSRALEMLA-------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|...
gi 2099372369 498 TSALD---TESQQQVEQEILAAKGSgrAVLMVT 527
Cdd:PRK11629 173 TGNLDarnADSIFQLLGELNRLQGT--AFLVVT 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
349-526 |
1.04e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.84 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VAVVPQEPLLFAR-SLHA 426
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGLGGCSWAQVTAAARRVgaHDFITRLpqgYDTEVgELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQ 506
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIKWV--YELFPRL---HERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180
....*....|....*....|
gi 2099372369 507 QQVEQEILAAKGSGRAVLMV 526
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLV 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
348-527 |
1.11e-15 |
|
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: 75.86 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYlCRQVAVVPQEPLLFAR-SLHA 426
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGLGGCSWAQVTA--AARRVGAHDFiTRLPqgydtevgelGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTE 504
Cdd:TIGR01189 93 NLHFWAAIHGGAQRTIedALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|...
gi 2099372369 505 SQQQVEQEILAAKGSGRAVLMVT 527
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTT 184
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
62-308 |
1.20e-15 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 77.52 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 62 VLLGLSSAvtelvCDVTFVGTLS-RTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLwyl 140
Cdd:cd18575 47 LVLALASA-----LRFYLVSWLGeRVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 141 aRGLCLF----ATMAWLSPRMALLTALALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGA 216
Cdd:cd18575 119 -RNLLLLigglVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 217 AAHYRQRLQQSHRLEKKDV---ALYTASLWTSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLD 293
Cdd:cd18575 198 RQRFATAVEAAFAAALRRIrarALLTALVIFLVFGAIVF---VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSE 274
|
250
....*....|....*
gi 2099372369 294 YFPTLMKAVGSSEKI 308
Cdd:cd18575 275 VWGDLQRAAGAAERL 289
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
349-556 |
1.53e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.97 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRL-----LLDGHPLPAYQHSY-----------LCRQVAV 412
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELITNpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEP--LLFARSLHANISYG---LGgcswaQVTAAARRVGAHdFITRLPQGYD-TEVGELGgqLSGGQRQAVAIARALL 486
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpvaLG-----VKKSEAKKLAKF-YLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEGPPHEV 556
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
22-308 |
1.71e-15 |
|
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: 77.08 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCdvTFVGT--LSRTQSR----LQRRVF 95
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLA--SYLQTylMAYVGQRvvrdLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 96 AAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAV 175
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 176 GHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALYTASLWTSGF-SALALkM 254
Cdd:cd18552 160 GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELlGAIAI-A 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 255 GILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18552 239 LVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
350-566 |
1.82e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.13 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ----VAVVPQ--EPLLFARS 423
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkrIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHANISYGLGGCSWAQVTAAARrvgAHDFITRLpqGYDTEVGELGG-QLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNY---AHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 503 TESQQQVEQEILAAK-GSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDW 566
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVShDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
333-527 |
2.39e-15 |
|
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: 75.45 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYpGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLL----LDGHPLPAYQHSYLCR 408
Cdd:cd03290 1 VQVTNGYFSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHANISYG--LGGCSWAQVTAAArrvGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALL 486
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGspFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQE-ILA-AKGSGRAVLMVT 527
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHLSDHLMQEgILKfLQDDKRTLVLVT 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-509 |
3.14e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHpLPAYQHSYLCRQVAVV------------PQEP 417
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-VPFKRRKEFARRIGVVfgqrsqlwwdlpAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLfarsLHANIsYglggcswaqvtaaarRVGAHDFITRLpqGYDTEVGELGG-------QLSGGQRQAVAIARALLRDPR 490
Cdd:COG4586 117 FR----LLKAI-Y---------------RIPDAEYKKRL--DELVELLDLGElldtpvrQLSLGQRMRCELAAALLHRPK 174
|
170
....*....|....*....
gi 2099372369 491 ILILDEHTSALDTESQQQV 509
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAI 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
353-502 |
3.56e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL---------PAYQhsylcRQVAVVPQEPLLFAR- 422
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgiclPPEK-----RRIGYVFQDARLFPHy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:PRK11144 92 KVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-564 |
4.53e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAV 412
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQEP--LLFARSLHANISYG---LGGCSWA---QVTAAARRVGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARA 484
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGpinLGLDEETvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVTGRAALAARAQR-VVVLEGGEVRQEGPPHEVLRPGSL 562
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQPDL 231
|
..
gi 2099372369 563 LR 564
Cdd:PRK13652 232 LA 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-557 |
6.09e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEP------------ 417
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 -LLFARSLHANISyglGGCSWAQVTAAARRVG-AHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:PRK15112 109 iLDFPLRLNTDLE---PEQREKQIIETLRQVGlLPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGS-GRAVLMVTGRAALAARAQ-RVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
21-279 |
6.45e-15 |
|
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: 75.66 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 21 CAAVMGLMAASALGEMA---VPYYMGRASDWVAREDELAAILpMVLLGLSSAVTelVCDVTFVGTLS-RTQSRLQRRVFA 96
Cdd:cd18574 7 AAALVNIQIPLLLGDLVnviSRSLKETNGDFIEDLKKPALKL-LGLYLLQSLLT--FAYISLLSVVGeRVAARLRNDLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 97 AVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVG 176
Cdd:cd18574 84 SLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 177 HFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKK---DVALYTaslwtsGFSALALK 253
Cdd:cd18574 164 SFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKlglGIGIFQ------GLSNLALN 237
|
250 260
....*....|....*....|....*....
gi 2099372369 254 ---MGILYYGGQLVAAGTVSTGDLVTFLL 279
Cdd:cd18574 238 givLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
350-527 |
9.89e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ--PTA---GRLLLDGHPL--PAYQHSYLCRQVAVVPQEPLLFAR 422
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISY-----GLGGCSWAQVTAAARRVGAHDFIT-RLPQGydtevgelGGQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK14243 106 SIYDNIAYgarinGYKGDMDELVERSLRQAALWDEVKdKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|.
gi 2099372369 497 HTSALDTESQQQVEqEILAAKGSGRAVLMVT 527
Cdd:PRK14243 178 PCSALDPISTLRIE-ELMHELKEQYTIIIVT 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
348-527 |
1.14e-14 |
|
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: 77.64 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLlldghplpayQHSylcRQVAVVPQEPLLFARSLHAN 427
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHS---GRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 428 ISYGLGGCSWaQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQ 507
Cdd:TIGR01271 507 IIFGLSYDEY-RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180
....*....|....*....|
gi 2099372369 508 QVEQEILAAKGSGRAVLMVT 527
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVT 605
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
333-572 |
1.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.40 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGR---QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHS----Y 405
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQ--EPLLFARSLHANISYGLG--GCSWAQVTAAARR----VG-AHDFITRLPqgydtevgelgGQLSGGQR 476
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQnfGVSQEEAEALAREklalVGiSESLFEKNP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRA-ALAARAQRVVVLEGGEVRQEGPPHE 555
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGKPKD 231
|
250
....*....|....*..
gi 2099372369 556 VLRPGSLLRDwGQQGAP 572
Cdd:PRK13649 232 IFQDVDFLEE-KQLGVP 247
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
27-280 |
1.67e-14 |
|
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: 74.37 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 27 LMAASALGEMAVPYYMGRASDWVAREDELAA-----ILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQ 101
Cdd:cd18541 7 FLILVDLLQLLIPRIIGRAIDALTAGTLTASqllryALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 102 SITELRADGAGDVAMRVTRDAEDVREALGEALslllWYLARGLCLFAT----MAWLSPRMALLTALALPLLLALPRAVG- 176
Cdd:cd18541 87 SPSFYQKNRTGDLMARATNDLNAVRMALGPGI----LYLVDALFLGVLvlvmMFTISPKLTLIALLPLPLLALLVYRLGk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 177 ----HFRQAlapqmQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRlqqSHRLEKK--DVALYTASLW-----TS 245
Cdd:cd18541 163 kihkRFRKV-----QEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKL---NEEYVEKnlRLARVDALFFpliglLI 234
|
250 260 270
....*....|....*....|....*....|....*
gi 2099372369 246 GFSALAlkmgILYYGGQLVAAGTVSTGDLVTFLLY 280
Cdd:cd18541 235 GLSFLI----VLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
333-556 |
2.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSY-PGR--QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY---- 405
Cdd:PRK13641 3 IKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LCRQVAVVPQ--EPLLFARSLHANISYGLG--GCSWAQVTAAA----RRVG-AHDFITRLPqgydtevgelgGQLSGGQR 476
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfGFSEDEAKEKAlkwlKKVGlSEDLISKSP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHE 555
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVThNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
.
gi 2099372369 556 V 556
Cdd:PRK13641 232 I 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
328-563 |
2.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 328 DLQGHLQLEDVWFSYpGRQEP----VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA--- 400
Cdd:PRK13645 2 DFSKDIILDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 401 --YQHSYLCRQVAVVPQEP--LLFARSLHANISYG---LGgcswAQVTAAARRVGAHDFITRLPQGYdteVGELGGQLSG 473
Cdd:PRK13645 81 kiKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnLG----ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 474 GQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAA-KGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEG 551
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVThNMDQVLRIADEVIVMHEGKVISIG 233
|
250
....*....|..
gi 2099372369 552 PPHEVLRPGSLL 563
Cdd:PRK13645 234 SPFEIFSNQELL 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
333-520 |
2.45e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY--QHSylcrQV 410
Cdd:PRK10762 5 LQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSS----QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 A---VVPQE-PLLFARSLHANISYG------LGGCSWAQVTAAARRVgahdfITRLPQGYDTEvgELGGQLSGGQRQAVA 480
Cdd:PRK10762 79 AgigIIHQElNLIPQLTIAENIFLGrefvnrFGRIDWKKMYAEADKL-----LARLNLRFSSD--KLVGELSIGEQQMVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 481 IARALLRDPRILILDEHTSAL-DTESQQ--QVEQEiLAAKGSG 520
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETESlfRVIRE-LKSQGRG 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
338-511 |
2.60e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 338 VWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKS-TLVALVSRLHQP----TAGRLLLDGHPLPAYQHSYLCR---- 408
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLFARSLHaNISYGLggcswAQVTA--------AAR--------RVGAHDFITRLpqgydtevGELGGQLS 472
Cdd:PRK15134 93 KIAMIFQEPMVSLNPLH-TLEKQL-----YEVLSlhrgmrreAARgeilncldRVGIRQAAKRL--------TDYPHQLS 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 473 GGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQ 511
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQ 197
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-308 |
3.31e-14 |
|
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: 73.58 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDW--VAREDELAAILPMVLLGLSSAVTELVCDVTFVGTLSRT-QS---RLQRRVF 95
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgQRiiyDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 96 AAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLAlprAV 175
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL---AT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 176 GHFRQALAPQMQKAQARASEVAV---ETFQAMATVRSFANEDGAAAHYRQrLQQSHRLEKKDVALYTASLW--TSGFSAL 250
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAflqESISGMSVIQLFNREKREFEEFDE-INQEYRKANLKSIKLFALFRplVELLSSL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 251 ALkMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18544 238 AL-ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
348-558 |
4.44e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP----TAGRLLLDGHPLPAyqHSYLCRQVAVVPQEPLLFARS 423
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP--CALRGRKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHANISYGLGGC-------SWAQVTAAARRVGAHDfITRLPQGYDTEvgelggqLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK10418 95 LHTMHTHARETClalgkpaDDATLTAALEAVGLEN-AARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 497 HTSALDTESQQQVE---QEILAAKGSGraVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:PRK10418 167 PTTDLDVVAQARILdllESIVQKRALG--MLLVThDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
348-546 |
5.61e-14 |
|
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: 72.58 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLlldghplpayQHSylcRQVAVVPQEPLLFARSLHAN 427
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHS---GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 428 ISYGLG--GCSWAQVTAAARrvgAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:cd03291 118 IIFGVSydEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2099372369 506 QQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGE 546
Cdd:cd03291 195 EKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
331-564 |
7.51e-14 |
|
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: 72.19 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQpTAGRLLLDG-----HPLPAYQHSY 405
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnsVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 lcrqvAVVPQEPLLFARSLHANIS-YGlggcSWA--QVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIA 482
Cdd:cd03289 80 -----GVIPQKVFIFSGTFRKNLDpYG----KWSdeEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 483 RALLRDPRILILDEHTSALDTESqQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSL 562
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
..
gi 2099372369 563 LR 564
Cdd:cd03289 230 FK 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-567 |
9.46e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPA----YQHSYLCRQVAVVPQ--EPLLFARS 423
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHANISYGLG--GCSWAQVTAAARR----VG-AHDFITRLPqgYDtevgelggqLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK13634 103 VEKDICFGPMnfGVSEEDAKQKAREmielVGlPEELLARSP--FE---------LSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 497 HTSALDTESQQQVeQEILAA--KGSGRAVLMVTGRAA-LAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDWG 567
Cdd:PRK13634 172 PTAGLDPKGRKEM-MEMFYKlhKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIG 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-557 |
1.21e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 342 YPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ--PTA---GRLLLDGHPL--PAYQHSYLCRQVAVVP 414
Cdd:PRK14267 13 YYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIysPDVDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 415 QEPLLFAR-SLHANISYGLggcswaQVTAAARRVGAHDFITR-------LPQGYDTEVGELGGQLSGGQRQAVAIARALL 486
Cdd:PRK14267 92 QYPNPFPHlTIYDNVAIGV------KLNGLVKSKKELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-557 |
1.32e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAG-----RLLLDGHPLPAYQHSY-LCRQVAVVPQEPLLFAR 422
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISYGlggcswaqvtaaarrVGAHDFITR-----LPQGYDTEVGELGG----------QLSGGQRQAVAIARALLR 487
Cdd:PRK14271 116 SIMDNVLAG---------------VRAHKLVPRkefrgVAQARLTEVGLWDAvkdrlsdspfRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGPPHEVL 557
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
349-567 |
2.03e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.79 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQV------AVVP-----QEP 417
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIgllaqnATTPgditvQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFARSLHANISYGLGGCSWAQVTAAARRVGahdfITRLP-QGYDTevgelggqLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATG----ITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099372369 497 HTSALDTESQ---QQVEQEILAAKGSGRAVLMvTGRAALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLRDWG 567
Cdd:PRK10253 170 PTTWLDISHQidlLELLSELNREKGYTLAAVL-HDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
328-509 |
3.19e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 328 DLQGHLQLED--VWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY 405
Cdd:PRK15079 13 DLKVHFDIKDgkQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 406 LC---RQVAVVPQEPL-----------LFA---RSLHANISyglGGCSWAQVTAAARRVG-AHDFITRLPQgydtevgel 467
Cdd:PRK15079 93 WRavrSDIQMIFQDPLaslnprmtigeIIAeplRTYHPKLS---RQEVKDRVKAMMLKVGlLPNLINRYPH--------- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2099372369 468 ggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:PRK15079 161 --EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQV 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
350-518 |
3.51e-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: 72.16 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRL--HQPTAGRLLLDGHPLPAYQHSYLCRQ-VAVVPQEPLLFAR-SLH 425
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISYG----LGGCSWAQVTAAARrvgAHDFITRLpQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSAL 501
Cdd:TIGR02633 97 ENIFLGneitLPGGRMAYNAMYLR---AKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|
gi 2099372369 502 dTESQQQVEQEI---LAAKG 518
Cdd:TIGR02633 173 -TEKETEILLDIirdLKAHG 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-527 |
1.19e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 342 YPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGrlllDGHPLPAYQHSYLcrqvavvPQEPLL-F 420
Cdd:PRK11819 16 VPP-KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYL-------PQEPQLdP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 421 ARSLHANISYGLGgcswaQVTAAARR-------------------------------VGAHDFIT---------RLPQGy 460
Cdd:PRK11819 84 EKTVRENVEEGVA-----EVKAALDRfneiyaayaepdadfdalaaeqgelqeiidaADAWDLDSqleiamdalRCPPW- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 461 DTEVGelggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:PRK11819 158 DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVT 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
349-551 |
1.25e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDghplpayqhsylcRQVAVVPQEPLLFARSLHANI 428
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 429 SYgLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQ 508
Cdd:PTZ00243 742 LF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 509 VEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEG 551
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-527 |
1.44e-12 |
|
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: 70.35 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 341 SYPGrQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGrlllDGHPLPAYQHSYLcrqvavvPQEPLL- 419
Cdd:TIGR03719 13 VVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----EARPQPGIKVGYL-------PQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 FARSLHANISYGLG----------------GCSWAQVTAAARR----------VGAHDFIT---------RLPQGyDTEV 464
Cdd:TIGR03719 81 PTKTVRENVEEGVAeikdaldrfneisakyAEPDADFDKLAAEqaelqeiidaADAWDLDSqleiamdalRCPPW-DADV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 465 GELggqlSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:TIGR03719 160 TKL----SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVT 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-517 |
1.50e-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: 70.22 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLK---GVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRL-------LLDGHPLPAYQ 402
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 403 HSYLCRQVAVVPQEPLLFA-RSLHANISYGLGgCSWAQVTAAARRVgahdfITRLPQGYDTEVGE-----LGGQLSGGQR 476
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLTEAIG-LELPDELARMKAV-----ITLKMVGFDEEKAEeildkYPDELSEGER 433
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAK 517
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAR 474
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
346-502 |
1.64e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY---QHSYL-CRQVAVVPQE----P 417
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLrAKHVGFVFQSfmliP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 LLFARSlHANISYGLGGCSWAQvtaaaRRVGAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEH 497
Cdd:PRK10584 102 TLNALE-NVELPALLRGESSRQ-----SRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*
gi 2099372369 498 TSALD 502
Cdd:PRK10584 174 TGNLD 178
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
22-308 |
2.00e-12 |
|
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: 67.90 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCDVTFVGTLSRTQSR----LQRRVFAA 97
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERllydLRLRVFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 98 VLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAvgh 177
Cdd:cd18546 82 LQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 178 FRQALAPQMQKAQARASEVA---VETFQAMATVRSFANEDGAAAH-------YRQRLQQSHRLekkdVALYTASLWTSGF 247
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNadlQETLAGIRVVQAFRRERRNAERfaelsddYRDARLRAQRL----VAIYFPGVELLGN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 248 SALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18546 235 LATAA---VLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-527 |
4.96e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpayqhsylcrqVAVVPQEP---------- 417
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-----------VTRSPQDGlangivyise 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 418 ------LLFARSLHANISY-GLGGCS--WAQVTAAARRVGAHDFIT----RLPqGYDTEVGELggqlSGGQRQAVAIARA 484
Cdd:PRK10762 335 drkrdgLVLGMSVKENMSLtALRYFSraGGSLKHADEQQAVSDFIRlfniKTP-SMEQAIGLL----SGGNQQKVAIARG 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 485 LLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS 452
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-526 |
5.70e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 356 ELRPGEVLALLGPPGAGKSTLV-ALVSRLhQPTAGRLLLDghPLPAYQHSYLCRQVAVVPQEpllFARSLHANIsyglgG 434
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAkLLAGVL-KPDEGEVDPE--LKISYKPQYIKPDYDGTVED---LLRSITDDL-----G 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 435 CSWAQvtaaarrvgaHDFITRL--PQGYDTEVGELggqlSGGQRQAVAIARALLRDPRILILDEHTSALDtesqqqVEQE 512
Cdd:PRK13409 430 SSYYK----------SEIIKPLqlERLLDKNVKDL----SGGELQRVAIAACLSRDADLYLLDEPSAHLD------VEQR 489
|
170 180
....*....|....*....|.
gi 2099372369 513 ILAAK-------GSGRAVLMV 526
Cdd:PRK13409 490 LAVAKairriaeEREATALVV 510
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-564 |
6.56e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.68 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSY----LCRQVAVVPQEP--LLFARSLHA 426
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 427 NISYGLGGCSWAQvtAAARRVGAHDFITrlpQGYDTEVGELGG-QLSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:PRK13643 105 DVAFGPQNFGIPK--EKAEKIAAEKLEM---VGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 506 QQQVEQEILAAKGSGRAVLMVTGRA-ALAARAQRVVVLEGGEVRQEGPPHEVLRPGSLLR 564
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
345-518 |
7.05e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 345 RQEPVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQPT-AGRLLLDGHPlPAYQhsyLCRQVAVVPQEPLLFAr 422
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRK-PTKQ---ILKRTGFVTQDDILYP- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 slHANISYGLGGCSWAQV----TAAARRVGAHDFITRL--PQGYDTEVGE--LGGqLSGGQRQAVAIARALLRDPRILIL 494
Cdd:PLN03211 154 --HLTVRETLVFCSLLRLpkslTKQEKILVAESVISELglTKCENTIIGNsfIRG-ISGGERKRVSIAHEMLINPSLLIL 230
|
170 180
....*....|....*....|....*.
gi 2099372369 495 DEHTSALDTESQQQVEQEI--LAAKG 518
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLgsLAQKG 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-517 |
7.25e-12 |
|
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: 65.51 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 356 ELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpAYQHSYlcrqvaVVPQEPLLfARSLHANISYGLGGC 435
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQY------IKADYEGT-VRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 436 SWAQVTAAARrvgahdfiTRLPQGYDTEVGELggqlSGGQRQAVAIARALLRDPRILILDEHTSALDtesqqqVEQEILA 515
Cdd:cd03237 93 PYFKTEIAKP--------LQIEQILDREVPEL----SGGELQRVAIAACLSKDADIYLLDEPSAYLD------VEQRLMA 154
|
..
gi 2099372369 516 AK 517
Cdd:cd03237 155 SK 156
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-556 |
1.42e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQ--PTAGRLL----------------LD 394
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpsKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 395 GHPLPAYQHSY-----------------LCRQVAVVPQEPllFA----RSLHANISYGLGGCSWAQVTAAARrvgAHDFI 453
Cdd:TIGR03269 79 GEPCPVCGGTLepeevdfwnlsdklrrrIRKRIAIMLQRT--FAlygdDTVLDNVLEALEEIGYEGKEAVGR---AVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 454 TRLPQGYdtEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTG--RAA 531
Cdd:TIGR03269 154 EMVQLSH--RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTShwPEV 231
|
250 260
....*....|....*....|....*
gi 2099372369 532 LAARAQRVVVLEGGEVRQEGPPHEV 556
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
349-565 |
1.83e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGR---LLLDGHPL--PAYQHSYLC---------------- 407
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKkkTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 408 ---RQVAVVPQ--EPLLFARSLHANISYGL--GGCSWAQVTAAARR----VG-AHDFITRLPQGydtevgelggqLSGGQ 475
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLFEQTIEKDIIFGPvsMGVSKEEAKKRAAKyielVGlDESYLQRSPFE-----------LSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 476 RQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPH 554
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVThDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
250
....*....|.
gi 2099372369 555 EVLRPGSLLRD 565
Cdd:PRK13651 251 DILSDNKFLIE 261
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
295-496 |
1.85e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.53 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 295 FPTLMKAVGSSEKIFEFLDREPQVAPSGTMAPTDLQgHLQLEDVWFSYPGRQEPVlKGVSLELRPGEVLALLGPPGAGKS 374
Cdd:PRK10522 286 LPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 375 TLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQVAVVPQEPLLFARSlhanisygLGGCSWAQVTAAARrvgahDFIT 454
Cdd:PRK10522 364 TLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL--------LGPEGKPANPALVE-----KWLE 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 455 RLPQGYDTEVGE---LGGQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK10522 431 RLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
55-308 |
2.26e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 65.23 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 55 LAAILPMVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALS 134
Cdd:cd18564 54 LLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 135 LLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRavgHFRQALAPQMQKAQARASEVAV---ETFQAMATVRSFA 211
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAAR---RFSRRIKEASREQRRREGALASvaqESLSAIRVVQAFG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 212 NEDGAAAHYRQRLQQSHRLEKKDVALYTASLWT-SGFSALALkMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRV 290
Cdd:cd18564 211 REEHEERRFARENRKSLRAGLRAARLQALLSPVvDVLVAVGT-ALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRD 289
|
250
....*....|....*...
gi 2099372369 291 LLDYFPTLMKAVGSSEKI 308
Cdd:cd18564 290 LAKLTGRIAKASASAERV 307
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-506 |
2.27e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.35 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHqPTA---GRLLLDGHPlpayqhsylCR--------QVAVV--PQE 416
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEV---------CRfkdirdseALGIViiHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 ----PLLfarSLHANISYG-----LGGCSWAQVTAAAR----RVGAHDfitrLPqgyDTEVGELGGqlsgGQRQAVAIAR 483
Cdd:NF040905 87 laliPYL---SIAENIFLGnerakRGVIDWNETNRRARellaKVGLDE----SP---DTLVTDIGV----GKQQLVEIAK 152
|
170 180
....*....|....*....|....
gi 2099372369 484 ALLRDPRILILDEHTSAL-DTESQ 506
Cdd:NF040905 153 ALSKDVKLLILDEPTAALnEEDSA 176
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
22-291 |
3.02e-11 |
|
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: 64.43 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCDVT---FVGTLS-RTQSRLQRRVFAA 97
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLrryLAGRLSlGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 98 VLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLwYLARGLCLFATMAWLSPRMALLTALALPLLLALPRavgH 177
Cdd:cd18543 82 LQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVAR---R 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 178 FRQALAPQMQKAQARASEVAV---ETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEKKDVALyTASLWT--SGFSALAL 252
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATvveESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARL-RARFWPllEALPELGL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 2099372369 253 kMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVL 291
Cdd:cd18543 237 -AAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-526 |
3.20e-11 |
|
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: 65.96 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 356 ELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDghpLP-AYQHSYlcrqvaVVPQEPLLFARSLHANISYGLGG 434
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKiSYKPQY------ISPDYDGTVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 435 cSWAQvTAAARRVGahdfITRLpqgYDTEVGELggqlSGGQRQAVAIARALLRDPRILILDEHTSALDtesqqqVEQEIL 514
Cdd:COG1245 433 -SYYK-TEIIKPLG----LEKL---LDKNVKDL----SGGELQRVAIAACLSRDADLYLLDEPSAHLD------VEQRLA 493
|
170
....*....|....*....
gi 2099372369 515 AAK-------GSGRAVLMV 526
Cdd:COG1245 494 VAKairrfaeNRGKTAMVV 512
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-526 |
9.55e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQPTAGRLLLDGHPLpAYQHsylCRQ-----VAVVPQE-------PLL 419
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVqCLFGAYPGRWEGEIFIDGKPV-KIRN---PQQaiaqgIAMVPEDrkrdgivPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 farSLHANISYGLGG--CSWAQVTAAARRVGAHDFITRLPqgYDTEVGELG-GQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK13549 357 ---GVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLK--VKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190
....*....|....*....|....*....|
gi 2099372369 497 HTSALDTESQQQVEQEILAAKGSGRAVLMV 526
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-527 |
1.10e-10 |
|
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: 64.08 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VAVVPQEpllfaRSLHANIS- 429
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVqALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAgIAMVPED-----RKRHGIVPi 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 430 YGLGG----------CSWAQVTAAARRVGAHDFITRLPQGYDTEVGELGGqLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:TIGR02633 354 LGVGKnitlsvlksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180
....*....|....*....|....*...
gi 2099372369 500 ALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVS 460
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
333-506 |
1.32e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEpvLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRL--------LLDGHPLPAYQHS 404
Cdd:PRK11701 7 LSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 405 YLCR-QVAVVPQEP---LLFARSLHANIS---YGLGGCSWAQVTAAA----RRVG-AHDFITRLPQGYdtevgelggqlS 472
Cdd:PRK11701 85 RLLRtEWGFVHQHPrdgLRMQVSAGGNIGerlMAVGARHYGDIRATAgdwlERVEiDAARIDDLPTTF-----------S 153
|
170 180 190
....*....|....*....|....*....|....
gi 2099372369 473 GGQRQAVAIARALLRDPRILILDEHTSALDTESQ 506
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQ 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
345-509 |
1.74e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 345 RQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH---PLPAYQHSYLCRQVAVVPQEP---L 418
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LFARSLHANISYGLGGCSWAQVTAAARRVG-AHDFITRLPQgydtEVGELGGQLSGGQRQAVAIARALLRDPRILILDEH 497
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAwLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170
....*....|..
gi 2099372369 498 TSALDTESQQQV 509
Cdd:PRK10261 491 VSALDVSIRGQI 502
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
340-527 |
1.82e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYpgRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHP----LPAYQHSyLCRQVAVVPQ 415
Cdd:PRK13540 9 FDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdLCTYQKQ-LCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 EPLLfarSLHANISYGLGGCSWAQVTAAARRVGAHDFITRLPQGYdtevgelggqLSGGQRQAVAIARALLRDPRILILD 495
Cdd:PRK13540 86 NPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|..
gi 2099372369 496 EHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTS 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
333-526 |
2.36e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVwfSYPGRQEPVlkgvSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLCRQ-VA 411
Cdd:PRK11288 258 LRLDGL--KGPGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 VVP----QEPLLFARSLHANIS------YGLGGC----SWAQVTaAARRVGAHDFITRLPQgydtevgELGGQLSGGQRQ 477
Cdd:PRK11288 332 LCPedrkAEGIIPVHSVADNINisarrhHLRAGClinnRWEAEN-ADRFIRSLNIKTPSRE-------QLIMNLSGGNQQ 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMV 526
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV 452
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
343-502 |
2.67e-10 |
|
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: 60.35 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 343 PGRQE-PVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQP--TAGRLLLDGHPLPAYQHSYLcRQVAVVPQE-- 416
Cdd:cd03233 15 KGRSKiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkALANRTEGNvsVEGDIHYNGIPYKEFAEKYP-GEIIYVSEEdv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 417 --PLLFARslhanisyglggcswaQVTAAARRVGAHDFItrlpQGydtevgelggqLSGGQRQAVAIARALLRDPRILIL 494
Cdd:cd03233 94 hfPTLTVR----------------ETLDFALRCKGNEFV----RG-----------ISGGERKRVSIAEALVSRASVLCW 142
|
....*...
gi 2099372369 495 DEHTSALD 502
Cdd:cd03233 143 DNSTRGLD 150
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
343-524 |
2.76e-10 |
|
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: 59.95 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 343 PGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVS-RLHQPT-AGRLLLDGHPLPAyqhsYLCRQVAVVPQEPLLF 420
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgRKTAGViTGEILINGRPLDK----NFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 421 ARS-------LHANisygLGGcswaqvtaaarrvgahdfitrlpqgydtevgelggqLSGGQRQAVAIARALLRDPRILI 493
Cdd:cd03232 92 PNLtvrealrFSAL----LRG------------------------------------LSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190
....*....|....*....|....*....|...
gi 2099372369 494 LDEHTSALDTESQQQVEQEI--LAAkgSGRAVL 524
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLkkLAD--SGQAIL 162
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
340-527 |
4.24e-10 |
|
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: 63.11 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 340 FSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSylCRQ-VAVVPQEPL 418
Cdd:TIGR01257 938 FEPSGR--PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA--VRQsLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LFAR---SLHANISYGLGGCSW--AQVTAAA--RRVGAHDfitrlpqgydtEVGELGGQLSGGQRQAVAIARALLRDPRI 491
Cdd:TIGR01257 1014 LFHHltvAEHILFYAQLKGRSWeeAQLEMEAmlEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 492 LILDEHTSALDTESQQQVEQEILAAKgSGRAVLMVT 527
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMST 1117
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
22-308 |
5.60e-10 |
|
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: 60.56 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCDVTFVGTLSR-TQS---RLQRRVFAA 97
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKvGQRilyDLRQDLFSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 98 VLRQSITELRADGAGDVAMRVTRDAEDVREAL--------GEALSLLlwylarglCLFATMAWLSPR-----MALLTALA 164
Cdd:cd18545 83 LQKLSFSFFDSRPVGKILSRVINDVNSLSDLLsnglinliPDLLTLV--------GIVIIMFSLNVRlalvtLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 165 LPLLLALPRAVGHFRQAlapqmQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRqRLQQSHRLEKKDVALYTASLW- 243
Cdd:cd18545 155 LVVFLLRRRARKAWQRV-----RKKISNLNAYLHESISGIRVIQSFAREDENEEIFD-ELNRENRKANMRAVRLNALFWp 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 244 ---TSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18545 229 lveLISALGTAL---VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
346-509 |
6.99e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 346 QEPVLKGVSLELRPGEVLALLGPPGAGKSTL-----------------VALVSRLHQpTAGRLLLDGHPLPAyQHSYLCR 408
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagshIELLGRTVQ-REGRLARDIRKSRA-NTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 409 QVAVVPQEPLLfarslhANISYGLGGCS--WAQVT---AAARRVGAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIAR 483
Cdd:PRK09984 94 QFNLVNRLSVL------ENVLIGALGSTpfWRTCFswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180
....*....|....*....|....*.
gi 2099372369 484 ALLRDPRILILDEHTSALDTESQQQV 509
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIV 191
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-527 |
7.92e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 341 SYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSylcRQVAVVPQEPLLF 420
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 421 AR-SLHANISY--GLGGCSWAQVTAAARR-VGAHDFITRLPQgydtevgelggQLSGGQRQAVAIARALLRDPRILILDE 496
Cdd:PRK13543 95 ADlSTLENLHFlcGLHGRRAKQMPGSALAiVGLAGYEDTLVR-----------QLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190
....*....|....*....|....*....|.
gi 2099372369 497 HTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHLRGGGAALVTT 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
333-527 |
1.13e-09 |
|
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: 61.57 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL-----PAYQHSYLC 407
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 408 RQVAVVpqEPLLFARSlHANISYGLGGCSWAQVTAAARRVgahdfITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLR 487
Cdd:TIGR01257 2018 PQFDAI--DDLLTGRE-HLYLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 488 DPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS 2127
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
349-509 |
1.27e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.92 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP----TAGRLLLDGHPL----PAYQHSYLCRQVAVVPQEPL-- 418
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklsPRERRKIIGREIAMIFQEPSsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 -----LFARSLHANISYGLGGCSWAQVTAAAR--------RVGA--HDFITR-LPQgydtevgelggQLSGGQRQAVAIA 482
Cdd:COG4170 102 ldpsaKIGDQLIEAIPSWTFKGKWWQRFKWRKkraiellhRVGIkdHKDIMNsYPH-----------ELTEGECQKVMIA 170
|
170 180
....*....|....*....|....*..
gi 2099372369 483 RALLRDPRILILDEHTSALDTESQQQV 509
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQI 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-503 |
2.20e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQ---PTAGRLLLDGHPLPAYQHSY-----LCRQVAV-VP---- 414
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvYNAETDVhFPhltv 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 415 QEPLLFARSLHaniSYGLGGCSWAQVTAAARRVGAHDFITRLPQGYDTEVG-ELGGQLSGGQRQAVAIARALLRDPRILI 493
Cdd:TIGR00956 156 GETLDFAARCK---TPQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170
....*....|
gi 2099372369 494 LDEHTSALDT 503
Cdd:TIGR00956 233 WDNATRGLDS 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
341-509 |
4.03e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 341 SYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLH--QPTAGRLLLDGHPLPayqhsylcRQVAVVPQEPL 418
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LfarslhanisyglggCSWAQVTAAARRVGAHDfitrlPQGYDTEVGElggqLSGGQRQAVAIARALLRDPRILILDEHT 498
Cdd:COG2401 109 K---------------GDFKDAVELLNAVGLSD-----AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170
....*....|.
gi 2099372369 499 SALDTESQQQV 509
Cdd:COG2401 165 SHLDRQTAKRV 175
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
348-519 |
9.70e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTL-------VAL------------VSRLHQ--P----------TAGRLLLDGH 396
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLmkilngeVLLddgriiyeqdliVARLQQdpPrnvegtvydfVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 397 PLPAYQHsyLCRQVAVVPQEPLL--FARsLHANISYgLGGcsWaQVTAaarRVgaHDFITRLPQGYDTEVGELGGqlsGG 474
Cdd:PRK11147 97 YLKRYHD--ISHLVETDPSEKNLneLAK-LQEQLDH-HNL--W-QLEN---RI--NEVLAQLGLDPDAALSSLSG---GW 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2099372369 475 QRQAvAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS 519
Cdd:PRK11147 162 LRKA-ALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
359-527 |
9.75e-09 |
|
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: 54.30 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 359 PGEVLALLGPPGAGKSTLVALVSRLHQPTAGR-LLLDGHPLPAYQHSylcrqvavvpqepllfarslhanisyglggcsw 437
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLD--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 438 aqvtaaarrvgahdfitrlpQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI---- 513
Cdd:smart00382 48 --------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170
....*....|....*.
gi 2099372369 514 --LAAKGSGRAVLMVT 527
Cdd:smart00382 108 llLLKSEKNLTVILTT 123
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-308 |
1.01e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 56.75 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVARE---DELAAILPMVLLGL-SSAVTELVCDV--TFVGTL--SRTQSRLQRR 93
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDDVLIQlgpGGNTSLLLLLVLGLaGAYVLSALLGIlrGRLLARlgERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 94 VFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPR 173
Cdd:cd18563 82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 174 AVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQShrlekKDVALYTASLWTSGFSALALK 253
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQEL-----LDANIRAEKLWATFFPLLTFL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 254 MG-----ILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18563 237 TSlgtliVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
337-513 |
1.24e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 337 DVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKS-TLVALVSRLHQPTA----GRLLLD---------GHPLPAYQ 402
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGlvqcDKMLLRrrsrqvielSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 403 HSYLCRQVAVVPQEPL-----LFARSLHANISYGL-GGCSWAQVTAAARRVGAHdfiTRLPQGyDTEVGELGGQLSGGQR 476
Cdd:PRK10261 99 RHVRGADMAMIFQEPMtslnpVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQ---VRIPEA-QTILSRYPHQLSGGMR 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-520 |
1.49e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 347 EPVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGH------PLPAYQHSYLC-----RQVAVVPQ 415
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnANEAINHGFALvteerRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 EPLLFaRSLHANI-----SYGLGGC----SWAQVTAAARRVgahdfitRLPqGYDTEVGelggQLSGGQRQAVAIARALL 486
Cdd:PRK10982 341 LDIGF-NSLISNIrnyknKVGLLDNsrmkSDTQWVIDSMRV-------KTP-GHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 487 RDPRILILDEHTSALDTESQQQVEQEI--LAAKGSG 520
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIaeLAKKDKG 443
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
333-519 |
1.55e-08 |
|
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: 57.25 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLdGHPLpayqhsylcrQVAV 412
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQ--EPLLFARSLHANISYGLGGCSWAQVTAAARR-VGAHDFitrlpQGYDTEvgELGGQLSGGQRQAVAIARALLRDP 489
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyVGRFNF-----KGSDQQ--KKVGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190
....*....|....*....|....*....|
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILAAKGS 519
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAGC 492
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
353-527 |
2.28e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHS--------YLC--RQvavvpQEPLLFAR 422
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLPedRQ-----SSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANI-SYGLGGCSWAQVTAAARRV--GAHDFITRLPQGYDTEVGelggQLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:PRK15439 357 PLAWNVcALTHNRRGFWIKPARENAVleRYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180
....*....|....*....|....*...
gi 2099372369 500 ALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFIS 460
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
348-527 |
2.38e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVA-LVSRL-HQPTAGRLLLDGHPL-------PAYQHSYLCRQVAV-VP--Q 415
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSAtLAGREdYEVTGGTVEFKGKDLlelspedRAGEGIFMAFQYPVeIPgvS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 416 EPLLFARSLHANISYglggcswaQVTAAARRVGAHDFIT------RLPQGYDTEVGELGgqLSGGQRQAVAIARALLRDP 489
Cdd:PRK09580 95 NQFFLQTALNAVRSY--------RGQEPLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 2099372369 490 RILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVT 202
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
176-295 |
3.64e-08 |
|
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: 55.16 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 176 GHFRQALAPQMQkAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRL----QQSHRLEKKDVALYTASLWTSGFSALA 251
Cdd:cd18567 163 PPLRRATEEQIV-ASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLvdaiNADIRLQRLQILFSAANGLLFGLENIL 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2099372369 252 lkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYF 295
Cdd:cd18567 242 ----VIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKL 281
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
335-510 |
4.21e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 335 LEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLpAYQHS--YLCRQVAV 412
Cdd:PRK10982 1 MSNISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkeALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 413 VPQE-PLLFARSLHANISYGlggcswaqvtaaaRRVGAHDFITRLPQGYDTEV--GELG---------GQLSGGQRQAVA 480
Cdd:PRK10982 78 VHQElNLVLQRSVMDNMWLG-------------RYPTKGMFVDQDKMYRDTKAifDELDididprakvATLSVSQMQMIE 144
|
170 180 190
....*....|....*....|....*....|
gi 2099372369 481 IARALLRDPRILILDEHTSALdteSQQQVE 510
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSL---TEKEVN 171
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
64-308 |
6.41e-08 |
|
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: 54.59 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 64 LGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLAR- 142
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATf 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 143 --GLCLFATMAW-LSPRMALLTALALPLLLALPRAVGHFrqalAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAH 219
Cdd:cd18558 148 gtGFIIGFIRGWkLTLVILAISPVLGLSAVVWAKILSGF----TDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 220 YRQRLQQSHRLEKKDVALYTASLWTSGFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLM 299
Cdd:cd18558 224 YAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFA 303
|
....*....
gi 2099372369 300 KAVGSSEKI 308
Cdd:cd18558 304 NARGAAYHI 312
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-526 |
6.94e-08 |
|
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: 53.91 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 358 RPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLllDGHP-----LPAYQ----HSYLCR------QVAVVPQEPLLFAR 422
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeiLDEFRgselQNYFTKllegdvKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANISyglggcswaQVTAAARRVGAHDFI---TRLPQGYDTEVGelggQLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:cd03236 102 AVKGKVG---------ELLKKKDERGKLDELvdqLELRHVLDRNID----QLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|...
gi 2099372369 500 ALDtesqqqVEQEILAAK------GSGRAVLMV 526
Cdd:cd03236 169 YLD------IKQRLNAARlirelaEDDNYVLVV 195
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-308 |
9.31e-08 |
|
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: 53.97 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLGLSSAVTELVCdvTFVGTLS------RTQSRLQRRVF 95
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVF--RYLQGYLaekasqKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 96 AAVLRQSITELraDGA--GDVAMRVTRDAEDVREALGEALSLLLwylaRGLCLFAT----MAWLSPRMALLTALALPLLL 169
Cdd:cd18542 80 DHLQRLSFSFH--DKArtGDLMSRCTSDVDTIRRFLAFGLVELV----RAVLLFIGaliiMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 170 ALPRavgHFRQALAP---QMQKAQARASEVAVETFQAMATVRSFANE-------DGAAAHYRQR-LQQSHRLekkdvALY 238
Cdd:cd18542 154 LFSY---VFFKKVRPafeEIREQEGELNTVLQENLTGVRVVKAFAREdyeiekfDKENEEYRDLnIKLAKLL-----AKY 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 239 TASLWTSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18542 226 WPLMDFLSGLQIVL---VLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
315-518 |
9.36e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 315 EPQVAPSGTMAPTDlQGHLQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLH-QPTAGRLLL 393
Cdd:PRK10938 244 EPDEPSARHALPAN-EPRIVLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 394 DGhplpayqhsylcRQ------VAVVPQEPLLFARSLHANI----------------SYGLggcswAQVTAAARRVGAHD 451
Cdd:PRK10938 321 FG------------RRrgsgetIWDIKKHIGYVSSSLHLDYrvstsvrnvilsgffdSIGI-----YQAVSDRQQKLAQQ 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 452 FITRLpqGYDTEVGELGGQ-LSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQ--EILAAKG 518
Cdd:PRK10938 384 WLDIL--GIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRfvDVLISEG 451
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
350-508 |
1.09e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQH-SYLCRQVAVVPQ------EPLLfar 422
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrRAVCPRIAYMPQglgknlYPTL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 423 SLHANIS-----YGLGgcswaqvtAAARRV---------GAHDFITRLpqgydtevgelGGQLSGGQRQAVAIARALLRD 488
Cdd:NF033858 94 SVFENLDffgrlFGQD--------AAERRRridellratGLAPFADRP-----------AGKLSGGMKQKLGLCCALIHD 154
|
170 180
....*....|....*....|
gi 2099372369 489 PRILILDEHTSALDTESQQQ 508
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQ 174
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-308 |
1.71e-07 |
|
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: 53.18 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 22 AAVMGLMAASALGEMAVPYYMGRASDWVAreDELAAILPMVLLGLSSAVTELVCdVTFVGTLSrtqSRLQRRVFAAVLRQ 101
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLII--EGLGGGGGVDFSGLLRILLLLLG-LYLLSALF---SYLQNRLMARVSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 102 SITELRAD----------------GAGDVAMRVTRDAEDVREALGEALSLLLwylaRGLCL----FATMAWLSPRMALLT 161
Cdd:cd18547 76 TVYDLRKDlfeklqrlplsyfdthSHGDIMSRVTNDVDNISQALSQSLTQLI----SSILTivgtLIMMLYISPLLTLIV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 162 ALALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRlqqSHRLEKKDV-ALYTA 240
Cdd:cd18547 152 LVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEI---NEELYKASFkAQFYS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 241 SL---WTSGFSALALkMGILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18547 229 GLlmpIMNFINNLGY-VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
353-558 |
2.09e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKS----TLVALVSRLHQPTAGRLLLDGHPL----PAYQHSYLCRQVAVVPQEPLlfaRSL 424
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLqrisEKERRNLVGAEVAMIFQDPM---TSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 425 haNISYGLGgcswAQVTAA----------ARRVGAHDFITRLpqGYDTEVGELG---GQLSGGQRQAVAIARALLRDPRI 491
Cdd:PRK11022 103 --NPCYTVG----FQIMEAikvhqggnkkTRRQRAIDLLNQV--GIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 492 LILDEHTSALDTESQQQVEQEILA-AKGSGRAVLMVT-GRAALAARAQRVVVLEGGEVRQEGPPHEVLR 558
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLElQQKENMALVLIThDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
357-526 |
2.18e-07 |
|
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: 53.63 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 357 LRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLllDGHP-----LPAYQ----HSYLCR------QVAVVPQEPLLFA 421
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYFKKlangeiKVAHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 422 RSLHANISYGLggcswaqvTAAARRVGAHDFITRLPQG--YDTEVGELggqlSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:COG1245 174 KVFKGTVRELL--------EKVDERGKLDELAEKLGLEniLDRDISEL----SGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|...
gi 2099372369 500 ALDtesqqqVEQEILAAK------GSGRAVLMV 526
Cdd:COG1245 242 YLD------IYQRLNVARlirelaEEGKYVLVV 268
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-552 |
2.25e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 331 GHLQLEDVWFSYPGrqepvlkgvslelrpGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLcrqV 410
Cdd:PRK15056 19 GHTALRDASFTVPG---------------GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 411 AVVPQE-------PLL------FARSLHANISYGLGGCSWAQVTAAARRVGAHDFITRlpqgydtEVGELggqlSGGQRQ 477
Cdd:PRK15056 81 AYVPQSeevdwsfPVLvedvvmMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHR-------QIGEL----SGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 478 AVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVTGRAALAARAQRVVVLEGGEVRQEGP 552
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
301-527 |
2.38e-07 |
|
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: 53.60 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 301 AVGSSEKIFEFLDREPQVAPSGTMAPTDlQGhLQLEDVWFSYPGRQEpVLKGVSLELRPGEVLALLGPPGAGKSTLVALV 380
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQD-NG-IKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 381 SRLHQPTAGRLlldghPLPAYQHSYLcrqvavVPQEPLLFARSLHANISYGLG-------GCSWAQVTAAARRVGAHDFI 453
Cdd:TIGR00954 499 GELWPVYGGRL-----TKPAKGKLFY------VPQRPYMTLGTLRDQIIYPDSsedmkrrGLSDKDLEQILDNVQLTHIL 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 454 TRlPQGYDTeVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTEsqqqVEQEIL-AAKGSGRAVLMVT 527
Cdd:TIGR00954 568 ER-EGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYrLCREFGITLFSVS 636
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
349-524 |
3.08e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 349 VLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLHQP--TAGRLLLDGHPLPA-YQHS--YLCRQVAVVPQ----EPL 418
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLnVLAERVTTGviTGGDRLVNGRPLDSsFQRSigYVQQQDLHLPTstvrESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 419 LFARSLHANisyglggcswAQVTAAA--RRVgahDFITRL---PQGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILI 493
Cdd:TIGR00956 858 RFSAYLRQP----------KSVSKSEkmEYV---EEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190
....*....|....*....|....*....|..
gi 2099372369 494 -LDEHTSALDTESQQQVEQEILAAKGSGRAVL 524
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
357-526 |
3.32e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 357 LRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLllDGHP-----LPAYQ----HSYLCR------QVAVVPQEPLLFA 421
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevLKRFRgtelQNYFKKlyngeiKVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 422 RSLHANISyglggcswaQVTAAARRVGAHDFItrlpqgydteVGELG---------GQLSGGQRQAVAIARALLRDPRIL 492
Cdd:PRK13409 174 KVFKGKVR---------ELLKKVDERGKLDEV----------VERLGlenildrdiSELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 493 ILDEHTSALDtesqqqVEQEILAAK-----GSGRAVLMV 526
Cdd:PRK13409 235 FFDEPTSYLD------IRQRLNVARlirelAEGKYVLVV 267
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
337-527 |
3.57e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 337 DVWFSYPGrqEPVLK-----GVSLELRpgevLALLGPPGAGKSTLVALVSRLHQPTAGRLL--------------LDGHP 397
Cdd:PLN03073 513 DASFGYPG--GPLLFknlnfGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 398 LPAYQHSYLCRQVAVVPQEpllfarSLHANI-SYGLGGCSWAQVTAAarrvgahdfitrlpqgydtevgelggqLSGGQR 476
Cdd:PLN03073 587 LSSNPLLYMMRCFPGVPEQ------KLRAHLgSFGVTGNLALQPMYT---------------------------LSGGQK 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 477 QAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGsgrAVLMVT 527
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG---GVLMVS 681
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
337-509 |
5.63e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 337 DVWFSYPGRQEPVLKGVSLELRPGEVLALLGPPGAGKS-TLVALVSRLHQP--TAGRLLLDGHP---LPAYQHSYL-CRQ 409
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnLPEKELNKLrAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEP-------------LLFARSLHANISyglggcswaQVTAAARRVGAHDFItRLPQG------YDTEvgelggq 470
Cdd:PRK09473 99 ISMIFQDPmtslnpymrvgeqLMEVLMLHKGMS---------KAEAFEESVRMLDAV-KMPEArkrmkmYPHE------- 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 471 LSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQV 509
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQI 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
350-527 |
1.27e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTlVALVSRLHQPTAGRLLLDGHPLPAYQHSyLCRQVAVvpQEPLLFAR----SLH 425
Cdd:NF000106 29 VDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRA-LRRTIG*--HRPVR*GRresfSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANIsYGLGgcSWAQVTAAARRVGAHDFITRLpqGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:NF000106 105 ENL-YMIG--R*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
170 180
....*....|....*....|..
gi 2099372369 506 QQQVEQEILAAKGSGRAVLMVT 527
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTT 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-515 |
1.43e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 334 QLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAY--QHsylcRQ-- 409
Cdd:PRK11147 321 EMENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYfdQH----RAel 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 ---------VAVVPQEPLLFARSLHAnISYglggcswaqvtaaarrvgAHDFITRlPQGYDTEVgelgGQLSGGQRQAVA 480
Cdd:PRK11147 395 dpektvmdnLAEGKQEVMVNGRPRHV-LGY------------------LQDFLFH-PKRAMTPV----KALSGGERNRLL 450
|
170 180 190
....*....|....*....|....*....|....*
gi 2099372369 481 IARALLRDPRILILDEHTSALDTESQQQVEqEILA 515
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLDVETLELLE-ELLD 484
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
333-496 |
1.73e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.76 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSYLC---RQ 409
Cdd:PRK11831 8 VDMRGVSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 410 VAVVPQEPLLFAR-SLHANISYGLggcswaqvtaaaRRvgaHdfiTRLPQG--YDT------EVGELGG------QLSGG 474
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPL------------RE---H---TQLPAPllHSTvmmkleAVGLRGAaklmpsELSGG 147
|
170 180
....*....|....*....|..
gi 2099372369 475 QRQAVAIARALLRDPRILILDE 496
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDE 169
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
198-301 |
4.48e-06 |
|
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: 48.60 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 198 VETFQAMATVRSFANEDGAAAHYRQR----LQQSHRLEKKDVALYTASLWTSGFSALalkmGILYYGGQLVAAGTVSTGD 273
Cdd:cd18570 184 IESLKGIETIKSLNAEEQFLKKIEKKfsklLKKSFKLGKLSNLQSSIKGLISLIGSL----LILWIGSYLVIKGQLSLGQ 259
|
90 100
....*....|....*....|....*...
gi 2099372369 274 LVTFLLYQIQFTDVLRVLLDYFPTLMKA 301
Cdd:cd18570 260 LIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
333-505 |
5.96e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 333 LQLEDVWFSYPGRqePVLKGVSLELRPGEVLALLGPPGAGKSTLV-ALVSRLhQPTAGRllldghplpayqhsylcrqva 411
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLrTLVGEL-EPDSGT--------------------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 412 vvpqepllFARSLHANISYglggcsWAQVTaaarrvgAHDF---IT--------RLPQGYDTEV-GELG----GQ----- 470
Cdd:PRK15064 376 --------VKWSENANIGY------YAQDH-------AYDFendLTlfdwmsqwRQEGDDEQAVrGTLGrllfSQddikk 434
|
170 180 190
....*....|....*....|....*....|....*....
gi 2099372369 471 ----LSGGQRQAVAIARALLRDPRILILDEHTSALDTES 505
Cdd:PRK15064 435 svkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES 473
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
25-284 |
7.71e-06 |
|
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: 47.88 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 25 MGLMAASALGEMAVPYYMGRASDWVAREDELAAILPMVLLG-------LSSAVTELvCDVTFVGTLSRTQSRLQRRVFAA 97
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLayglariLSSLFNEL-RDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 98 VLRQSITELRADGAGDVAMRVTRDAEDVREALGEAL-------------SLLLWYL---ARGLCLFATMA---WLSprma 158
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLfnilptilelllvCGILWYLygwSYALITLVTVAlyvAFT---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 159 lltalalplllalpRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQqshRLEKKDVALY 238
Cdd:cd18582 157 --------------IKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALA---KYEKAAVKSQ 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 239 TaSLWTSGFS-----ALALkMGILYYGGQLVAAGTVSTGDLVTFLLYQIQF 284
Cdd:cd18582 220 T-SLALLNIGqaliiSLGL-TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQL 268
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
21-283 |
9.46e-06 |
|
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: 47.78 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 21 CAAVMGLMAASALGEMAVPYYMGRASDWVAREDELAAI----LPMVLLGLSSAVTELVCdvtfvgtlSRTQSR------- 89
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYIlrtgLLMLLLALLGLIAGILA--------GYFAAKasqgfgr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 90 -LQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLL-----------------WYLARGLC-----L 146
Cdd:cd18548 73 dLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVrapimligaiimafrinPKLALILLvaipiL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 147 FATMAWLSprmalltalalplllalPRAVGHFRQalapqMQKAQARASEVAVETFQAMATVRSFANEDgaaahyrqrlQQ 226
Cdd:cd18548 153 ALVVFLIM-----------------KKAIPLFKK-----VQKKLDRLNRVVRENLTGIRVIRAFNRED----------YE 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099372369 227 SHRLEKKDVALYTASLWTSGFSAL----------ALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQ 283
Cdd:cd18548 201 EERFDKANDDLTDTSLKAGRLMALlnplmmlimnLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQ 267
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
199-280 |
1.01e-05 |
|
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: 47.44 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 199 ETFQAMATVRSFANEDgaaaHYRQRLQQS---HRLEKKDVALYTASLwtsgFSALALKMGILY-----YGGQLVAAGTVS 270
Cdd:cd18549 186 DSLSGIRVVKAFANEE----YEIEKFDEGndrFLESKKKAYKAMAYF----FSGMNFFTNLLNlvvlvAGGYFIIKGEIT 257
|
90
....*....|
gi 2099372369 271 TGDLVTFLLY 280
Cdd:cd18549 258 LGDLVAFLLY 267
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
353-509 |
1.85e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP----TAGRLLLDGHPL----PAYQHSYLCRQVAVVPQEPLL----- 419
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLlrlsPRERRKLVGHNVSMIFQEPQScldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 --FARSLHANI-SYGLGGCSWAQVTAAARRvgAHDFITRLP-QGYDTEVGELGGQLSGGQRQAVAIARALLRDPRILILD 495
Cdd:PRK15093 106 erVGRQLMQNIpGWTYKGRWWQRFGWRKRR--AIELLHRVGiKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170
....*....|....
gi 2099372369 496 EHTSALDTESQQQV 509
Cdd:PRK15093 184 EPTNAMEPTTQAQI 197
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-526 |
1.91e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 342 YPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTL-VALVSRLH-QPTAGRLLLDGhplpayqhsylcRQVAVvpqepll 419
Cdd:NF040905 270 HPERK--VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgRNISGTVFKDG------------KEVDV------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 420 faRSLHANISYGLggcswAQVT--------------------AAARRVGAHDFI-----TRLPQGYDTE-------VGEL 467
Cdd:NF040905 329 --STVSDAIDAGL-----AYVTedrkgyglnliddikrnitlANLGKVSRRGVIdeneeIKVAEEYRKKmniktpsVFQK 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2099372369 468 GGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI--LAAkgSGRAVLMV 526
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIIneLAA--EGKGVIVI 460
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
90-283 |
2.68e-05 |
|
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: 46.32 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 90 LQRRVFAAVLRQSI---TELRAdgaGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALP 166
Cdd:cd18550 74 LRVQLYAHLQRMSLaffTRTRT---GEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 167 LLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQA--MATVRSFANEDGAAAHYRQRLQQSHRLEKKdVALYTASLWT 244
Cdd:cd18550 151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVR-QALAGRWFFA 229
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2099372369 245 S-GFSALALKMGILYYGGQLVAAGTVSTGDLVTFLLYQIQ 283
Cdd:cd18550 230 AlGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGR 269
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-527 |
5.33e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 348 PVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSrlhqptagrllldGHplPAYQ---HSYLCRQVAVVPQEPLlfARSl 424
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA-------------GH--PAYKileGDILFKGESILDLEPE--ERA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 425 HANISYG------LGGCSWAQVTAAA---RR-----------------------VGAHD-FITRlpqgydtEVGElggQL 471
Cdd:CHL00131 83 HLGIFLAfqypieIPGVSNADFLRLAynsKRkfqglpeldplefleiineklklVGMDPsFLSR-------NVNE---GF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099372369 472 SGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIT 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
353-502 |
6.08e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 353 VSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPLPAYQHSyLCRQVAVVPQepllfARSL-------- 424
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-TRRRVGYMSQ-----AFSLygeltvrq 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 425 ----HANIsYGLGGCSWAQ-VTAAARRVGAHDFITRLPqgydtevgelgGQLSGGQRQAVAIARALLRDPRILILDEHTS 499
Cdd:NF033858 359 nlelHARL-FHLPAAEIAArVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
...
gi 2099372369 500 ALD 502
Cdd:NF033858 427 GVD 429
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
309-519 |
7.68e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 309 FEFLDREPQVAPSGTmaptdlqghLQLEDVWFSYPGRQepVLKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTA 388
Cdd:PRK10636 298 FHFSFRAPESLPNPL---------LKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVS 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 389 GRL-LLDGHPLPAY-QH---------SYLCRQVAVVPQEPLLFARSLhanisygLGGCSWaqvtaaarrvgahdfitrlp 457
Cdd:PRK10636 367 GEIgLAKGIKLGYFaQHqleflradeSPLQHLARLAPQELEQKLRDY-------LGGFGF-------------------- 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099372369 458 QGydTEVGELGGQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEILAAKGS 519
Cdd:PRK10636 420 QG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
84-308 |
9.63e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 44.58 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 SRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTAL 163
Cdd:cd18561 65 QRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 164 ALPLLLALPRAVGHFRQALAPQMQKAQARASEVAVETFQAMATVRSFanedGAAAHYRQRLQ-QSHRLEKKDVALYTASL 242
Cdd:cd18561 145 FALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAF----GASKRRGNELAaRAEDLRQATMKVLAVSL 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099372369 243 WTSGFSALALKMGI---LYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18561 221 LSSGIMGLATALGTalaLGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
112-308 |
1.05e-04 |
|
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: 44.33 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 112 GDVAMRVTRDAEDVREALGEALSLLLWYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAV-GHFRQaLAPQMQKAQ 190
Cdd:cd18554 103 GEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFfGRLRK-LTKERSQAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 191 ARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLekkdvALYTASLWTSGFSALAL-----KMGILYYGGQLVA 265
Cdd:cd18554 182 AEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTR-----ALKHTRWNAKTFSAVNTitdlaPLLVIGFAAYLVI 256
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2099372369 266 AGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18554 257 EGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
61-289 |
1.29e-04 |
|
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: 44.03 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 61 MVLLGLSSAVTELVCDVTFVGTLSRTQSRLQRRVFAAVLRQSITELRADGAGDVAMRVtRDAEDVREAL-GEALSLLLwY 139
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLtGSALTLVL-D 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 140 LARGLCLFATMAWLSPRMALLTALALPLLLALPRAVG-HFRQALAPQMQKAqARASEVAVETFQAMATVRSFANEDGAAA 218
Cdd:cd18588 126 LVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTpILRRRLEEKFQRG-AENQSFLVETVTGIETVKSLAVEPQFQR 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2099372369 219 HYRQRLqqsHRLEKKDVALYTASLWTSGFSALALKM---GILYYGGQLVAAGTVSTGDLVTFLLYQIQFTD-VLR 289
Cdd:cd18588 205 RWEELL---ARYVKASFKTANLSNLASQIVQLIQKLttlAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQpVLR 276
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-527 |
1.48e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 351 KGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGHPL-PAYQHSYLCRQVAVVPQ---EPLLFAR-SLH 425
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 426 ANISY-------GLGGcSWA-------QVTAAARRvgahDFITRLPQGYDTEVGELggqlSGGQRQAVAIARALLRDPRI 491
Cdd:PRK09700 360 QNMAIsrslkdgGYKG-AMGlfhevdeQRTAENQR----ELLALKCHSVNQNITEL----SGGNQQKVLISKWLCCCPEV 430
|
170 180 190
....*....|....*....|....*....|....*.
gi 2099372369 492 LILDEHTSALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
356-513 |
2.16e-04 |
|
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: 42.17 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 356 ELRPGEVLALLGPPGAGKSTLVALVSRLHQPTAGRLLLDGhPLPAYQHSYLcrqvavvpqepllfarslhanisyglggc 435
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI----------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099372369 436 swaqvtaaarrvgahdfitrlpqgydtevgelggQLSGGQRQAVAIARALLRDPRILILDEHTSALDTESQQQVEQEI 513
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
344-527 |
7.53e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 344 GRQEPVLKGVSLELRPGEVLALLGPPGAGKSTLValvsrlhqptagrllldghplpayqhsylcRQVAVVpqeplLFARS 423
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGAQ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 424 LHANISYGLG-GCSWAQVTAaarrvgahDFITRLPQgydtevgelggqLSGGQRQAVAIARAL---LRDPRIL-ILDEHT 498
Cdd:cd03227 50 SATRRRSGVKaGCIVAAVSA--------ELIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEID 109
|
170 180
....*....|....*....|....*....
gi 2099372369 499 SALDTESQQQVEQEILAAKGSGRAVLMVT 527
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIVIT 138
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
185-284 |
1.47e-03 |
|
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: 40.98 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 185 QMQKAQARASEVAVETFQAMATVRSFANEDgaaahyrqrlQQSHRLEKKDVALYTASL----WTSGFS---ALALKMG-- 255
Cdd:cd18778 170 KVREALGELNALLQDNLSGIREIQAFGREE----------EEAKRFEALSRRYRKAQLramkLWAIFHplmEFLTSLGtv 239
|
90 100 110
....*....|....*....|....*....|
gi 2099372369 256 -ILYYGGQLVAAGTVSTGDLVTFLLYQIQF 284
Cdd:cd18778 240 lVLGFGGRLVLAGELTIGDLVAFLLYLGLF 269
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
236-308 |
1.61e-03 |
|
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: 40.93 E-value: 1.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2099372369 236 ALYTASLWTSGFSALALkmgILYYGGQLVAAGTVSTGDLVTFLLYQIQFTDVLRVLLDYFPTLMKAVGSSEKI 308
Cdd:cd18540 226 ALFLPIVLFLGSIATAL---VLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
110-278 |
3.89e-03 |
|
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: 39.45 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 110 GAGDVAMRVTRDAeDVREAL-GEALSLLLwYLARGLCLFATMAWLSPRMALLTALALPLLLALPRAVGHFRQALAPQMQK 188
Cdd:cd18779 97 STGDLLMRLSSNA-TIRELLtSQTLSALL-DGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 189 AQARASEVAVETFQAMATVRSFANEDGAAAH----YRQRLQQSHRLEKKDVALYTASLWTSGFSALALkmgiLYYGGQLV 264
Cdd:cd18779 175 AQAEAQSYLVEALSGIETLKASGAEDRALDRwsnlFVDQLNASLRRGRLDALVDALLATLRLAAPLVL----LWVGAWQV 250
|
170
....*....|....
gi 2099372369 265 AAGTVSTGDLVTFL 278
Cdd:cd18779 251 LDGQLSLGTMLALN 264
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
350-386 |
5.27e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 38.40 E-value: 5.27e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2099372369 350 LKGVSLELRPGEVLALLGPPGAGKSTLVALVSRLHQP 386
Cdd:pfam03215 35 LDAMFLENAKHRILLISGPSGCGKSTVIKELSKELGP 71
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
84-279 |
6.29e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 39.04 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 84 SRTQSRLQRRVFAAVLRQSITELRADGAGDVaMRVTRDAEDVRE--------ALGEALSLLLwylarglcLFATMAWLSP 155
Cdd:cd18783 71 TRIDARLALRTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQfltgqlfgTLLDATSLLV--------FLPVLFFYSP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099372369 156 RMALLTALALPLLLALPRA-VGHFRQALApQMQKAQARASEVAVETFQAMATVRSFANEDGAAAHYRQRLQQSHRLEkkd 234
Cdd:cd18783 142 TLALVVLAFSALIALIILAfLPPFRRRLQ-ALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRAR--- 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2099372369 235 VALYTASLWTSGFSALALKM---GILYYGGQLVAAGTVSTGDLVTFLL 279
Cdd:cd18783 218 FAVGRLSNWPQTLTGPLEKLmtvGVIWVGAYLVFAGSLTVGALIAFNM 265
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
470-502 |
7.61e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 7.61e-03
10 20 30
....*....|....*....|....*....|...
gi 2099372369 470 QLSGGQRQAVAIARALLRDPRILILDEHTSALD 502
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| |
