|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-740 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 860.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 37 RPALPRVASRLVPPELPLLRVWVAGLSRCALLWLGARGVVGAALGfrrestrvlGWLAVLEPLAAALGLALPGLALFREL 116
Cdd:TIGR00958 21 RDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAVKPLVAALCLATPSLSSLRAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 117 VSWRAPEDADSAGHLHWegrlDAFAFSYWAALPAATLWYKIRSLWVQ------GARGAFGLaMSRLLVFLGPEKSHVQFI 190
Cdd:TIGR00958 92 AFWEALDPAVRVALGLW----SWFVWSYGAALPAAALWAVLSSAGASekeaeqGQSETADL-LFRLLGLSGRDWPWLISA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLR 270
Cdd:TIGR00958 167 FVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 271 QETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYK 350
Cdd:TIGR00958 247 QDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 351 VLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYFG 430
Cdd:TIGR00958 327 LLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 431 GQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPNCPKSGSLASLTLRGSVQFQDVSF 510
Cdd:TIGR00958 407 GQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 511 AYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLL 590
Cdd:TIGR00958 487 SYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 FGRSFKENIAYGLVQEPtMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:TIGR00958 567 FSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 671 SALDANsqslVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMV 740
Cdd:TIGR00958 646 SALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
172-742 |
1.12e-158 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 471.96 E-value: 1.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 172 AMSRLLVFLGPEKSHVQFILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNS 251
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 252 TMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMIT 331
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 332 LVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVN 411
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 412 VWTSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPNCP-K 490
Cdd:COG1132 248 FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPdP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 491 SGSLASLTLRGSVQFQDVSFAYPnrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLP 570
Cdd:COG1132 328 PGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 571 KYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQA 650
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLM 730
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|..
gi 529002597 731 TNEGRYWAMVQA 742
Cdd:COG1132 563 ARGGLYARLYRL 574
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
190-478 |
2.48e-144 |
|
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: 424.19 E-value: 2.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18589 1 VLGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWY 349
Cdd:cd18589 81 RQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 350 KVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYF 429
Cdd:cd18589 161 QSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 529002597 430 GGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18589 241 GGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
492-720 |
3.71e-126 |
|
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: 375.27 E-value: 3.71e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 492 GSLASLTLRGSVQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPK 571
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 572 YEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLVQEPtMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAV 651
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERgsRSVLFITQRLSSVEQADHILFLEGGTI 720
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
165-741 |
8.49e-121 |
|
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: 378.41 E-value: 8.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 165 ARGAFGLAMSRLLVFLGPEKSHV-QFILALVFLSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEF 243
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLlQVLLASLLINLLA-LATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 244 AADGIYNSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDdTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWA 323
Cdd:COG2274 215 LRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 324 SPSLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQK 403
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 404 -EALAYAVNVWTSSLSGMLLkVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYL 482
Cdd:COG2274 374 lRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 483 DRVPNCPKSGSLASL-TLRGSVQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQ 561
Cdd:COG2274 453 DLPPEREEGRSKLSLpRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 562 VLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGS 641
Cdd:COG2274 532 ILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD-PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 642 QLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTII 721
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
570 580
....*....|....*....|
gi 529002597 722 EAGTHQQLMTNEGRYWAMVQ 741
Cdd:COG2274 689 EDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
172-736 |
5.30e-106 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 335.52 E-value: 5.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 172 AMSRLLVFLGPEKshVQFILALVFL--SCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIY 249
Cdd:TIGR02204 5 PLAALWPFVRPYR--GRVLAALVALliTAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 250 NSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTM 329
Cdd:TIGR02204 83 TWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 330 ITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYA 409
Cdd:TIGR02204 163 LVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 410 V---NVWTSSLSGMllkVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVP 486
Cdd:TIGR02204 243 LltaIVIVLVFGAI---VGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 487 N--CPKSGSLASLTLRGSVQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLL 564
Cdd:TIGR02204 320 DikAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 565 DGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLVqEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLS 644
Cdd:TIGR02204 400 DGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP-DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQADHILFLEGGTIIEAG 724
Cdd:TIGR02204 479 GGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRIVAQG 556
|
570
....*....|..
gi 529002597 725 THQQLMTNEGRY 736
Cdd:TIGR02204 557 THAELIAKGGLY 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
503-742 |
9.81e-104 |
|
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: 317.56 E-value: 9.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGK-PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMVQA 742
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
175-736 |
2.24e-93 |
|
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: 302.41 E-value: 2.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 175 RLLVFLGPEKShvQFILALVFLscFGEMAI-PFFTGRLTDWIvqDETAAAFTQNVTL-MSVLTIASAVLEFAADGIYNST 252
Cdd:TIGR02203 4 RLWSYVRPYKA--GLVLAGVAM--ILVAATeSTLAALLKPLL--DDGFGGRDRSVLWwVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 253 MGRVH----SHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIR-GLCLLGL---MLWAS 324
Cdd:TIGR02203 78 LSWVSnkvvRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIV----LVReTLTVIGLfivLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 325 PSLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKE 404
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 405 ALAYAVNVWTSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDR 484
Cdd:TIGR02203 234 TSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 485 VPNcPKSGSLASLTLRGSVQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLL 564
Cdd:TIGR02203 314 PPE-KDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 565 DGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLS 644
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLV----ERLLYEspergsRSVLFITQRLSSVEQADHILFLEGGTI 720
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVqaalERLMQG------RTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570
....*....|....*.
gi 529002597 721 IEAGTHQQLMTNEGRY 736
Cdd:TIGR02203 546 VERGTHNELLARNGLY 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
503-737 |
8.02e-82 |
|
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: 260.24 E-value: 8.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIAYGlVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 663 VLILDDATSALDANSqslvERLLYESPERGS--RSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYW 737
Cdd:cd03251 159 ILILDEATSALDTES----ERLVQAALERLMknRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
191-478 |
3.61e-81 |
|
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: 260.55 E-value: 3.61e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLR 270
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 271 QETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYK 350
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 351 VLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYFG 430
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 529002597 431 GQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
231-736 |
3.07e-80 |
|
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: 270.85 E-value: 3.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 231 MSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDdTSTMSESLSSDLSLLLWYL 310
Cdd:TIGR01846 185 MLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 311 IRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKF 390
Cdd:TIGR01846 264 LFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRW 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 391 RQKLHEMMVLNQKealAYAVNVWTSSLSGMLLKVG---ILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPR 467
Cdd:TIGR01846 344 DRQLAAYVAASFR---VTNLGNIAGQAIELIQKLTfaiLLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQD 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 468 VQKAVGFSEKIFEYLDRvPNCPKSGSLASL-TLRGSVQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKS 545
Cdd:TIGR01846 421 FQQTGIALERLGDILNS-PTEPRSAGLAALpELRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKS 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 546 TVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLVQEPtMEEITAAAVESGAHGFI 625
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVIHAAKLAGAHDFI 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 626 SELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPeRGsRSVLFITQRLSS 705
Cdd:TIGR01846 577 SELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC-RG-RTVIIIAHRLST 654
|
490 500 510
....*....|....*....|....*....|.
gi 529002597 706 VEQADHILFLEGGTIIEAGTHQQLMTNEGRY 736
Cdd:TIGR01846 655 VRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
368-734 |
9.24e-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: 265.85 E-value: 9.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 368 IEVLSAMPTVRSFANEEGEAQKFRQKLHE-----MMVLnqKEALayavnvwtssLSGMLLK--------VGILYFGGQLV 434
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtMKVL--RVAF----------LSSAVLEffaslsiaLVAVYIGFRLL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 435 tSGSVSSGRLVTFILyqiqftIAVEVLL------SRYPRVQKAVGFSEKIFEYLDRVPNCPKSGSL-ASLTLRGSVQFQD 507
Cdd:COG4988 269 -GGSLTLFAALFVLL------LAPEFFLplrdlgSFYHARANGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELED 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 508 VSFAYPNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQE 587
Cdd:COG4988 342 VSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQN 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 588 PLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:COG4988 420 PYLFAGTIRENLRLGR-PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLD 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 668 DATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEG 734
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
376-739 |
3.14e-79 |
|
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: 265.53 E-value: 3.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 376 TVRSFANEEGEAQKFRQKLHE-----------MMVLNQKEALAYAVnvwtsslsGMllkVGILYFGGQLVTSGSVSSGRL 444
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARyeraavksqtsLALLNFGQALIIAL--------GL---TAMMLMAAQGVVAGTMTVGDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 445 VTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPNCP-KSGSLASLTLRGSVQFQDVSFAYpnRPDVPVLQG 523
Cdd:COG5265 299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVAdAPDAPPLVVGGGEVRFENVSFGY--DPERPILKG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGL 603
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 604 VqEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSqslvER 683
Cdd:COG5265 457 P-DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT----ER 531
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 684 LLYESPERGS--RSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAM 739
Cdd:COG5265 532 AIQAALREVArgRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
501-734 |
2.19e-78 |
|
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: 250.99 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYpnRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQ 580
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGRSFKENIAYGlVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 661 PRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEG 734
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
353-741 |
7.61e-76 |
|
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: 255.46 E-value: 7.61e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 353 AEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYFGGQ 432
Cdd:COG4987 184 GRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 433 LVTSGSVSSGRLVTFILyqiqFTIAV-EVLL------SRYPRVQKAvgfSEKIFEYLDRVPNCPKSGSLASLTLRGSVQF 505
Cdd:COG4987 264 LVAAGALSGPLLALLVL----AALALfEALAplpaaaQHLGRVRAA---ARRLNELLDAPPAVTEPAEPAPAPGGPSLEL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPDvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:COG4987 337 EDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLLFGRSFKENIAYGlVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:COG4987 416 QRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 666 LDDATSALDA-NSQSLVERLLYESPErgsRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMVQ 741
Cdd:COG4987 495 LDEPTEGLDAaTEQALLADLLEALAG---RTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
503-741 |
1.43e-75 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 243.93 E-value: 1.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQV 581
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGRSFKENIAYGlVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 662 RVLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMVQ 741
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
503-742 |
7.65e-75 |
|
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: 242.14 E-value: 7.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIAYGLVqEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRP-DATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 663 VLILDDATSALDANSqslvERLLYESPER--GSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMV 740
Cdd:cd03253 158 ILLLDEATSALDTHT----EREIQAALRDvsKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
..
gi 529002597 741 QA 742
Cdd:cd03253 234 KA 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
191-478 |
3.36e-74 |
|
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: 242.08 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLR 270
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 271 QETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYK 350
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 351 VLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYFG 430
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 529002597 431 GQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
349-744 |
4.99e-71 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 243.33 E-value: 4.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 349 YKVLAEQVQESLaksSQVAIevlsamptVRSFANEEGEAQKFRQ---KL--HEMMVLNQkEALAYAVNVWTSSLSGMllk 423
Cdd:PRK13657 191 YHDLFAHVSDAI---GNVSV--------VQSYNRIEAETQALRDiadNLlaAQMPVLSW-WALASVLNRAASTITML--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 424 vGILYFGGQLVTSGSVSSGRLVTFILYqiqftiaVEVLLSRYPRVqkaVGFSEKI----------FEYLDRVPNCPKSGS 493
Cdd:PRK13657 256 -AILVLGAALVQKGQLRVGEVVAFVGF-------ATLLIGRLDQV---VAFINQVfmaapkleefFEVEDAVPDVRDPPG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 494 LASLT-LRGSVQFQDVSFAYPNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY 572
Cdd:PRK13657 325 AIDLGrVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 573 EHRYLHRQVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVA 652
Cdd:PRK13657 403 TRASLRRNIAVVFQDAGLFNRSIEDNIRVGR-PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLA 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 653 LARALIRKPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
410
....*....|..
gi 529002597 733 EGRYWAMVQAPG 744
Cdd:PRK13657 560 GGRFAALLRAQG 571
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
503-718 |
6.22e-71 |
|
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: 229.19 E-value: 6.22e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIayglvqeptmeeitaaavesgahgfiselsegydtevgeagsqLSGGQRQAVALARALIRKPR 662
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 663 VLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGG 718
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
192-478 |
4.34e-70 |
|
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: 231.43 E-value: 4.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 192 ALVFL--SCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18784 1 AFFFLlaAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWY 349
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 350 KVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYF 429
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 529002597 430 GGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
254-736 |
3.83e-67 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 232.60 E-value: 3.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 254 GRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRG----LCLLGLMLWASPSLTM 329
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 330 ITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEalaya 409
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKM----- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 410 vnVWTSSLSGMLLkvgilyfggQLVTSGSVSsgrlvtFILYQIQF----------TIAV------------EVLLSRYPR 467
Cdd:PRK11176 245 --VSASSISDPII---------QLIASLALA------FVLYAASFpsvmdtltagTITVvfssmialmrplKSLTNVNAQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 468 VQKAVGFSEKIFEYLDRVPNcPKSGSLASLTLRGSVQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTV 547
Cdd:PRK11176 308 FQRGMAACQTLFAILDLEQE-KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 548 AALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHGFISE 627
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINK 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 628 LSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVE 707
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIE 543
|
490 500
....*....|....*....|....*....
gi 529002597 708 QADHILFLEGGTIIEAGTHQQLMTNEGRY 736
Cdd:PRK11176 544 KADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
501-724 |
1.16e-62 |
|
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: 208.98 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQ 580
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 661 PRVLILDDATSALDANS-QSLVERLlyeSPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAG 724
Cdd:cd03245 159 PPILLLDEPTSAMDMNSeERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
233-741 |
6.15e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 215.74 E-value: 6.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 233 VLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIR 312
Cdd:PRK10790 73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVAT----VLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 313 GLCLLGLMLWASPSL-------------TMITLVALPLLFLLPekmgkwykvLAEQVQESLAKSSQVAIEVLSAMPTVrs 379
Cdd:PRK10790 149 SAALIGAMLVAMFSLdwrmalvaimifpAVLVVMVIYQRYSTP---------IVRRVRAYLADINDGFNEVINGMSVI-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 380 faneegeaQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLK-----------VGILYFGGqLVTSGSVSSGRLVTFI 448
Cdd:PRK10790 218 --------QQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 449 LYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRvpncPKS--GSLASLTLRGSVQFQDVSFAYpnRPDVPVLQGLTF 526
Cdd:PRK10790 289 SYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDG----PRQqyGNDDRPLQSGRIDIDNVSFAY--RDDNLVLQNINL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGlvqE 606
Cdd:PRK10790 363 SVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---R 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 607 PTMEEITAAAVES-GAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:PRK10790 440 DISEEQVWQALETvQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL 519
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 686 YESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMVQ 741
Cdd:PRK10790 520 AAV--REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
275-742 |
7.37e-60 |
|
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: 214.99 E-value: 7.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 275 FFQKNQTGEITSRVTDDTSTMSESLSSDLSLL--LWYLIrglcLLGLML-WASPSLTMITLVALPLLFLLPEKMGKWYKV 351
Cdd:TIGR01193 246 FFSTRRTGEIVSRFTDASSIIDALASTILSLFldMWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFNK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 352 LAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQK----FRQKLHEMMVLNQKEALAYAVNVWTSslsgMLLKVGIL 427
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTK----LILNVVIL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 428 YFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFE-YLDRVPNCPKSGSLASLTLRGSVQFQ 506
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYP-NRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:TIGR01193 478 DVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:TIGR01193 555 QEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 666 LDDATSALDA-NSQSLVERLLYESpergSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAMVQA 742
Cdd:TIGR01193 635 LDESTSNLDTiTEKKIVNNLLNLQ----DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
353-730 |
1.54e-55 |
|
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: 199.97 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 353 AEQVQESLAKSSQVaIEVLSAMPTVRsfaneegeaQKFRQKLHEMMVLNqkeALAYAVNVWTSSLS---GMLLKVGILYF 429
Cdd:COG4618 193 ANAFAEAALRNAEV-IEAMGMLPALR---------RRWQRANARALALQ---ARASDRAGGFSALSkflRLLLQSAVLGL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 430 GGQLVTSGSVSSGRLvtfilyqiqftIAVEVLLSR--YPrVQKAVG----FS------EKIFEYLDRVPNCPKSGSLAsl 497
Cdd:COG4618 260 GAYLVIQGEITPGAM-----------IAASILMGRalAP-IEQAIGgwkqFVsarqayRRLNELLAAVPAEPERMPLP-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 498 TLRGSVQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYL 577
Cdd:COG4618 326 RPKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 HRQVAAVGQEPLLFGRSFKENIAygLVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARAL 657
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 658 IRKPRVLILDDATSALDAN-SQSLVERLLyESPERGsRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLM 730
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEgEAALAAAIR-ALKARG-ATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
471-715 |
3.42e-52 |
|
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: 189.81 E-value: 3.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 471 AVGFSEKIFEYLDRVPNcPKSGSLASLTLR-GSVQFQDVSFAYPNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAA 549
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPR-PLAGKAPVTAAPaSSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 550 LLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELS 629
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR-PDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 630 EGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERgsRSVLFITQRLSSVEQA 709
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALA 523
|
....*.
gi 529002597 710 DHILFL 715
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
189-458 |
1.88e-50 |
|
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: 177.84 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNV--TLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQ 266
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVysLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 267 AVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMG 346
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 347 KWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGI 426
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 529002597 427 LYFGGQLVTSGSVSSGRLVTFILYQIQFTIAV 458
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
501-725 |
3.12e-50 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 175.37 E-value: 3.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYpnRPD-VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHR 579
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENIA-YGLVQEptmEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDpFGEYSD---EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
500-741 |
8.27e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 184.26 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 500 RGSVQFQDVSFAYPNRPDvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFIsELSEGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAA-PNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAM 739
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
..
gi 529002597 740 VQ 741
Cdd:PRK11160 571 KQ 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
260-739 |
9.78e-50 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 183.76 E-value: 9.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 260 LQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLM-LWASPSLTMITLVALPLl 338
Cdd:PRK10789 71 LREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPV- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 339 fllpekMGKWYKVLAEQVQESLaKSSQVAI--------EVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAV 410
Cdd:PRK10789 150 ------MAIMIKRYGDQLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDAR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 411 NVWTSSLS-GM--LLKVGilyFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPN 487
Cdd:PRK10789 223 FDPTIYIAiGManLLAIG---GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 488 CpKSGSLASLTLRGSVQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE 567
Cdd:PRK10789 300 V-KDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 568 PLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQ 647
Cdd:PRK10789 378 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGR-PDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQ 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERgsRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQ 727
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534
|
490
....*....|..
gi 529002597 728 QLMTNEGRYWAM 739
Cdd:PRK10789 535 QLAQQSGWYRDM 546
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
503-733 |
3.74e-49 |
|
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: 172.52 E-value: 3.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPL--LFGRSFKENIAYGLVQ----EPTMEEITAAAVEsgAHGfISELSEgydtevgEAGSQLSGGQRQAVALARA 656
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlglpREEIRERVEEALE--LVG-LEHLAD-------RPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
360-731 |
4.04e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 178.70 E-value: 4.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 360 LAKSSQVAIEVLSAMPTVrsfaneeGEAQKFRQKLHEMMVlnQKEALAYAVNVWTSSLSG---MLLKVGILYFGGQLVTS 436
Cdd:TIGR01842 182 LADSALRNAEVIEAMGMM-------GNLTKRWGRFHSKYL--SAQSAASDRAGMLSNLSKyfrIVLQSLVLGLGAYLAID 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 437 GSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPncPKSGSLASLTLRGSVQFQDVSFAYPNrP 516
Cdd:TIGR01842 253 GEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYP--SRDPAMPLPEPEGHLSVENVTIVPPG-G 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFK 596
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVA 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIAYgLVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:TIGR01842 410 ENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 677 SQSLVERLLYESPERGsRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMT 731
Cdd:TIGR01842 489 GEQALANAIKALKARG-ITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
516-739 |
5.85e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.49 E-value: 5.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQG-LTFTLRPGEVTALVGPNGSGKST-VAALLQNLyqPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGR 593
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSlLNALLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAYGLVQePTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PRK11174 438 TLRDNVLLGNPD-ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 674 DANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGRYWAM 739
Cdd:PRK11174 517 DAHSEQLVMQALNA--ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
192-478 |
1.17e-45 |
|
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: 164.82 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 192 ALVFLS--CFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18590 1 AFLFLTlaVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWY 349
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 350 KVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYF 429
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 529002597 430 GGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
521-671 |
2.50e-45 |
|
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: 158.97 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGR-SFKENI 599
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 600 AYGLvqepTMEEITAAAVESGAHGFISELSEGY--DTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
499-741 |
3.93e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 175.22 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 499 LRGSVQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ---------------------- 556
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 557 --------------------------------PTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGLv 604
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK- 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 605 QEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERL 684
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 685 LYESPERGSRSVLFITQRLSSVEQADHILFLEG----GTIIEA-GTHQQLMT-NEGRYWAMVQ 741
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSvQDGVYKKYVK 1463
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
456-732 |
1.04e-43 |
|
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: 165.46 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 456 IAVEVLLSRYPRVQkAVGFSEKIFEY---LDRVPNCPKSGSLASLTLRGS---VQFQDVSFAYPNRP--DVPVLQGLTFT 527
Cdd:COG1123 209 IADRVVVMDDGRIV-EDGPPEEILAApqaLAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGkgGVRAVDDVSLT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 528 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEH---RYLHRQVAAVGQEPL--LFGR-SFKENIAY 601
Cdd:COG1123 288 LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 602 GLVQEPTM--EEITAAavesgahgfISELSE--GYDTEVGEA-GSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:COG1123 368 PLRLHGLLsrAERRER---------VAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVS 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 677 SQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:COG1123 439 VQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
504-735 |
2.04e-43 |
|
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: 156.94 E-value: 2.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLhRQVAA 583
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHGFisELSEGYDTEVGEagsqLSGGQRQAVALARALIRKPR 662
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNEGR 735
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
506-730 |
3.12e-43 |
|
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: 156.89 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAV 584
Cdd:COG1124 5 RNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEPllfgrsfkeniaYGLVqEP--TMEEITAAAVEsgAHGF------ISELSEgydtEVGEAGS-------QLSGGQRQ 649
Cdd:COG1124 85 FQDP------------YASL-HPrhTVDRILAEPLR--IHGLpdreerIAELLE----QVGLPPSfldryphQLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 650 AVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQ 728
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
..
gi 529002597 729 LM 730
Cdd:COG1124 226 LL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
503-724 |
4.67e-43 |
|
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: 155.36 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPD-VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY---EHRYLH 578
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLL-------FGRSFKE--NIAYGLVQEPTMEEITAAAVESGahgfisELSEGYdteVGEAGSQLSGGQRQ 649
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGV------GLPEEV---LNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 650 AVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
504-720 |
2.21e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.05 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY---EHRylhRQ 580
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppEWR---RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGRSFKENIAYGLV---QEPTMEEITAAAVESGahgfiseLSEGY-DTEVgeagSQLSGGQRQAVALARA 656
Cdd:COG4619 76 VAYVPQEPALWGGTVRDNLPFPFQlreRKFDRERALELLERLG-------LPPDIlDKPV----ERLSGGERQRLALIRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFIT------QRLssveqADHILFLEGGTI 720
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVShdpeqiERV-----ADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
503-730 |
3.36e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyEHRYLHRQVA 582
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGR-SFKENI-----AYGLVQEPTMEEITAAAVESGahgfiseLSEGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFG-------LTDAADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLM 730
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
503-719 |
3.88e-42 |
|
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: 152.24 E-value: 3.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDV--PVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLyQPTEGQVlldgeplpkyehrYLHR 579
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENIAYGLVQEPTMEE--ITAAAVESGahgfISELSEGYDTEVGEAGSQLSGGQRQAVALARAL 657
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERYEkvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 658 IRKPRVLILDDATSALDANsqslVERLLYES----PERGSRSVLFITQRLSSVEQADHILFLEGGT 719
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAH----VGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
369-740 |
4.29e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 165.97 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 369 EVLSAMPTVRSFANEEGEAQKFR--QKLHEMMVL--NQKEALAYAVnvwtssLSGMLL---KVGiLYFGGQLVTSGSVSS 441
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNlsEKLYSKYILkaNFMESLHIGM------INGFILasyAFG-FWYGTRIIISDLSNQ 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 442 --------GRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPNCPKSGSLASLTLRGSVQFQDVSFAYP 513
Cdd:PTZ00265 314 qpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYD 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 514 NRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLL-DGEPLPKYEHRYLHRQVAAVGQEPLLFG 592
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 RSFKENIAYGLVQEPTMEEITAAAVESGA--------------------------------------------------- 621
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvs 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 622 -----HGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSV 696
Cdd:PTZ00265 554 kkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 697 LFITQRLSSVEQADHILFL-----------------------------------------------EGGTIIEAGTHQQL 729
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDAL 713
|
490
....*....|..
gi 529002597 730 MTNE-GRYWAMV 740
Cdd:PTZ00265 714 MKNKnGIYYTMI 725
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
503-733 |
4.77e-42 |
|
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: 153.66 E-value: 4.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLL-FGRSFKENIAYG------LVQEPTME--EITAAAVES-GahgfISELSegyDTEVGEagsqLSGGQRQAVA 652
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlgLFGRPSAEdrEAVEEALERtG----LEHLA---DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 653 LARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMT 731
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 529002597 732 NE 733
Cdd:COG1120 228 PE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
504-719 |
6.17e-42 |
|
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: 151.85 E-value: 6.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAA 583
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEP--LLFGRSFKENIAYGLVQ----EPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGGQRQAV 651
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGT 719
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
504-720 |
5.47e-41 |
|
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: 147.75 E-value: 5.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAA 583
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEPLLFGRSFKENIayglvqeptmeeitaaavesgahgfiselsegydtevgeagsqLSGGQRQAVALARALIRKPRV 663
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQADHILFLEGGTI 720
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGA-TRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
191-478 |
5.61e-41 |
|
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: 151.90 E-value: 5.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAF-----TQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVF 265
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIfglslKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 266 QAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKM 345
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 346 GKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVG 425
Cdd:cd18573 162 GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 426 ILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18573 242 VLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
503-722 |
8.94e-41 |
|
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: 148.77 E-value: 8.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNR-PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyehryLHRQV 581
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFG-RSFKENIAYGL-VQEPTMEEITAAAVEsgahgfiselsegYDTEVGEAG------SQLSGGQRQAVAL 653
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLeLQGVPKAEARERAEE-------------LLELVGLSGfenaypHQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLS-SVEQADHILFLEG--GTIIE 722
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
255-703 |
1.18e-40 |
|
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: 156.75 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 255 RVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVA 334
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 335 LPLLFLLPEKMGKWYKVLAEQVQESLAKS-SQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVW 413
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQALARLRGElAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 414 TSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVL---LSRYPRVQKAvgfSEKIFEYLDRVPNCPK 490
Cdd:TIGR02868 243 LTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALpaaAQQLTRVRAA---AERIVEVLDAAGPVAE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 491 S---GSLASLTLRGSVQFQDVSFAYPnrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE 567
Cdd:TIGR02868 320 GsapAAGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 568 PLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIAYGlVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQ 647
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDA-NSQSLVERLLyeSPERGsRSVLFITQRL 703
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAeTADELLEDLL--AALSG-RTVVLITHHL 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
260-744 |
1.69e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 160.91 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 260 LQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTM---SESLSSDLSLLLWYLIRGLCLLGLM----LWASPSLTMITL 332
Cdd:PLN03232 985 LHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIdrnVANLMNMFMNQLWQLLSTFALIGTVstisLWAIMPLLILFY 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 333 VALPllfllpekmgkWYKVLAEQVQ--ESLAKSSQVAI--EVLSAMPTVRSFaneegEAQKFRQKLH-EMMVLNQKEALA 407
Cdd:PLN03232 1065 AAYL-----------YYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY-----KAYDRMAKINgKSMDNNIRFTLA 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 408 -YAVNVWTS----SLSGMLL----KVGILYFGGQLVTSGSVSSGRLVtfILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:PLN03232 1129 nTSSNRWLTirleTLGGVMIwltaTFAVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAENSLNSVERV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 479 FEYLDRVPNCP----KSGSLASLTLRGSVQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN 553
Cdd:PLN03232 1207 GNYIDLPSEATaiieNNRPVSGWPSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 554 LYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENIayglvqEPTMEEITAAAVES--GAH--GFISELS 629
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDADLWEAleRAHikDVIDRNP 1358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 630 EGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQA 709
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDC 1436
|
490 500 510
....*....|....*....|....*....|....*.
gi 529002597 710 DHILFLEGGTIIEAGTHQQLMTNEGR-YWAMVQAPG 744
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHSTG 1472
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
503-724 |
1.71e-40 |
|
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: 146.69 E-value: 1.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRyLHRQVA 582
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIayglvqeptmeeitaaavesgahgfiselsegydtevgeaGSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQADHILFLEGGTIIEAG 724
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
504-719 |
1.33e-39 |
|
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: 143.15 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAA 583
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VgqepllfgrsfkeniayglvqeptmeeitaaavesgahgfiselsegydtevgeagSQLSGGQRQAVALARALIRKPRV 663
Cdd:cd00267 78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQA-DHILFLEGGT 719
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
503-722 |
1.58e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 146.77 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyehryLHRQV 581
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFG-RSFKENIAYGL-VQEPTMEEITAAAVEsgahgFISelsegydtEVGEAG------SQLSGGQRQAVAL 653
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLeLRGVPKAERRERARE-----LLE--------LVGLAGfedaypHQLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 654 ARALIRKPRVLILDDATSALDA----NSQSLVERLLyespERGSRSVLFITqrlSSVEQA----DHILFLEG--GTIIE 722
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDAltreRLQDELLRLW----QETGKTVLFVT---HDVDEAvflaDRVVVLSArpGRIVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
503-732 |
4.82e-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: 151.98 E-value: 4.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT---EGQVLLDGEPLPKYEHRYLHR 579
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPL--LFGRSFKENIAYGL-VQEPTMEEITAAAVESGAHGFISELSEGYDtevgeagSQLSGGQRQAVALARA 656
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALeNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
503-729 |
4.35e-38 |
|
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: 141.55 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTEGQVLLDGEPLPKYEHR-- 575
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 576 YLHRQVAAVGQEPLLFGRSFKENIAYGL-VQEPTMEEITAAAVESGahgfiseLSE-GYDTEVGE--AGSQLSGGQRQAV 651
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrLHGIKLKEELDERVEEA-------LRKaALWDEVKDrlHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFIT------QRLssveqADHILFLEGGTIIEAGT 725
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVThnmqqaARV-----ADRTAFLLNGRLVEFGP 223
|
....
gi 529002597 726 HQQL 729
Cdd:cd03260 224 TEQI 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
503-720 |
6.17e-38 |
|
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: 139.07 E-value: 6.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLhRQVA 582
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGR-SFKENIayglvqeptmeeitaaavesgahgfiselsegydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 662 RVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTI 720
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
506-724 |
1.31e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.34 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QepllfgrsfkeniayglvqepTMEEITaaavesgahgfISELSE-GYDTevgeagsqLSGGQRQAVALARALIRKPRVL 664
Cdd:cd03214 80 Q---------------------ALELLG-----------LAHLADrPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 665 ILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
191-744 |
8.22e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 149.33 E-value: 8.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCF-------GEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEF------AADGIYNSTmgRVH 257
Cdd:TIGR00957 964 LFITFLSIFlfvcnhvSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFgysmavSIGGIQASR--VLH 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 258 SHLqgevFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPL 337
Cdd:TIGR00957 1042 QDL----LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 338 LFLlpekMGKWYKVLAEQVQ--ESLAKSSQVA--IEVLSAMPTVRSFANEEGEAQKFRQKLHEmmvlNQKEALAYAV-NV 412
Cdd:TIGR00957 1118 YFF----VQRFYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVaNR 1189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 413 WtssLSGMLLKVG--ILYFGG--QLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKIFEYLDRVPNC 488
Cdd:TIGR00957 1190 W---LAVRLECVGncIVLFAAlfAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 489 P----KSGSLASLTLRGSVQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVL 563
Cdd:TIGR00957 1267 PwqiqETAPPSGWPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 564 LDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKENI-AYGLVQEptmEEITAAAVESGAHGFISELSEGYDTEVGEAGSQ 642
Cdd:TIGR00957 1345 IDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQYSD---EEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQADHILFLEGGTIIE 722
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGEVAE 1499
|
570 580
....*....|....*....|..
gi 529002597 723 AGTHQQLMTNEGRYWAMVQAPG 744
Cdd:TIGR00957 1500 FGAPSNLLQQRGIFYSMAKDAG 1521
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
503-733 |
1.63e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.53 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLqNLYQPTEGQVLLDGEPLPKYEHRylhrqV 581
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRR-----I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEpLLFGRSF----KENIAYGLVQE--------PTMEEITAAAVES-GAHGFIselsegyDTEVGEagsqLSGGQR 648
Cdd:COG1121 78 GYVPQR-AEVDWDFpitvRDVVLMGRYGRrglfrrpsRADREAVDEALERvGLEDLA-------DRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGtIIEAGTHQ 727
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPE 223
|
....*.
gi 529002597 728 QLMTNE 733
Cdd:COG1121 224 EVLTPE 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
502-729 |
9.42e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 138.36 E-value: 9.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpkyeHRYLH--- 578
Cdd:COG1118 2 SIEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPpre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLLFgR--SFKENIAYGL-VQEPTMEEItAAAVEsgahgfisELSEgydtEVGEAG------SQLSGGQRQ 649
Cdd:COG1118 75 RRVGFVFQHYALF-PhmTVAENIAFGLrVRPPSKAEI-RARVE--------ELLE----LVQLEGladrypSQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 650 AVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFIT-QRLSSVEQADHILFLEGGTIIEAGTHQQ 728
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVThDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
.
gi 529002597 729 L 729
Cdd:COG1118 221 V 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
503-733 |
2.13e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 135.25 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG-EPLPKYEHRYLHRQV 581
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVEsgahgfiselsegydtEVG------EAGSQLSGGQRQ 649
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenlgVPREEMRKRVDEALK----------------LVGmedfrdREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 650 AVALARALIRKPRVLILDDATSALDANSQ----SLVERLlyeSPERGsRSVLFITQRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRkevlETIRKL---NKEEG-ITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*...
gi 529002597 726 HQQLMTNE 733
Cdd:TIGR04520 220 PREIFSQV 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
501-725 |
2.27e-35 |
|
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: 133.31 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAY-PNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHR 579
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENI-AYGlvqEPTMEEITAAavesgahgfiselsegydTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
501-748 |
3.52e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 144.11 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENIayglvqEPTMEEITAAAVES--GAH--GFISELSEGYDTEVGEAGSQLSGGQRQAVALAR 655
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNEGR 735
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
250
....*....|....
gi 529002597 736 YWA-MVQAPGGPGA 748
Cdd:PLN03130 1466 AFSkMVQSTGAANA 1479
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
503-724 |
4.70e-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: 132.26 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEhrylhR 579
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLF-GRSFKENIAYGL-VQEPTMEEITAAAVESGAHGFISELSEGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03259 73 NIGMVFQDYALFpHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYP-------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 658 IRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLS-SVEQADHILFLEGGTIIEAG 724
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
189-471 |
6.18e-35 |
|
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: 134.60 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAV 268
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 269 LRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKW 348
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 349 YKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILY 428
Cdd:cd07346 163 IRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 529002597 429 FGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKA 471
Cdd:cd07346 243 YGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQA 285
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
503-719 |
1.32e-34 |
|
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: 130.00 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE--HRYLHRQ 580
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLF-GRSFKENIAYGlvqeptmeeitaaavesgahgfiselsegydtevgeagsqLSGGQRQAVALARALIR 659
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGT 719
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
190-478 |
1.45e-34 |
|
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: 133.53 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVfLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQN-------VTLMSVLTIaSAVLEFAADGIYNSTMGRVHSHLQG 262
Cdd:cd18780 2 TIALL-VSSGTNLALPYFFGQVIDAVTNHSGSGGEEALralnqavLILLGVVLI-GSIATFLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 EVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLP 342
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 343 EKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLL 422
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 423 KVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18780 240 IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
503-731 |
5.00e-34 |
|
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: 130.31 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPK---YEHRYLHR 579
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGR-SFKENIAYGLVQ-----EPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGGQ 647
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREhtrlsEEEIREIVLEKLE----------------AVGLRGaedlypAELSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTH 726
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
....*
gi 529002597 727 QQLMT 731
Cdd:cd03261 222 EELRA 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
503-732 |
5.66e-34 |
|
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: 130.01 E-value: 5.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEHRYLH 578
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQE-PLLFGRSFKENIAYGL-VQEPTMEEITAAavesgahgfISELSEgydtEVGEAG------SQLSGGQRQA 650
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVALPLeIAGVPKAEIEER---------VLELLE----LVGLEDkadaypAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 529002597 730 MTN 732
Cdd:cd03258 229 FAN 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
503-724 |
1.60e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.25 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLY---QPTEGQVLLDGEPLPKYEHR---Y 576
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 LHRQVAAVGQE-PLLFGRSFKENIAYGL-VQEPTMEEITAAAVESgahgfiseLSegydtEVGEAG------SQLSGGQR 648
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALPLrVTGKSRKEIRRRVREV--------LD-----LVGLSDkakalpHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 649 QAVALARALIRKPRVLILDDATSALD-ANSQSLVeRLLYESPERGSrSVLFITQRLSSVEQADH-ILFLEGGTIIEAG 724
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDpETSWEIM-ELLEEINRRGT-TVLIATHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
503-720 |
3.06e-33 |
|
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: 127.22 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPD-VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR----YL 577
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 HRQVAAVGQEP-LLFGRSFKENIAYGL----VQEPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGG 646
Cdd:cd03255 81 RRHIGFVFQSFnLLPDLTALENVELPLllagVPKKERRERAEELLE----------------RVGLGDrlnhypSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTI 720
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
503-685 |
4.96e-33 |
|
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: 126.44 E-value: 4.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTEGQVLLDGEPLPKYEHRYlHR 579
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGR-SFKENIA-----YGLvqEPTMEEITAAAVESGAHGFIselsegyDTEVGeagsQLSGGQRQAVAL 653
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRfwaalYGL--RADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
503-733 |
2.06e-32 |
|
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: 125.86 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY---EHRYLHR 579
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGrSF--KENIAYGLVQ-----EPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGG 646
Cdd:COG1127 83 RIGMLFQGGALFD-SLtvFENVAFPLREhtdlsEAEIRELVLEKLE----------------LVGLPGaadkmpSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYE-SPERGSRSVLfITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVV-VTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*....
gi 529002597 725 THQQLMTNE 733
Cdd:COG1127 225 TPEELLASD 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
516-712 |
4.45e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.91 E-value: 4.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PkyeHRYLHRQVAAVGQEPLLF 591
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsP---RDAQAAGIAIIHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 -GRSFKENIA-------YGLVQEPTMEEITAAAVES-GAHgfISElsegyDTEVGEagsqLSGGQRQAVALARALIRKPR 662
Cdd:COG1129 92 pNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--IDP-----DTPVGD----LSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 663 VLILDDATSALDAN-SQSL---VERLlyesPERGsRSVLFITQRLSSVEQ-ADHI 712
Cdd:COG1129 161 VLILDEPTASLTEReVERLfriIRRL----KAQG-VAIIYISHRLDEVFEiADRV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
502-729 |
7.16e-32 |
|
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: 123.99 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNrpdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylHRQV 581
Cdd:cd03296 2 SIEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHGFI-----SELSEGYDtevgeagSQLSGGQRQAVALAR 655
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
503-722 |
1.01e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.23 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPN-RPDVPVLQGLTFTLRPGEVTALVGPNGSGKST---VAALLQnlyQPTEGQVLLDGEPLpkyeHRYLH 578
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDI----SSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAA--------VGQEPLLFGR-SFKENIAYGLVqeptMEEITAAAVESGAHgfisELSEgydtEVGEAG------SQL 643
Cdd:COG1136 78 RELARlrrrhigfVFQFFNLLPElTALENVALPLL----LAGVSRKERRERAR----ELLE----RVGLGDrldhrpSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIE 722
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
504-718 |
1.63e-31 |
|
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: 122.26 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylhrqVAA 583
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEpLLFGRSF----KENIAYGLVQEPtmeeitaaavesgahGFISELSEGYDTEVGEA----G---------SQLSGG 646
Cdd:cd03235 73 VPQR-RSIDRDFpisvRDVVLMGLYGHK---------------GLFRRLSKADKAKVDEAlervGlseladrqiGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGG 718
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
503-733 |
1.99e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEP--LLFGRSFKENIAYGL----VQEPTMEE-ITAAAVESGAHGFISELSEgydtevgeagsQLSGGQRQAVALAR 655
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLenkkVPPKKMKDiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
502-687 |
3.93e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.21 E-value: 3.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEhrylh 578
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtgLPPEK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLLFG-RSFKENIAYGL----VQEPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGGQ 647
Cdd:COG3842 77 RNVGMVFQDYALFPhLTVAENVAFGLrmrgVPKAEIRARVAELLE----------------LVGLEGladrypHQLSGGQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANsqsLVERLLYE 687
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAK---LREEMREE 177
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
507-721 |
9.10e-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: 120.05 E-value: 9.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYPNRPDVpvLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylhRQVAAVGQ 586
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 587 EP--LLFGRSFKENIAYGLVQEPTMEEITAAAVESGAhgfISELSEGYDTEvgeagsqLSGGQRQAVALARALIRKPRVL 664
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLD---LYALKERHPLS-------LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 665 ILDDATSALDANSQSLVERLLYESPERGsRSVLFIT---QRLSSVeqADHILFLEGGTII 721
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQG-KAVIVIThdyEFLAKV--CDRVLLLANGAIV 205
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
190-478 |
9.92e-31 |
|
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: 122.21 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVFLSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18576 2 LILLLLSSAIG-LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRGLCLL----GLMLWASPSLTMITLVALPLLFLLPEKM 345
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAE----FLRQILTLiggvVLLFFISWKLTLLMLATVPVVVLVAVLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 346 GKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVG 425
Cdd:cd18576 157 GRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 426 ILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18576 237 VLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
503-732 |
1.37e-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: 120.48 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLF-GRSFKENIayGLVqePTMEEITAAAVESGAhgfiSELSEGYDTEVGEAG----SQLSGGQRQAVALARAL 657
Cdd:cd03295 79 YVIQQIGLFpHMTVEENI--ALV--PKLLKWPKEKIRERA----DELLALVGLDPAEFAdrypHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 658 IRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRL-SSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
506-729 |
2.15e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.28 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPDvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:PRK13635 9 EHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVES-GAHGFIselsegyDTEvgeaGSQLSGGQRQAVALARALI 658
Cdd:PRK13635 88 QNPdnQFVGATVQDDVAFGLenigVPREEMVERVDQALRQvGMEDFL-------NRE----PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
507-733 |
7.53e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 119.41 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpKYEHRYL---HRQVAA 583
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEP--LLFGRSFKENIAYG-----LVQEPTMEEITAAAVESGAhgfiselsEGYDTevgEAGSQLSGGQRQAVALARA 656
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVGM--------EGFEN---KPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVE-QADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGI-TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
517-732 |
1.82e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 116.76 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE-HRYLHRQVAAVGQEPLLFGR-S 594
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENI---AYGLVQ---EPTMEEITAAavesgahgFiSELSEGYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:cd03224 92 VEENLllgAYARRRakrKARLERVYEL--------F-PRLKERRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 669 ATSALdanSQSLVERL---LYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:cd03224 159 PSEGL---APKIVEEIfeaIRELRDEG-VTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
517-732 |
2.21e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.02 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEHRYLHRQVAAVGQEPLLFG-R 593
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAYGLVQ---EPTmEEITAAAVEsgahgfisELsegydTEVGEAG------SQLSGGQRQAVALARALIRKPRVL 664
Cdd:COG1126 93 TVLENVTLAPIKvkkMSK-AEAEERAME--------LL-----ERVGLADkadaypAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 665 ILDDATSALDansqslverllyesPERgSRSVLFITQRLSS-------V--------EQADHILFLEGGTIIEAGTHQQL 729
Cdd:COG1126 159 LFDEPTSALD--------------PEL-VGEVLDVMRDLAKegmtmvvVthemgfarEVADRVVFMDGGRIVEEGPPEEF 223
|
...
gi 529002597 730 MTN 732
Cdd:COG1126 224 FEN 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
503-729 |
2.45e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQV 581
Cdd:PRK13648 8 IVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVESgahgfiSELSEGYDTEvgeaGSQLSGGQRQAVALAR 655
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLenhaVPYDEMHRRVSEALKQ------VDMLERADYE----PNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
503-733 |
2.75e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.89 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEP--LLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHGFiselsEGYDTEVGEAgSQLSGGQRQAVALARALIRK 660
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAV-----NMLDFKTREP-ARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 661 PRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTII-EAGTHQQLMTNE 733
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIkEAAPSELFATSE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
506-732 |
5.63e-29 |
|
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: 122.10 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNR--------PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQnLyQPTEGQVLLDGEPLPKYEH-- 574
Cdd:COG4172 279 RDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFDGQDLDGLSRra 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 575 -RYLHRQVAAVGQEPllFG-----RSFKENIAYGL-VQEPTM--EEITAAAVESgahgfiseLsegydTEVG-EAGS--- 641
Cdd:COG4172 357 lRPLRRRMQVVFQDP--FGslsprMTVGQIIAEGLrVHGPGLsaAERRARVAEA--------L-----EEVGlDPAArhr 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 642 ---QLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEG 717
Cdd:COG4172 422 yphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKD 501
|
250
....*....|....*
gi 529002597 718 GTIIEAGTHQQLMTN 732
Cdd:COG4172 502 GKVVEQGPTEQVFDA 516
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
503-720 |
5.88e-29 |
|
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: 114.93 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEHRYLHRQ 580
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFG-RSFKENIAYGLVQEPTMEEITAaavesgahgfiSELSEGYDTEVGEAG------SQLSGGQRQAVAL 653
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEA-----------EERALELLEKVGLADkadaypAQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLS-SVEQADHILFLEGGTI 720
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
508-732 |
6.32e-29 |
|
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: 117.85 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 508 VSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQVLLDGEPLPKYEHR----YLHRQ 580
Cdd:COG0444 9 VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKelrkIRGRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLlfgRSFkeNiayglvqePTM--EEITAAAVEsgAHGFISElSEGYD------TEVG--EAGS-------QL 643
Cdd:COG0444 88 IQMIFQDPM---TSL--N--------PVMtvGDQIAEPLR--IHGGLSK-AEAREraiellERVGlpDPERrldryphEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYE-SPERGSrSVLFITQRLSSVEQ-ADHILFLEGGTII 721
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGL-AILFITHDLGVVAEiADRVAVMYAGRIV 230
|
250
....*....|.
gi 529002597 722 EAGTHQQLMTN 732
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
503-733 |
7.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 7.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVES-GAHGFIselsegyDTEvgeaGSQLSGGQRQAVA 652
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLenraVPRPEMIKIVRDVLADvGMLDYI-------DSE----PANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 653 LARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 529002597 733 E 733
Cdd:PRK13640 234 V 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
516-721 |
8.57e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.91 E-value: 8.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPkyehrylhrqvaavgqepllfGRSF 595
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYGLvqeptmeeitaAAVesgahgfiselsegydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03216 70 RDARRAGI-----------AMV-----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 529002597 676 NSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTII 721
Cdd:cd03216 116 AEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
518-732 |
5.34e-28 |
|
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: 113.89 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYL----HRQVAAVGQEPLLF-G 592
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 RSFKENIAYGL-VQEPTMEEITAAAVES----GAHGFISELSegydtevgeagSQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:cd03294 117 RTVLENVAFGLeVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 668 DATSALD----ANSQSLVERLLYESPergsRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:cd03294 186 EAFSALDplirREMQDELLRLQAELQ----KTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
506-733 |
6.51e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.19 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLL-FGRSFKENIAYG----------LVQEPtmEEITAAAVESGAhgfISELSEGYDTEvgeagsqLSGGQRQAVALA 654
Cdd:PRK11231 83 QHHLTpEGITVRELVAYGrspwlslwgrLSAED--NARVNQAMEQTR---INHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 655 RALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFItqrLSSVEQA----DHILFLEGGTIIEAGTHQQLM 730
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQG-KTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTPEEVM 226
|
...
gi 529002597 731 TNE 733
Cdd:PRK11231 227 TPG 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
506-733 |
6.82e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:COG4559 5 ENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QE-PLLFGRSFKENIAYGLVQEPTM----EEITAAAVE-SGAHGFiselsegydtevgeAG---SQLSGGQRQAVALARA 656
Cdd:COG4559 82 QHsSLAFPFTVEEVVALGRAPHGSSaaqdRQIVREALAlVGLAHL--------------AGrsyQTLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 657 LI-------RKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQ 728
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGG-GVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEE 226
|
....*
gi 529002597 729 LMTNE 733
Cdd:COG4559 227 VLTDE 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
503-732 |
6.90e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.88 E-value: 6.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEHRYLHRQ 580
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGR-SFKENIAYGLVQeptMEEITAAAVESGAHGFISELseGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLR---VRGASKEEAEKQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLfITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
506-733 |
2.05e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:PRK13548 6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLL-FGRSFKENIAYGL-----VQEPTMEEITAAAVESGAHGFiselsegydtevgeAGS---QLSGGQRQAVALARA 656
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 657 LIR------KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228
|
....
gi 529002597 730 MTNE 733
Cdd:PRK13548 229 LTPE 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
504-733 |
4.00e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpvlqgLTFTL--RPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEhrylh 578
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLLFGR-SFKENIAYGLvqEPTM-------EEITAAAVESGAHGFISELSEgydtevgeagsQLSGGQRQA 650
Cdd:COG3840 71 RPVSMLFQENNLFPHlTVAQNIGLGL--RPGLkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALD----ANSQSLVERLlyeSPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDEL---CRERG-LTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
....*...
gi 529002597 726 HQQLMTNE 733
Cdd:COG3840 214 TAALLDGE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
504-685 |
4.15e-27 |
|
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: 110.35 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLH---RQ 580
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGR-SFKENIAYGLVqeptmeeitaaavesGAHGFISELSEGYDTE-----------VGEAG------SQ 642
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRL---------------GRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 529002597 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
503-675 |
1.23e-26 |
|
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: 108.86 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEhrylhR 579
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHgfISELSEGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALD--LVQLEGYANRKP----SQLSGGQQQRVAIARALV 146
|
170
....*....|....*..
gi 529002597 659 RKPRVLILDDATSALDA 675
Cdd:cd03300 147 NEPKVLLLDEPLGALDL 163
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
503-725 |
1.24e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 111.71 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEHRYLH 578
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEP-LLFGRSFKENIAYGL-VQEPTMEEITAAAVEsgahgfISELsegydteVGEAG------SQLSGGQRQA 650
Cdd:COG1135 82 RKIGMIFQHFnLLSSRTVAENVALPLeIAGVPKAEIRKRVAE------LLEL-------VGLSDkadaypSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 651 VALARALIRKPRVLILDDATSALD-ANSQSLVErLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDpETTRSILD-LLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
503-733 |
1.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.89 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYpnRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEP--LLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHGF-ISELSEgydtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLgLEELRD-------RVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
503-729 |
2.14e-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: 107.59 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpKYEHRYLHRQVA 582
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGR-SFKENIAY-----GLVQEPTMEEitaaaVESGAHGFisELSEGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEE-----VELLLRVL--GLTDKANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
501-748 |
2.48e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.03 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYpnRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGRSFKENIAYGLvqEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFL--EASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 660 KPRVLIL-DDATS----ALDANSQSLVERLLyesperGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL-MTNE 733
Cdd:PTZ00243 1463 KGSGFILmDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQ 1536
|
250
....*....|....*
gi 529002597 734 GRYWAMVQAPGGPGA 748
Cdd:PTZ00243 1537 SIFHSMVEALGRSEA 1551
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
526-724 |
2.88e-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: 107.38 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 526 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE-------HRylhRQVAAVGQEPLLFGR 593
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlppQQ---RKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 -SFKENIAYGLVQEPTMEEITAAAVESGAHGfISELSEGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 673 LDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
503-720 |
2.99e-26 |
|
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: 107.11 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR---YLHR 579
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQE-PLLFGRSFKENIAYGL--VQEPTME---EITAAAVESGAHGFISELSEgydtevgeagsQLSGGQRQAVAL 653
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALevTGVPPREirkRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQADH-ILFLEGGTI 720
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGT-TVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
517-725 |
3.24e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.43 E-value: 3.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPK-------Y--EHRYLHRQVaAVGQE 587
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigYlpEERGLYPKM-KVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 588 PLLFGRsFKeniayGLvqeptmeeiTAAAVESGAHGFIS--ELSEGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLI 665
Cdd:COG4152 92 LVYLAR-LK-----GL---------SKAEAKRRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKG-TTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
506-732 |
3.83e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.20 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTEGQVLLDGEPL--PK---Y 572
Cdd:COG1117 15 RNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILLDGEDIydPDvdvV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 573 EHRylhRQVAAVGQEPLLFGRSFKENIAYGL-VQEPTMEEITAAAVES---GAHgfiseLsegYDtEV----GEAGSQLS 644
Cdd:COG1117 89 ELR---RRVGMVFQKPNPFPKSIYDNVAYGLrLHGIKSKSELDEIVEEslrKAA-----L---WD-EVkdrlKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSsveQA----DHILFLEGGTI 720
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE--LKKDYTIVIVTHNMQ---QAarvsDYTAFFYLGEL 231
|
250
....*....|..
gi 529002597 721 IEAGTHQQLMTN 732
Cdd:COG1117 232 VEFGPTEQIFTN 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
517-723 |
4.01e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.11 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFK 596
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIAYGLV---QEPTMEEITAAAVESGahgfiseLSEgydTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PRK10247 99 DNLIFPWQirnQQPDPAIFLDDLERFA-------LPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 529002597 674 DANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLE--GGTIIEA 723
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQphAGEMQEA 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
520-733 |
4.14e-26 |
|
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: 107.52 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY-EHRYLHRQVAAVGQEPLLFGR-SFKE 597
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 598 NIAYGlVQEPTMEEITAAAVESGAHGFISE---------LSEGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:cd03219 95 NVMVA-AQARTGSGLLLARARREEREARERaeellervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 669 ATSAL-DANSQSLVERLLyESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:cd03219 170 PAAGLnPEETEELAELIR-ELRERG-ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
515-722 |
5.04e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 108.24 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY---EHRYLHRQVAAVGQEPLlf 591
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSI-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 G-----RSFKENIAyglvqEPtMEEITAAAvESGAHGFISELSEGYDTEVGEAG---SQLSGGQRQAVALARALIRKPRV 663
Cdd:PRK10419 100 SavnprKTVREIIR-----EP-LRHLLSLD-KAERLARASEMLRAVDLDDSVLDkrpPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIE 722
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
503-732 |
5.58e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.15 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG----EPLPKYEHRYLh 578
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 rqVAAVGQEP--LLFGRSFKENIAYG---LVQEPTmeeitaaavesgahgfisELSEGYDTEVGEAG---------SQLS 644
Cdd:PRK13644 79 --VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPI------------------EIRKRVDRALAEIGlekyrhrspKTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQADHILFLEGGTIIEAG 724
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
....*...
gi 529002597 725 THQQLMTN 732
Cdd:PRK13644 218 EPENVLSD 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
501-675 |
6.15e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.78 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PKyehry 576
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlpPK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 lHRQVAAVGQEPLLF-GRSFKENIAYGL-VQEPTMEEItaaavesgahgfiselsegyDTEVGEAG-------------S 641
Cdd:COG3839 74 -DRNIAMVFQSYALYpHMTVYENIAFPLkLRKVPKAEI--------------------DRRVREAAellgledlldrkpK 132
|
170 180 190
....*....|....*....|....*....|....
gi 529002597 642 QLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
503-675 |
9.89e-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: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEhrylhR 579
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHGF-ISELSEGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELLqIEHLLDRKP-------KQLSGGQRQRVALGRAI 145
|
170
....*....|....*...
gi 529002597 658 IRKPRVLILDDATSALDA 675
Cdd:cd03301 146 VREPKVFLMDEPLSNLDA 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
521-732 |
1.06e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.67 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEHRYLHRQVAAVGQEPllfgrsfke 597
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 598 niaYG-LVQEPTMEEITAAAVEsgAHGFISElsEGYDTEVGEAGS--------------QLSGGQRQAVALARALIRKPR 662
Cdd:COG4608 105 ---YAsLNPRMTVGDIIAEPLR--IHGLASK--AERRERVAELLElvglrpehadryphEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
499-733 |
1.15e-25 |
|
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: 106.92 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 499 LRGSVQFQDVSFAYPNRPDvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLH 578
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLLFGRSFKENIayglvqEP----TMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNL------DPeckcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 655 RALIRKPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
520-731 |
1.66e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.34 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPTEGQVLLDGEPLPKYEHRYL---HRQVAAVGQEP--LLFGR 593
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 -SFKENIAYGL-VQEPTMeeiTAAAVESGAhgfISELSE-GYDTEVGEA-GSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK15134 379 lNVLQIIEEGLrVHQPTL---SAAQREQQV---IAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 670 TSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADH-ILFLEGGTIIEAGTHQQLMT 731
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHqVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
503-724 |
2.12e-25 |
|
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: 104.67 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP-----------LPk 571
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPldiaarnrigyLP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 572 yEHRYLHRQVAAvgQEPLLFGRSFKeniayGLvqepTMEEItAAAVESGAHGFisELSEGYDTEVgeagSQLSGGQRQAV 651
Cdd:cd03269 77 -EERGLYPKMKV--IDQLVYLAQLK-----GL----KKEEA-RRRIDEWLERL--ELSEYANKRV----EELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
520-725 |
3.18e-25 |
|
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: 104.73 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEhrylhRQVAAVGQEPLLFGR-SF 595
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYGL-VQEPTMEEITAAAVESGAHGFISELSEGYDTevgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:cd03299 89 YKNIAYGLkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 529002597 675 ANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
520-729 |
5.07e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.11 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpkyEHRYL-HRQVAAVGQEPLLFGR-SFKE 597
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIqQRDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 598 NIAYGL-VQEPTMEEITAAAVESGAhgfISELSEGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:PRK11432 98 NVGYGLkMLGVPKEERKQRVKEALE---LVDLAGFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 677 -SQSLVERlLYESPERGSRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK11432 171 lRRSMREK-IRELQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
517-733 |
5.26e-25 |
|
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: 104.29 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE-HRYLHRQVAAVGQEPLLFGR-S 594
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENIayglvqeptmeeITAAAVESGAHGFISELSEGYDT--EVGE----AGSQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:COG0410 95 VEENL------------LLGAYARRDRAEVRADLERVYELfpRLKErrrqRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 669 ATSALdanSQSLVERL---LYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:COG0410 163 PSLGL---APLIVEEIfeiIRRLNREG-VTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
502-724 |
5.54e-25 |
|
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: 103.01 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNRP---DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQVLLDGEPLPKYEHRy 576
Cdd:cd03213 3 TLSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 lhRQVAAVGQEPLLFGRSfkeniaygLVQEpTMEeitaaavesgahgFISELSegydtevgeagsQLSGGQRQAVALARA 656
Cdd:cd03213 82 --KIIGYVPQDDILHPTL--------TVRE-TLM-------------FAAKLR------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSS--VEQADHILFLEGGTIIEAG 724
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
504-733 |
6.89e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 104.87 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAA 583
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQE-PLLFGRSFKENIAYGLV-------------QEPTMEEITAAAVESGAHGFIselsegydtevgeagSQLSGGQRQ 649
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVAIGRYpwhgalgrfgaadREKVEEAISLVGLKPLAHRLV---------------DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 650 AVALARALIRKPRVLILDDATSALDANSQ----SLVERLlyeSPERGsrsvLFITQRLSSVEQA----DHILFLEGGTII 721
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQvdvlALVHRL---SQERG----LTVIAVLHDINMAarycDYLVALRGGEMI 227
|
250
....*....|..
gi 529002597 722 EAGTHQQLMTNE 733
Cdd:PRK10575 228 AQGTPAELMRGE 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
504-715 |
9.70e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPN-RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEhrylhRQ 580
Cdd:COG4525 5 TVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGAD-----RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VaaVGQ-EPLLFGRSFKENIAYGLvqepTMEEITAAAVESGAHGFISElsegydteVGEAG------SQLSGGQRQAVAL 653
Cdd:COG4525 80 V--VFQkDALLPWLNVLDNVAFGL----RLRGVPKAERRARAEELLAL--------VGLADfarrriWQLSGGMRQRVGI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQrlsSVEQAdhiLFL 715
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH---SVEEA---LFL 201
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
503-725 |
1.55e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 105.65 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYP-NRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEHRYLH 578
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQE-PLLFGRSFKENIAYGL-VQEPTMEEITAAavesgahgfISELSEgydtEVGEAG------SQLSGGQRQA 650
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLeLAGTPKAEIKAR---------VTELLE----LVGLSDkadrypAQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 651 VALARALIRKPRVLILDDATSALD-ANSQSLVErLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
502-732 |
1.67e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.58 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQVLLDGEPLpkYEHRY 576
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNI--YERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 ----LHRQVAAVGQEPLLFGRSFKENIAYGLV---QEPTME--EITAAAVESgahgfiSELSEGYDTEVGEAGSQLSGGQ 647
Cdd:PRK14258 82 nlnrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgWRPKLEidDIVESALKD------ADLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEG-----GTII 721
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLV 235
|
250
....*....|.
gi 529002597 722 EAGTHQQLMTN 732
Cdd:PRK14258 236 EFGLTKKIFNS 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
490-736 |
3.81e-24 |
|
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: 108.88 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 490 KSGSLASLTLRGSvqfqdvSFAYPnRPDVPVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLyQPTEGQVLLDGep 568
Cdd:TIGR00957 630 KPGEGNSITVHNA------TFTWA-RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 569 lpkyehrylhrQVAAVGQEPLLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHgfISELSEGYDTEVGEAGSQLSGGQR 648
Cdd:TIGR00957 700 -----------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPD--LEILPSGDRTEIGEKGVNLSGGQK 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDAN-SQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQ 727
Cdd:TIGR00957 767 QRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQ 846
|
....*....
gi 529002597 728 QLMTNEGRY 736
Cdd:TIGR00957 847 ELLQRDGAF 855
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
190-478 |
3.94e-24 |
|
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: 102.95 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVFLSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAAdgIYN-STMG-RVHSHLQGEVFQA 267
Cdd:cd18575 2 LIALLIAAAAT-LALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR--FYLvSWLGeRVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 268 VLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGK 347
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 348 WYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGIL 427
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 529002597 428 YFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18575 239 WLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
507-733 |
4.21e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAypnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQ 586
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 587 E-PLLFGRSFKENIAYG----LVQEPTMEEITAAAVESGAHgfiselSEGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK09536 85 DtSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAME------RTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 662 RVLILDDATSALDANSQ----SLVERLLyespERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK09536 159 PVLLLDEPTASLDINHQvrtlELVRRLV----DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
503-724 |
6.12e-24 |
|
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: 100.26 E-value: 6.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpvlqgLTF--TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylHRQ 580
Cdd:cd03298 1 VRLDKIRFSYGEQP-------MHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGR-SFKENIAYGLV-----QEPTMEEITAAAVESGAHGFISELSEgydtevgeagsQLSGGQRQAVALA 654
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 655 RALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
503-729 |
6.17e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVEsgahgfISELSEGYDTEvgeaGSQLSGGQRQAVALARA 656
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLenkgIPHEEMKERVNEALE------LVGMQDFKERE----PARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
518-733 |
7.96e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.90 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PKYEHR---YLhrqvaaVGQEPLL 590
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlgiYL------VPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 F-GRSFKENIAYGLVQEP-TMEEITAaavesgahgFISELSEGYDTEVgEAGSqLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK15439 98 FpNLSVKENILFGLPKRQaSMQKMKQ---------LLAALGCQLDLDS-SAGS-LEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 669 ATSALdanSQSLVERLLYESPERGSRSV--LFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK15439 167 PTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
489-730 |
1.05e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 489 PKSGSLASLtlrgSVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP 568
Cdd:PRK13536 32 SIPGSMSTV----AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 569 LPKyEHRYLHRQVAAVGQ-----------EPLL-FGRSFKENIAyglvqepTMEEITAAAVEsgahgfISELSEGYDTEV 636
Cdd:PRK13536 105 VPA-RARLARARIGVVPQfdnldleftvrENLLvFGRYFGMSTR-------EIEAVIPSLLE------FARLESKADARV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 637 geagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFL 715
Cdd:PRK13536 171 ----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERlCDRLCVL 245
|
250
....*....|....*
gi 529002597 716 EGGTIIEAGTHQQLM 730
Cdd:PRK13536 246 EAGRKIAEGRPHALI 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
517-732 |
1.08e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.76 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEP-LL 590
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 FGRSFKENIAYGLV------QEPTMEEITAAAVESgahgfiSELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK14247 95 PNLSIFENVALGLKlnrlvkSKKELQERVRWALEK------AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 665 ILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
526-732 |
2.29e-23 |
|
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: 102.49 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---------LPKyeHRylhRQVAAVGQEPLLFG-RSF 595
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargifLPP--HR---RRIGYVFQEARLFPhLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYGLVQEPTMEeiTAAAVESgahgfISELsegydteVGEAG------SQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:COG4148 95 RGNLLYGRKRAPRAE--RRISFDE-----VVEL-------LGIGHlldrrpATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 670 TSALDANSQS----LVERLlyesPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:COG4148 161 LAALDLARKAeilpYLERL----RDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
503-724 |
2.94e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.42 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEhRYLHRQVA 582
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLF----GRSFKENIAyglvqepTMEEITAAAVESGAHGFISE--LSEGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:cd03264 76 YLPQEFGVYpnftVREFLDYIA-------WLKGIPSKEVKARVDEVLELvnLGDRAKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
518-733 |
3.41e-23 |
|
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: 99.73 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PkyehrylhRQVAAVG-----QEP 588
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpP--------HRIARLGiartfQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 LLF-----------------GRSFKENIAYGLVQEPTMEEITAAAVEsgAHGFIsELSEGYDTEVGEagsqLSGGQRQAV 651
Cdd:COG0411 89 RLFpeltvlenvlvaaharlGRGLLAALLRLPRARREEREARERAEE--LLERV-GLADRADEPAGN----LSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 652 ALARALIRKPRVLILDDATSALDAN-SQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEeTEELAELIRRLRDERG-ITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEV 240
|
....
gi 529002597 730 MTNE 733
Cdd:COG0411 241 RADP 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
255-741 |
3.41e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.83 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 255 RVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSEslssdlslllwylirgLCLLGLMLWASPSLTMITLVA 334
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQ----------------IAEQLHGLWSAPFRIIVSMVL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 335 LPLLFLLPEKMGKWYKVLAEQVQ------------ESLAKSSQ-VAI--EVLSAMPTVRSFANEEGEAQKFRQKLHEMMV 399
Cdd:PLN03232 435 LYQQLGVASLFGSLILFLLIPLQtlivrkmrkltkEGLQWTDKrVGIinEILASMDTVKCYAWEKSFESRIQGIRNEELS 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 400 LNQKEALAYAVNVWTssLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFI-LYQI-QFTIA-VEVLLSRYPRVQKAVGFSE 476
Cdd:PLN03232 515 WFRKAQLLSAFNSFI--LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLsLFAVlRSPLNmLPNLLSQVVNANVSLQRIE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 477 KIFEYLDRV--PNCPKSGSLASLTLRGSvqfqdvSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQN 553
Cdd:PLN03232 593 ELLLSEERIlaQNPPLQPGAPAISIKNG------YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGE 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 554 LYQPTEGQVLLDGeplpkyehrylhrQVAAVGQEPLLFGRSFKENIAYGLVQEPtmeEITAAAVESGAHGFISELSEGYD 633
Cdd:PLN03232 667 LSHAETSSVVIRG-------------SVAYVPQVSWIFNATVRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRD 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 634 -TEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLfITQRLSSVEQADHI 712
Cdd:PLN03232 731 lTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVL-VTNQLHFLPLMDRI 809
|
490 500 510
....*....|....*....|....*....|....*....
gi 529002597 713 LFLEGGTIIEAGT----------HQQLMTNEGRYWAMVQ 741
Cdd:PLN03232 810 ILVSEGMIKEEGTfaelsksgslFKKLMENAGKMDATQE 848
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
503-732 |
3.96e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTEGQVLLDGEPL--PKY 572
Cdd:PRK14239 6 LQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIysPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 573 EHRYLHRQVAAVGQEPLLFGRSFKENIAYGL-VQEPTMEEITAAAVESGAHG--FISELSEG-YDTEVGeagsqLSGGQR 648
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrLKGIKDKQVLDEAVEKSLKGasIWDEVKDRlHDSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQrlsSVEQA----DHILFLEGGTIIEAG 724
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTR---SMQQAsrisDRTGFFLDGDLIEYN 229
|
....*...
gi 529002597 725 THQQLMTN 732
Cdd:PRK14239 230 DTKQMFMN 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
503-724 |
3.99e-23 |
|
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: 98.06 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYlhRQVA 582
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFG-RSFKENIAYGLVQEPTMEEITAAAVEsgahgfISELSEGYDTEVGeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLD------VVGLKDSAKKKVK----GFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 662 RVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
516-715 |
4.10e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 97.30 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLH---------RQVAAVGq 586
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpdslpltvRDLVAMG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 587 eplLFGRSfkeniayGLVQEPTME---EITAAAVESGAHGFiselsegydteVGEAGSQLSGGQRQAVALARALIRKPRV 663
Cdd:NF040873 82 ---RWARR-------GLWRRLTRDdraAVDDALERVGLADL-----------AGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQADHILFL 715
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
520-729 |
4.14e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylHRQVAAVGQEPLLFGR-SFKEN 598
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYGLVQEPTMEEITAAAVESGAHGFI-----SELSEGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 674 DANSQSLVERLLYESPERGSRSVLFITQ-RLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
505-721 |
5.44e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 505 FQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGeplpkyehrylHRQVAAV 584
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEPLLF-GRSFKENIAYG------LVQEptMEEITAAAVESGAHGF-ISELSE------GYDTEvGEAG---------- 640
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGdaelraLEAE--LEELEAKLAEPDEDLErLAELQEefealgGWEAE-ARAEeilsglgfpe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 641 -------SQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLL--YESpergsrSVLFITQ-R--LSSVeq 708
Cdd:COG0488 144 edldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLknYPG------TVLVVSHdRyfLDRV-- 215
|
250
....*....|...
gi 529002597 709 ADHILFLEGGTII 721
Cdd:COG0488 216 ATRILELDRGKLT 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
503-724 |
5.48e-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: 97.82 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAY-PNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyEHRYLHRQV 581
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGR-SFKENIAY-----GLVQeptmEEITAAavesgahgfISELSEGYDTE--VGEAGSQLSGGQRQAVAL 653
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaglyGLKG----DELTAR---------LEELADRLGMEelLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 654 ARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALG-KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
520-732 |
5.54e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV-----LLDG-EPLPKYEH--RYLHRQVAAVGQEPLLF 591
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 -GRSFKENIAYG--LVQEPTMEEITAAAVESGAhgfiselsegydtEVGEAGSQ------LSGGQRQAVALARALIRKPR 662
Cdd:PRK11264 98 pHRTVLENIIEGpvIVKGEPKEEATARARELLA-------------KVGLAGKEtsyprrLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 663 VLILDDATSALDAnsqSLVERLL--YESPERGSRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK11264 165 VILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
503-733 |
6.26e-23 |
|
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: 98.62 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQnlyqptegqvLLDGEplpkyehrylHRQva 582
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITGD----------LPP-- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSF-KENIA-----YGLV----QEPTMEEITAA-AVESGAHGFIsELSEGYDTE-----------VGEAG 640
Cdd:COG1119 56 TYGNDVRLFGERRgGEDVWelrkrIGLVspalQLRFPRDETVLdVVLSGFFDSI-GLYREPTDEqrerarellelLGLAH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 641 ------SQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRlssVEQA----D 710
Cdd:COG1119 135 ladrpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIppgiT 211
|
250 260
....*....|....*....|...
gi 529002597 711 HILFLEGGTIIEAGTHQQLMTNE 733
Cdd:COG1119 212 HVLLLKDGRVVAAGPKEEVLTSE 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
502-724 |
9.50e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.34 E-value: 9.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPN-RPDVPVLQGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTEGQVLLDGEPLPKYEHRY 576
Cdd:cd03234 3 VLPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 lhrQVAAVGQ-EPLLFGRSFKENIAYGLV---QEPTMEEITAAAVEsgahgfISELSEGYDTEVGEAG-SQLSGGQRQAV 651
Cdd:cd03234 82 ---CVAYVRQdDILLPGLTVRETLTYTAIlrlPRKSSDAIRKKRVE------DVLLRDLALTRIGGNLvKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAG 724
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
503-733 |
9.60e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 99.49 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRqVA 582
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQ----EP--------LLFGRSFKENIAYGLVQEPTMEEItaAAVESGAhgfiselsegyDTEVGEagsqLSGGQRQA 650
Cdd:PRK13537 84 VVPQfdnlDPdftvrenlLVFGRYFGLSAAAARALVPPLLEF--AKLENKA-----------DAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARG-KTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
....
gi 529002597 730 MTNE 733
Cdd:PRK13537 226 IESE 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
503-674 |
1.22e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.41 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYehrylHR 579
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithVPAE-----NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLFGR-SFKENIAYGL-VQEPTMEEITAAAVESGAHGFISELSEgydtevgEAGSQLSGGQRQAVALARAL 657
Cdd:PRK09452 87 HVNTVFQSYALFPHmTVFENVAFGLrMQKTPAAEITPRVMEALRMVQLEEFAQ-------RKPHQLSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 529002597 658 IRKPRVLILDDATSALD 674
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-446 |
1.38e-22 |
|
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: 98.70 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 202 MAIPF--FTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVhSHLQG-----EVFQAVLRQETE 274
Cdd:cd18577 18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTIT-GERQArrirkRYLKALLRQDIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 275 FFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGL-----------MLWASPSLTMITLValpllfllpe 343
Cdd:cd18577 97 WFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIafiyswkltlvLLATLPLIAIVGGI---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 344 kMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLK 423
Cdd:cd18577 167 -MGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
250 260
....*....|....*....|...
gi 529002597 424 VGILYFGGQLVTSGSVSSGRLVT 446
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPGDVLT 268
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
189-478 |
1.60e-22 |
|
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: 98.27 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDwivQDETAAAFTQNVTLMSVLTIASAVLEfaadGIYNSTMGR----VHSHLQGEV 264
Cdd:cd18551 3 LALLLSLLGTAASLAQPLLVKNLID---ALSAGGSSGGLLALLVALFLLQAVLS----ALSSYLLGRtgerVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 265 FQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRGLCLL----GLMLWASPSLTMITLVALPLLFL 340
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQ----LVTGVLTVvgavVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 341 LPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGM 420
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 421 LLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
515-725 |
2.38e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.55 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPllfGRS 594
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENIAYGLVQEPTMEEITAAAVESGAHGFISELSE-GYDTE-VGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK15112 100 LNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQvGLLPDhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 529002597 673 LDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
369-732 |
2.75e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 369 EVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTssLSGMLLKVGILYFGGQLVTSGSVSSGRLVT-- 446
Cdd:PLN03130 484 EVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFI--LNSIPVLVTVVSFGVFTLLGGDLTPARAFTsl 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 447 ----------FILYQIqFTIAVEVLLSrYPRVQKAVGFSEKIFeyldrVPNCPKSGSLASLTLRgsvqfqDVSFAYPNRP 516
Cdd:PLN03130 562 slfavlrfplFMLPNL-ITQAVNANVS-LKRLEELLLAEERVL-----LPNPPLEPGLPAISIK------NGYFSWDSKA 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTEGQVLLDGeplpkyehrylhrQVAAVGQEPLLFGRSF 595
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNATV 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYGLVQEPTMEEiTAAAVESGAHGFisELSEGYD-TEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PLN03130 696 RDNILFGSPFDPERYE-RAIDVTALQHDL--DLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 675 ANsqslVERLLYES---PERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PLN03130 773 AH----VGRQVFDKcikDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
519-733 |
3.47e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.07 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE-HRYLHRQVAAVGQEPLLFGR-SFK 596
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIAYGLVQEPTMEEITAAAVESGAHGF-ISELSEGYdtevgeaGSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03218 94 ENILAVLEIRGLSKKEREEKLEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 676 NSQSLVERLLYESPERG---------SRSVLFITQRLssveqadHILFleGGTIIEAGTHQQLMTNE 733
Cdd:cd03218 167 IAVQDIQKIIKILKDRGigvlitdhnVRETLSITDRA-------YIIY--EGKVLAEGTPEEIAANE 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
189-448 |
5.44e-22 |
|
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: 96.72 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFG--EMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQ 266
Cdd:cd18552 1 LALAILGMILVAatTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 267 AVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRG----LCLLGLMLWASPSLTMITLVALPLLFLLP 342
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTV----LVRDpltvIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 343 EKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLL 422
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250 260
....*....|....*....|....*.
gi 529002597 423 KVGILYFGGQLVTSGSVSSGRLVTFI 448
Cdd:cd18552 237 IALVLWYGGYQVISGELTPGEFISFI 262
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
519-687 |
7.71e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 7.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL---PKYEhrylhRQVAAVGQEPLLFGR-S 594
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQ-----RPINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENIAYGLVQEP-TMEEITAAAVESGAHGFISELSegydtevGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSAL 673
Cdd:PRK11607 108 VEQNIAFGLKQDKlPKAEIASRVNEMLGLVHMQEFA-------KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170
....*....|....
gi 529002597 674 DansQSLVERLLYE 687
Cdd:PRK11607 181 D---KKLRDRMQLE 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
516-719 |
7.76e-22 |
|
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: 94.71 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVL----LDGEPLPKYEHRYLHRQVAAVGQEPLLF 591
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 GRSFKENIAYGlvqEPTMEEITAAAVESGA-HGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:cd03290 92 NATVEENITFG---SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 529002597 671 SALDAN-SQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGT 719
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
507-732 |
1.38e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTEGQVLLDGEPLPKYEHRYLHRQ 580
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHGFISELSEGYDtEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
518-725 |
1.48e-21 |
|
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: 94.04 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEH----RYLHRQVAAVGQ-EPLLFG 592
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEdaraRLRARHVGFVFQsFQLLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 RSFKENIAYG--LVQEPTMEEITAAAVEsgahgfiselsegydtEVGEAG------SQLSGGQRQAVALARALIRKPRVL 664
Cdd:COG4181 105 LTALENVMLPleLAGRRDARARARALLE----------------RVGLGHrldhypAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 665 ILDDATSALDANSQSLVERLLYE-SPERGSRSVLfITQRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFElNRERGTTLVL-VTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
509-721 |
1.67e-21 |
|
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: 93.94 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 509 SFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQE- 587
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 588 ------PLLFGRSFKENIaYGLvqEP-----TMEEITAAAvesgahgfisELSEGYDTEVgeagSQLSGGQRQAVALARA 656
Cdd:cd03267 105 qlwwdlPVIDSFYLLAAI-YDL--PParfkkRLDELSELL----------DLEELLDTPV----RQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVER-LLYESPERGSrSVLFITQRLSSVEQ-ADHILFLEGGTII 721
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNfLKEYNRERGT-TVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
525-732 |
2.18e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.41 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY---EHRYLHRQ-VAAVGQE-PLLFGRSFKENI 599
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYGLV---------QEPTMEEITAAAVESGAHGFISELSegydtevgeagsqlsGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:PRK10070 128 AFGMElaginaeerREKALDALRQVGLENYAHSYPDELS---------------GGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 671 SALDANSQSLVERLLYESPERGSRSVLFITQRL-SSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
518-732 |
2.39e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.80 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEH---RYLHRQVAAVGQEPllfgrs 594
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNP------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 fkeniaYG----------LVQEPTM--EEITAAAVESGAHGFISEL---SEGYDtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11308 102 ------YGslnprkkvgqILEEPLLinTSLSAAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
508-732 |
3.76e-21 |
|
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: 97.83 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 508 VSFAYPNRpDVPVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQP---TEGQVLLDGEPL---PKYEHRYLH-R 579
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlglSERELRRIRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPL-----LF--GRSFKENIAygLVQEPTMEEITAAAVEsgahgfiseLSEgydtEVG--EAGS-------QL 643
Cdd:COG4172 93 RIAMIFQEPMtslnpLHtiGKQIAEVLR--LHRGLSGAAARARALE---------LLE----RVGipDPERrldayphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIE 722
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
250
....*....|
gi 529002597 723 AGTHQQLMTN 732
Cdd:COG4172 238 QGPTAELFAA 247
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
521-733 |
3.90e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQE-PLLFGRSFKENI 599
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYGLVQEPTMEEITAAavesgahgfISELSE--GYDTEVGEAGSQLSGGQRQAVALARALIR-------KPRVLILDDAT 670
Cdd:COG4138 91 ALHQPAGASSEAVEQL---------LAQLAEalGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 671 SALDANSQSLVERLLYESPERGsRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQG-ITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
516-721 |
4.33e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PKyehrylhrqvAA-------V 584
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPR----------DAialgigmV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEPLLFgRSFK--ENIAYGLvqEPTMEEI--TAAAVESgahgfISELSEGY------DTEVGeagsQLSGGQRQAVALA 654
Cdd:COG3845 86 HQHFMLV-PNLTvaENIVLGL--EPTKGGRldRKAARAR-----IRELSERYgldvdpDAKVE----DLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 655 RALIRKPRVLILDDATSAL-DANSQSL---VERLLyespERGsRSVLFITQRLSSVEQ-ADHILFLEGGTII 721
Cdd:COG3845 154 KALYRGARILILDEPTAVLtPQEADELfeiLRRLA----AEG-KSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
517-724 |
5.56e-21 |
|
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: 91.43 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQVLLDGE---PLPKYEHrylhrqvAAVGqeplLF 591
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEER-------ARLG----IF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 grsfkenIAYglvQEPtmEEITAAAVESgahgFISELSEGydtevgeagsqLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:cd03217 81 -------LAF---QYP--PEIPGVKNAD----FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 672 ALDANSQSLVERLLYESPERGsRSVLFIT--QRLSSVEQADHILFLEGGTIIEAG 724
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEG-KSVLIIThyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
523-733 |
5.77e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 5.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 523 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LP-----------KYEHRYLHRQVAAVgqEP 588
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPghqiarmgvvrTFQHVRLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 LLFG--RSFKENIAYGLVQEPTMEEITAAAVESGAHGfiseLSEGYDTEVG--EAGSqLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATW----LERVGLLEHAnrQAGN-LAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 665 ILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
515-675 |
8.91e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQP--TEGQVLLDGE---PLPKYEhrylhRQVAAVGQEP 588
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRrltALPAEQ-----RRIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 LLFGR-SFKENIAYGLVQEPTMEE----ITAAAVESGAHGFiselsegYDTEVGeagsQLSGGQRQAVALARALIRKPRV 663
Cdd:COG4136 86 LLFPHlSVGENLAFALPPTIGRAQrrarVEQALEEAGLAGF-------ADRDPA----TLSGGQRARVALLRALLAEPRA 154
|
170
....*....|..
gi 529002597 664 LILDDATSALDA 675
Cdd:COG4136 155 LLLDEPFSKLDA 166
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
515-729 |
1.00e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR----YL-HRQvaavGQEPL 589
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 590 LfgrSFKENIA-----YGlvQEPTMEEITAAAVESGAhgfISELSEGYdtevgeagsqLSGGQRQAVALARALIRKPRVL 664
Cdd:PRK13539 88 L---TVAENLEfwaafLG--GEELDIAAALEAVGLAP---LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 665 ILDDATSALDANSQSLVERLLyespergsrsvlfitqrlssveqADHilfLEGGTIIEAGTHQQL 729
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELI-----------------------RAH---LAQGGIVIAATHIPL 188
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
503-725 |
1.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAY-PNRPDVP-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV----LLDGEPLPKYEHRY 576
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 LHRQVAAVGQEP--LLFGRSFKENIAYGL----VQEPTMEEITAAAVEsgAHGFISELSEgydtevgEAGSQLSGGQRQA 650
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPqnfgIPKEKAEKIAAEKLE--MVGLADEFWE-------KSPFELSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQslVERL-LYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGT 725
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKAR--IEMMqLFESIHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGT 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
515-707 |
1.03e-20 |
|
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: 90.88 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYlHRQVAAVGQEPLLFGR- 593
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAYglvqeptmeeitAAAVESGAHGFISELSEgydtEVGEAG------SQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:TIGR01189 89 SALENLHF------------WAAIHGGAQRTIEDALA----AVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 529002597 668 DATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVE 707
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
503-718 |
1.49e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPDVpvLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR---YLHR 579
Cdd:PRK10908 2 IRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQE-PLLFGRSFKENIAYGLVqeptmeeITAAAVE------SGAHGFISELSEGYDTEVgeagsQLSGGQRQAVA 652
Cdd:PRK10908 80 QIGMIFQDhHLLMDRTVYDNVAIPLI-------IAGASGDdirrrvSAALDKVGLLDKAKNFPI-----QLSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 653 LARALIRKPRVLILDDATSALD-ANSQSLVErlLYESPERGSRSVLFITQRLSSVEQADH-ILFLEGG 718
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDdALSEGILR--LFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
503-719 |
1.57e-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: 88.27 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDgeplPKYEHRYLhrqva 582
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 avgqepllfgrsfkeniayglvqeptmeeitaaavesgahgfiselsegydtevgeagSQLSGGQRQAVALARALIRKPR 662
Cdd:cd03221 69 ----------------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPergsRSVLFIT---QRLSSVeqADHILFLEGGT 719
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVShdrYFLDQV--ATKIIELEDGK 144
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
503-725 |
2.28e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.83 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpKYEHR---YLHR 579
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEP--LLFGRSFKENIAYG-----LVQEPTMEEITAAAVESGahgfISELSEgydtevgEAGSQLSGGQRQAVA 652
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 653 LARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVE-QADHILFLEGGTIIEAGT 725
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
189-450 |
3.56e-20 |
|
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: 91.72 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVF--LSCFGEMAIPFFTGRLTDWIVQDetaaAFTQNVTLMSVLTIASAVLEFAADGIYNSTMG----RVHSHLQG 262
Cdd:cd18542 1 YLLAILAllLATALNLLIPLLIRRIIDSVIGG----GLRELLWLLALLILGVALLRGVFRYLQGYLAEkasqKVAYDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 EVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRGLCLLG----LMLWASPSLTMITLVALPLL 338
Cdd:cd18542 77 DLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 339 FLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLS 418
Cdd:cd18542 153 ALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFL 232
|
250 260 270
....*....|....*....|....*....|..
gi 529002597 419 GMLLKVGILYFGGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18542 233 SGLQIVLVLWVGGYLVINGEITLGELVAFISY 264
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
507-724 |
5.15e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpKYEHR---YLHRQVAA 583
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 584 VGQEP--LLFGRSFKENIAYGLVQEPTMEEITAAAVESG-----AHGFISELSEGydtevgeagsqLSGGQRQAVALARA 656
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAltlvdAQHFRHQPIQC-----------LSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAG 724
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
525-674 |
5.96e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.64 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEplpkyEHRYL---HRQVAAVGQEPLLFGR-SFKENIA 600
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 601 YGL--------VQEPTMEEItaaAVESGAHGFISELSegydtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK10771 94 LGLnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
..
gi 529002597 673 LD 674
Cdd:PRK10771 160 LD 161
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
189-450 |
6.27e-20 |
|
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: 90.93 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFL--SCFGEMAIPFFTGRLTDWIVQDE-TAAAFTQNVTLMSVLTIASAVLEFaadgIYNSTMG----RVHSHLQ 261
Cdd:cd18541 1 YLLGILFLilVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRF----LWRYLIFgasrRIEYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 262 GEVFQAVLRQETEFFQKNQTGEITSRVTDDTST---------MseslssdlslllwYLIRGLCL----LGLMLWASPSLT 328
Cdd:cd18541 77 NDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAvrmalgpgiL-------------YLVDALFLgvlvLVMMFTISPKLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 329 MITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMvlnqKEALAY 408
Cdd:cd18541 144 LIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYV----EKNLRL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 529002597 409 A-VNVWTSSLSGMLLKVG---ILYFGGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18541 220 ArVDALFFPLIGLLIGLSfliVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
515-692 |
7.77e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.32 E-value: 7.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYlHRQVAAVGQ----EPLL 590
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 fgrSFKENIAY--GLVQEPTMEEITAAAVESGAHGFisElsegyDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDD 668
Cdd:PRK13538 90 ---TALENLRFyqRLHGPGDDEALWEALAQVGLAGF--E-----DVPVR----QLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180
....*....|....*....|....
gi 529002597 669 ATSALDANSQSLVERLLYESPERG 692
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQG 179
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-684 |
1.27e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 512 YPNRPD-VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEP---LPKYEhRYlhRQVAAVGQE 587
Cdd:COG1101 12 NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK-RA--KYIGRVFQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 588 PLL---------------FGRSFKENIAYGLvqepTMEEITAaavesgahgFISELSE---GY----DTEVGeagsQLSG 645
Cdd:COG1101 89 PMMgtapsmtieenlalaYRRGKRRGLRRGL----TKKRREL---------FRELLATlglGLenrlDTKVG----LLSG 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 529002597 646 GQRQAVALARALIRKPRVLILDDATSALDANSQSLVERL 684
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEL 190
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
520-707 |
1.41e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 87.55 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYlHRQVAAVGQEPLLFGR-SFKEN 598
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYgLVQEPTMEEITAAAVESGAHGFiselsegYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQ 678
Cdd:cd03231 94 LRF-WHADHSDEQVEEALARVGLNGF-------EDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....*....
gi 529002597 679 SLVERLLYESPERGSRSVLFITQRLSSVE 707
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
517-729 |
1.47e-19 |
|
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: 88.20 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyEHRYLHRQVAAVGQEPL----LFG 592
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSvddeLTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 RsfkENIA-----YGLVQEPTMEEitaaavesgahgfISELSEGYdtEVGEAGSQL----SGGQRQAVALARALIRKPRV 663
Cdd:cd03265 91 W---ENLYiharlYGVPGAERRER-------------IDELLDFV--GLLEAADRLvktySGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
204-449 |
1.68e-19 |
|
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: 89.53 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 204 IPFFTGRLTDWIVQ--DETAAAFTQNV-----TLMSVLtIASAVLEFAAdgIYN-STMG-RVHSHLQGEVFQAVLRQETE 274
Cdd:cd18574 15 IPLLLGDLVNVISRslKETNGDFIEDLkkpalKLLGLY-LLQSLLTFAY--ISLlSVVGeRVAARLRNDLFSSLLRQDIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 275 FFQKNQTGEITSRVTDDT----STMSESlssdlslllwyLIRGL--------CLLGLMLwASPSLTMITLVALPLLFLLP 342
Cdd:cd18574 92 FFDTHRTGELVNRLTADVqefkSSFKQC-----------VSQGLrsvtqtvgCVVSLYL-ISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 343 EKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKeaLAYAVNVWTS----SLS 418
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK--LGLGIGIFQGlsnlALN 237
|
250 260 270
....*....|....*....|....*....|.
gi 529002597 419 GMLLkvGILYFGGQLVTSGSVSSGRLVTFIL 449
Cdd:cd18574 238 GIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
500-724 |
1.93e-19 |
|
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: 87.59 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 500 RGSVQFQDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEhrylhr 579
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 qvAAVGQEPLLFGRsfkENIA-YGLVQEPTMEEItaAAVESGAHGFiSELSEGYDTEVGEagsqLSGGQRQAVALARALI 658
Cdd:cd03220 91 --LGGGFNPELTGR---ENIYlNGRLLGLSRKEI--DEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
506-725 |
1.97e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPD---VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13633 8 KNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 A-VGQEP--LLFGRSFKENIAYG---LVQEPtmEEITAAAVESGAHGFISELSEgydtevgEAGSQLSGGQRQAVALARA 656
Cdd:PRK13633 88 GmVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRERVDESLKKVGMYEYRR-------HAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
520-704 |
2.77e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.56 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR----YLHRQVAAVGQ-EPLLFGRS 594
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENIAYGLV---------QEPTMEEITAAAVESGAHGFISElsegydtevgeagsqLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK11629 104 ALENVAMPLLigkkkpaeiNSRALEMLAAVGLEHRANHRPSE---------------LSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLS 704
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
505-729 |
4.48e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.15 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 505 FQDVSFAY-PNRP-------DVPVlqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV-----LLDGEPLPK 571
Cdd:PRK13634 5 FQKVEHRYqYKTPferralyDVNV------SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigerVITAGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 572 yEHRYLHRQVAAVGQ--EPLLFGRSFKENIAYGlvqePTMEEITAAAVESGAHGFISELseGYDTEVGEAGS-QLSGGQR 648
Cdd:PRK13634 79 -KLKPLRKKVGIVFQfpEHQLFEETVEKDICFG----PMNFGVSEEDAKQKAREMIELV--GLPEELLARSPfELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQ 727
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
..
gi 529002597 728 QL 729
Cdd:PRK13634 232 EI 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
502-725 |
5.93e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAY-PNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY----EHR 575
Cdd:PRK13649 2 GINLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 576 YLHRQVAAVGQ--EPLLFGRSFKENIAYGlvqeP-----TMEEITAAAVESGAHGFISElsEGYDTEVGEagsqLSGGQR 648
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGISE--SLFEKNPFE----LSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 649 QAVALARALIRKPRVLILDDATSALD-ANSQSLVErlLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGT 725
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDpKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
517-725 |
6.17e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 86.66 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQVLLDGEPL----PkyEHRylhrqvAAVG----- 585
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIlelsP--DER------ARAGiflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLLF-GRSFKE--NIAYGLVQEptmEEITAAAVESGAHGFISEL--SEGY-DTEVGEaGsqLSGGQRQAVALARALIR 659
Cdd:COG0396 84 QYPVEIpGVSVSNflRTALNARRG---EELSAREFLKLLKEKMKELglDEDFlDRYVNE-G--FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 660 KPRVLILDDATSALDANSQSLV----ERLLyeSPERGsrsVLFIT--QRLSSVEQADHILFLEGGTIIEAGT 725
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVaegvNKLR--SPDRG---ILIIThyQRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
513-725 |
1.04e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 513 PNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTEGQVLLDGEplpkyehrylhrqVAA-----V 584
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILEPTSGRVEVNGR-------------VSAllelgA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEPLLFGRsfkENI-----AYGLVQEPtMEEITAAAVEsgahgFiSELSEGYDTEVGeagsQLSGGQRQAVALARALIR 659
Cdd:COG1134 98 GFHPELTGR---ENIylngrLLGLSRKE-IDEKFDEIVE-----F-AELGDFIDQPVK----TYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:COG1134 164 DPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
501-719 |
1.14e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTEGQVLLdgeplPKyehryl 577
Cdd:COG4178 361 GALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYGSGRIAR-----PA------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 HRQVAAVGQEPLLFGRSFKENIAY-GLVQEPTMEEITAAAVESGAHGFISELSEGYDTEvgeagSQLSGGQRQAVALARA 656
Cdd:COG4178 425 GARVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEADWD-----QVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYEspERGSRSVLFITQRLSSVEQADHILFLEGGT 719
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
484-730 |
1.26e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 91.38 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 484 RVPNCPKSGSLASLTLRGSVQFQDVSFAYPNrpdvpvlqgltftlrpGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVL 563
Cdd:PTZ00243 655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 564 LDgeplpkyehrylhRQVAAVGQEPLLFGRSFKENIaygLVQEPTMEEITAAAVE-SGAHGFISELSEGYDTEVGEAGSQ 642
Cdd:PTZ00243 719 AE-------------RSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVRvSQLEADLAQLGGGLETEIGEKGVN 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 643 LSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLfITQRLSSVEQADHILFLEGGTIIE 722
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVL-ATHQVHVVPRADYVVALGDGRVEF 861
|
....*...
gi 529002597 723 AGTHQQLM 730
Cdd:PTZ00243 862 SGSSADFM 869
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
503-733 |
1.47e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEP--LLFGRSFKENIAYGLV-QEPTMEEITAAAVESGAHGFISELSEgydtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVnMGLDKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLS-SVEQADHILFLEGGTIIEAGThQQLMTNE 733
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG-KTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
502-729 |
1.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYpnRPDVP----VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL---PKYEH 574
Cdd:PRK13646 2 TIRFDNVSYTY--QKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthkTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 575 -RYLHRQVAAVGQ--EPLLFGRSFKENIAYGlvqePTMEEITAAAVESGAHGFISELseGYDTEVGEAGS-QLSGGQRQA 650
Cdd:PRK13646 80 iRPVRKRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
504-700 |
1.52e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEhrylhRQV 581
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----RGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 aAVGQEPLLFGRSFKENIAYGLvqepTMEEITAAAVESGAHGFISelsegydtEVGEAGS------QLSGGQRQAVALAR 655
Cdd:PRK11248 75 -VFQNEGLLPWRNVQDNVAFGL----QLAGVEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIAR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFIT 700
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
516-740 |
1.53e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPlpkyeHRY------LHRQVAAVGQE-- 587
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 588 --PLLfgrSFKENI-------AYGLVQEPTMEEITAAAVEsgahgfisELSEGYD--TEVGEagsqLSGGQRQAVALARA 656
Cdd:PRK11288 90 lvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLE--------HLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTIIEagTHQQL--MTNE 733
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG-RVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMaqVDRD 231
|
....*..
gi 529002597 734 GRYWAMV 740
Cdd:PRK11288 232 QLVQAMV 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
520-720 |
2.47e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY-EHRYLHRQVAAvgqepLLFGRSFKEN 598
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEArEDTRLMFQDAR-----LLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYGLV---QEPTMEEITAAAVESGAhgfiselsegydtevGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:PRK11247 102 VGLGLKgqwRDAALQALAAVGLADRA---------------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 529002597 676 ----NSQSLVERLLYESpergSRSVLFITQRLS-SVEQADHILFLEGGTI 720
Cdd:PRK11247 167 ltriEMQDLIESLWQQH----GFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-478 |
2.66e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 86.02 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQN----VTLMSVLTIASAVLEfAADGIYNSTMG-RVHSHLQGE 263
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLllllVLGLAGAYVLSALLG-ILRGRLLARLGeRITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 264 VFQAVLRQETEFFQKNQTGEITSRVTDDTSTMseslssdlsllLWYLIRGLC-----------LLGLMLWASPSLTMITL 332
Cdd:cd18563 82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRL-----------QDFLSDGLPdfltnilmiigIGVVLFSLNWKLALLVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 333 VALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKealayAVNV 412
Cdd:cd18563 151 IPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR-----AEKL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 413 WTS--SLSGMLLKVG---ILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18563 226 WATffPLLTFLTSLGtliVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
520-733 |
2.73e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGR-SFKEN 598
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYG------LVQEPTMEEITAAAVESGAHGFISELSEGYDTevgeagsqLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK10253 102 VARGryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 673 LDANSQ-SLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK10253 174 LDISHQiDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
503-722 |
3.73e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLdGEPLpkyEHRYL--HRQ 580
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---KIGYFdqHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLlfgrsfkENIAYGLvqePTMEEITAAAVeSGAHGFISElsegydtEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:COG0488 389 ELDPDKTVL-------DELRDGA---PGGTEQEVRGY-LGRFLFSGD-------DAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 661 PRVLILDDATSALDANSQSLVERLL--YEsperGsrSVLFITQ-R--LSSVeqADHILFLEGGTIIE 722
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALddFP----G--TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
520-720 |
4.32e-18 |
|
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: 82.48 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPkyehrylhrqvaavgqepllfGRSFKENI 599
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYG--LVQEptmeeitaaavESGAHGFISELSegydteVGE---AGSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:cd03215 74 RAGiaYVPE-----------DRKREGLVLDLS------VAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 529002597 675 ANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTI 720
Cdd:cd03215 137 VGAKAEIYRLIRELADAG-KAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
506-731 |
4.57e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPDV-PVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PRK15134 9 ENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 ----QVAAVGQEPLL-------FGRSFKENIAY--GLVQEPTMEEITAAAVESGAHGFISELSEgydtevgeAGSQLSGG 646
Cdd:PRK15134 89 vrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGIRQAAKRLTD--------YPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNR 240
|
....*.
gi 529002597 726 HQQLMT 731
Cdd:PRK15134 241 AATLFS 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
516-726 |
4.88e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPT---EGQVLLDGEPLPKYEHRYLHRQ-VAAVGQEPLLF 591
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 -GRSFKENIAYGlvQEPTMEEITA-AAVESGAHGFISELseGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK13549 95 kELSVLENIFLG--NEITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 670 TSALDANSQSLVERLLYESPERGSRSVlFITQRLSSVEQ-ADHIlfleggTIIEAGTH 726
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACI-YISHKLNEVKAiSDTI------CVIRDGRH 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
502-727 |
5.39e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG-------EPLPKyEH 574
Cdd:PRK11124 2 SIQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDK-AI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 575 RYLHRQVAAVGQE----PLLfgrSFKENiaygLVQEP------TMEEITAAAVESGAHGFISELSEGYDTevgeagsQLS 644
Cdd:PRK11124 78 RELRRNVGMVFQQynlwPHL---TVQQN----LIEAPcrvlglSKDQALARAEKLLERLRLKPYADRFPL-------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsrsvlfITQRLSSVE------QADHILFLEGG 718
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG------ITQVIVTHEvevarkTASRVVYMENG 217
|
....*....
gi 529002597 719 TIIEAGTHQ 727
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
502-675 |
5.85e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.05 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylHRQV 581
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGR-SFKENIAYGL----VQEPTMEE-ITAAAVesgahgfISELSEGYDTEvgeaGSQLSGGQRQAVALAR 655
Cdd:PRK11650 79 AMVFQNYALYPHmSVRENMAYGLkirgMPKAEIEErVAEAAR-------ILELEPLLDRK----PRELSGGQRQRVAMGR 147
|
170 180
....*....|....*....|
gi 529002597 656 ALIRKPRVLILDDATSALDA 675
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA 167
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
503-717 |
1.41e-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: 80.66 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVlldgeplpkyeHRYLHRQVA 582
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLLFGRSFKENIAYglvqePTMEEitaaavesgahgfiselsegydtevgeagsqLSGGQRQAVALARALIRKPR 662
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 663 VLILDDATSALDANSqslvERLLYESPERGSRSVLFITQRLSSVEQADHILFLEG 717
Cdd:cd03223 112 FVFLDEATSALDEES----EDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
512-733 |
1.87e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.38 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 512 YPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEhR------YLhrqva 582
Cdd:COG1137 13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEditHLPMHK-RarlgigYL----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 avGQEPLLFGR-SFKENIAygLVQEptMEEITAAAVESGAHGFISELSEGY--DTevgeAGSQLSGGQRQAVALARALIR 659
Cdd:COG1137 84 --PQEASIFRKlTVEDNIL--AVLE--LRKLSKKEREERLEELLEEFGITHlrKS----KAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 660 KPRVLILD------DATSALDAnsQSLVERLlyesPERGSrSVLfITqrlssveqaDH-------------ILFleGGTI 720
Cdd:COG1137 154 NPKFILLDepfagvDPIAVADI--QKIIRHL----KERGI-GVL-IT---------DHnvretlgicdrayIIS--EGKV 214
|
250
....*....|...
gi 529002597 721 IEAGTHQQLMTNE 733
Cdd:COG1137 215 LAEGTPEEILNNP 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-718 |
2.25e-17 |
|
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: 81.74 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG----EPLPKyehrylhRQVaaVGQE-PLLFGRSF 595
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitEPGPD-------RMV--VFQNySLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYG----LVQEPTMEEitAAAVESgaHGFISELSEGYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDATS 671
Cdd:TIGR01184 72 RENIALAvdrvLPDLSKSER--RAIVEE--HIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 529002597 672 ALDA-NSQSLVERLLYESPERGSrSVLFITQRL-SSVEQADHILFLEGG 718
Cdd:TIGR01184 144 ALDAlTRGNLQEELMQIWEEHRV-TVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
520-732 |
2.55e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL-------------PKYEHRYLHRQVAAVGQ 586
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 587 EPLLFGR-SFKENIAYGLVQ--EPTMEEITAAAVESGAHGFISELSEGydtevgEAGSQLSGGQRQAVALARALIRKPRV 663
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQvlGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 664 LILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
524-734 |
3.68e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQE--PLLFGRSFKeniaY 601
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtPPFAMPVFQ----Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 602 GLVQEPtmeeitAAAVESGAHGFISELSE--GYDTEVGEAGSQLSGGQRQAVALARALIR-----KP--RVLILDDATSA 672
Cdd:PRK03695 90 LTLHQP------DKTRTEAVASALNEVAEalGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 673 LDANSQSLVERLLYESPERGsRSVLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMTNEG 734
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQG-IAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
523-732 |
3.96e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 523 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEH---RYLHRQVAAVGQEPLlfgRSFKENI 599
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPL---ASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYG-LVQEPT---MEEITAAAVESGAH------GFISELSEGYDTEvgeagsqLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:PRK15079 116 TIGeIIAEPLrtyHPKLSRQEVKDRVKammlkvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 670 TSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
516-722 |
5.12e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.84 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPT---EGQVLLDGEP-----LPKYEHR---YLHRQVAAV 584
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVcrfkdIRDSEALgivIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 gqePLLfgrSFKENIAYGlvqeptmeeitaaaVESGAHGFIS---------------ELSEGYDTEVGEAGSqlsgGQRQ 649
Cdd:NF040905 91 ---PYL---SIAENIFLG--------------NERAKRGVIDwnetnrrarellakvGLDESPDTLVTDIGV----GKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 650 AVALARALIRKPRVLILDDATSAL-DANSQSLVErLLYESPERGSRSVLfITQRLSSVEQ-ADHILFLEGGTIIE 722
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLELKAQGITSII-ISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
520-732 |
7.47e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQVLLDGEPL--PKYEHRYLHRQVAAVGQEPLLFG 592
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 R-SFKENIAYGL------VQEPTMEEITAAAVESGAhgfiseLSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK14267 99 HlTIYDNVAIGVklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 666 LDDATSALDANSQSLVERLLYESPErgSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
518-719 |
9.84e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 80.17 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 518 VPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLldgeplpkYEHRY--------LHRQVAAVgqepl 589
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGgwvdlaqaSPREILAL----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 590 lfgRsfKENIAYglVQE--------PTMEEITAAAVESGAhgfisELSEGYDtEVGEAGSQL--------------SGGQ 647
Cdd:COG4778 91 ---R--RRTIGY--VSQflrviprvSALDVVAEPLLERGV-----DREEARA-RARELLARLnlperlwdlppatfSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQ-ADHILFLEGGT 719
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGT-AIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
411-667 |
1.05e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.08 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 411 NVWTSSLsgMLLKVGILYFGGQLVtsGSVSSGRLVTFILyqiqfTI-----AVEVLLSRYPRVQKA-VGFsEKIfEYLDR 484
Cdd:COG4615 236 NNWGNLL--FFALIGLILFLLPAL--GWADPAVLSGFVL-----VLlflrgPLSQLVGALPTLSRAnVAL-RKI-EELEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 485 VPNCPKSGSLASLTLRGSVQFQ-----DVSFAYPNRPDVP--VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP 557
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPADFQtlelrGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 558 TEGQVLLDGEPLPKyEHRYLHRQ-VAAVGQEPLLFGRsfkeniAYGLVQEPTMEEITA----------AAVESGAhgfis 626
Cdd:COG4615 385 ESGEILLDGQPVTA-DNREAYRQlFSAVFSDFHLFDR------LLGLDGEADPARAREllerleldhkVSVEDGR----- 452
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 529002597 627 eLSegyDTEvgeagsqLSGGQRQAVALARALI-RKPrVLILD 667
Cdd:COG4615 453 -FS---TTD-------LSQGQRKRLALLVALLeDRP-ILVFD 482
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
504-721 |
1.19e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.01 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 504 QFQDVSFAYPN-RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGqvlldgeplpkyEHRYLHRQVA 582
Cdd:PRK10535 6 ELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG------------TYRVAGQDVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQEPLL------FGRSFKEniaYGLVQEPTMEE-ITAAAVESG---------AHGFISELseGYDTEVGEAGSQLSGG 646
Cdd:PRK10535 74 TLDADALAqlrrehFGFIFQR---YHLLSHLTAAQnVEVPAVYAGlerkqrllrAQELLQRL--GLEDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQADHILFLEGGTII 721
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRG-HTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
502-732 |
1.46e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAYPnrPDVPV----LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL-PKYEHRY 576
Cdd:PRK13641 2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 577 L---HRQVAAVGQ--EPLLFGRSFKENIAYGlvqePTMEEITAAAVESGAHGFISELseGYDTEVGEAGS-QLSGGQRQA 650
Cdd:PRK13641 80 LkklRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 651 VALARALIRKPRVLILDDATSALDANSQSLVERLLYESpERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
...
gi 529002597 730 MTN 732
Cdd:PRK13641 233 FSD 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
505-722 |
4.00e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 505 FQDVSFAYPNRP-DV-PVlqglTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKyEHRYLHRQ-V 581
Cdd:PRK10522 325 LRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKlF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGRsfkeniayglVQEPTMEEITAAAVESGAHgfISELSEGYDTEVGE-AGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10522 400 SAVFTDFHLFDQ----------LLGPEGKPANPALVEKWLE--RLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 661 PRVLILDDAtsALDANSQ---SLVERLLYESPERGsRSVLFITQRLSSVEQADHILFLEGGTIIE 722
Cdd:PRK10522 468 RDILLLDEW--AADQDPHfrrEFYQVLLPLLQEMG-KTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
516-724 |
4.01e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTEGQVLLDGEPLPKYEHRylHRQVAAVGQEPllf 591
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 gRSfkeniAYGLVQepTMeeiTAAAVES----GAHGFISELSEGYDtEVGEAGS---------QLSGGQRQAVALARALI 658
Cdd:PRK10418 89 -RS-----AFNPLH--TM---HTHARETclalGKPADDATLTAALE-AVGLENAarvlklypfEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
502-725 |
5.99e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 502 SVQFQDVSFAY-PNRP-DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--PKYEHRYL 577
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 HRQVAAVGQEP--LLFGRSFKENIAYGLVQ-EPTMEEITAAAVESGAhgfISELSegYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFGPINlGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 655 RALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGT 725
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
519-729 |
6.38e-16 |
|
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: 78.74 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGeplpkyehrylhrQVAAVGQEPLLFGRSFKEN 598
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYGLV--QEPTMEEITAAAVESGahgfISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDAn 676
Cdd:cd03291 118 IIFGVSydEYRYKSVVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV- 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 677 sqsLVERLLYES---PERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:cd03291 193 ---FTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
507-700 |
7.27e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 507 DVSFAYPNRPDV---PVL--QGLT---------FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPky 572
Cdd:COG1129 240 ELEDLFPKRAAApgeVVLevEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 573 ehryLHRQVAAVgqepllfgrsfKENIAY--------GLVQEPTMEE-ITAAAVES-GAHGFIS-----ELSEGY----- 632
Cdd:COG1129 318 ----IRSPRDAI-----------RAGIAYvpedrkgeGLVLDLSIREnITLASLDRlSRGGLLDrrrerALAEEYikrlr 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 633 ------DTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFIT 700
Cdd:COG1129 383 iktpspEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVIS 451
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
519-729 |
7.52e-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: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGeplpkyehrylhrQVAAVGQEPLLFGRSFKEN 598
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IAYGLvqepTMEE------ITAAAVESGahgfISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:TIGR01271 507 IIFGL----SYDEyrytsvIKACQLEED----IALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 673 LDAnsqsLVERLLYES---PERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:TIGR01271 579 LDV----VTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
521-691 |
8.41e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PT---EGQVLLDGEPL--PKYEHRYLHRQVAAVGQEPLLFGR 593
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAYG---LVQEPTMEEITAAAVESGAhgfiseLSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDAT 670
Cdd:PRK14243 106 SIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180
....*....|....*....|.
gi 529002597 671 SALDANSQSLVERLLYESPER 691
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQ 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
517-726 |
8.98e-16 |
|
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: 80.64 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTEGQVLLDGEPLPKYEHRYLHRQ-VAAVGQEPLLFGR 593
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 -SFKENIAYGlvqeptmEEITA-------AAVESGAHGFISELSEGyDTEVGEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:TIGR02633 93 lSVAENIFLG-------NEITLpggrmayNAMYLRAKNLLRELQLD-ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGSRSVlFITQRLSSVEQ-ADHIlfleggTIIEAGTH 726
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKAHGVACV-YISHKLNEVKAvCDTI------CVIRDGQH 219
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
189-455 |
1.25e-15 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 78.21 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETA------AAFTQNVTLMSVLTIASAVLEFaadgIYNSTMGRVhshlqg 262
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSY----LQNRLMARV------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 eVFQAV--LRQETE---------FFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRGLCL----LGLMLWASPSL 327
Cdd:cd18547 73 -SQRTVydLRKDLFeklqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQ----LISSILTivgtLIMMLYISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 328 TMITLVALPLLFLLPEKMGKW-YKVLAEQvQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQK-EA 405
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRsQKYFRKQ-QKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQF 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 529002597 406 LAYAVNVWTSSLSGMLLkVGILYFGGQLVTSGSVSSGRLVTFILYQIQFT 455
Cdd:cd18547 227 YSGLLMPIMNFINNLGY-VLVAVVGGLLVINGALTVGVIQAFLQYSRQFS 275
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
520-731 |
1.46e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.11 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLyqPTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKEN 598
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLlSALLRLL--STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 IayglvqEP----TMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:TIGR01271 1312 L------DPyeqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 675 ANSQSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMT 731
Cdd:TIGR01271 1386 PVTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
515-729 |
1.76e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPT----EGQVLLDGEPLpkyEHRYLHRQVAAVGQEPLL 590
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 FGR-SFKENI---AYGLVQEPTMEEITAAAVESgahgFISELS--EGYDTEVGEAGSQ--LSGGQRQAVALARALIRKPR 662
Cdd:TIGR00955 111 IPTlTVREHLmfqAHLRMPRRVTKKEKRERVDE----VLQALGlrKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQQL 729
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
517-732 |
1.95e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLPKYEHRYLHRQVAAVGQEP----- 588
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 --LLFGRSFKENI-AYGLVQEPTMEEITAAAVESgaHGFISELSEGYDTEvgeagsqLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK10261 416 prQTVGDSIMEPLrVHGLLPGKAAAARVAWLLER--VGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADH---ILFLegGTIIEAGTHQQLMTN 732
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvaVMYL--GQIVEIGPRRAVFEN 554
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
515-729 |
2.62e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLpkyehRYLHRQV------------- 581
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRQVielseqsaaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 ------AAVGQEPLL-------FGRSFKENIAygLVQEPTMEEITAAAVESGAHGFISElsegYDTEVGEAGSQLSGGQR 648
Cdd:PRK10261 101 vrgadmAMIFQEPMTslnpvftVGEQIAESIR--LHQGASREEAMVEAKRMLDQVRIPE----AQTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQ 727
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGSVE 254
|
..
gi 529002597 728 QL 729
Cdd:PRK10261 255 QI 256
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
520-731 |
2.89e-15 |
|
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: 76.82 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTEGQVLLDGEPLPKYEHRYLHRQVAAVGQEPLLFGRSFKEN 598
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 599 I-AYGLVQEptmEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANS 677
Cdd:cd03289 97 LdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 529002597 678 QSLVERLLYESpeRGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMT 731
Cdd:cd03289 174 YQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
517-733 |
3.14e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV--------------LLDGEPLPKYEHRY--LHRQ 580
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhELITNPYSKKIKNFkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEP--LLFGRSFKENIAYGlvqePTMEEITAAAVESGAHGFISELSEGYD-TEVGEAGsqLSGGQRQAVALARAL 657
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529002597 658 IRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANN-KTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
189-471 |
4.25e-15 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 76.72 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFlSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAAdGIYNSTMG-RVHSHLQGEVFQA 267
Cdd:cd18570 8 LLLSLLI-TLLG-IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIR-SYLLLKLSqKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 268 VLRQETEFFQKNQTGEITSRVTD-----------------DTSTMseslssdlslllwylirgLCLLGLMLWASPSLTMI 330
Cdd:cd18570 85 LLKLPLSFFETRKTGEIISRFNDankireaissttislflDLLMV------------------IISGIILFFYNWKLFLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 331 TLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAV 410
Cdd:cd18570 147 TLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 411 NVWTSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKA 471
Cdd:cd18570 227 QSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
189-453 |
4.81e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 76.37 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAAdGIYNSTMG-RVHSHLQGEVFQA 267
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQ-TYLSARIGqGVMYDLRVQLYAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 268 VLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGK 347
Cdd:cd18550 82 LQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 348 WYKVLAEQVQESLAKSSQVAIEVLSA--MPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALayaVNVWTSSLSGMLLKVG 425
Cdd:cd18550 162 RRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQAL---AGRWFFAALGLFTAIG 238
|
250 260 270
....*....|....*....|....*....|.
gi 529002597 426 ---ILYFGGQLVTSGSVSSGRLVTFILYQIQ 453
Cdd:cd18550 239 palVYWVGGLLVIGGGLTIGTLVAFTALLGR 269
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
506-733 |
5.28e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVG 585
Cdd:COG4604 5 KNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLL-----------FGRsF---------------KENIAY-GLvqeptmEEItaaavesgAHGFISElsegydtevge 638
Cdd:COG4604 82 QENHInsrltvrelvaFGR-FpyskgrltaedreiiDEAIAYlDL------EDL--------ADRYLDE----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 639 agsqLSGGQRQAVALARALIRKPRVLILDDATSALD-ANSQSLVERLLYESPERGsRSVL-------FitqrlSSVeQAD 710
Cdd:COG4604 136 ----LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMKLLRRLADELG-KTVVivlhdinF-----ASC-YAD 204
|
250 260
....*....|....*....|...
gi 529002597 711 HILFLEGGTIIEAGTHQQLMTNE 733
Cdd:COG4604 205 HIVAMKDGRVVAQGTPEEIITPE 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-732 |
5.91e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.90 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 496 SLTLRGSVQFQDVSFAYPNRPdvpvlqgltftlrpgeVTALVGPNGSGKSTVAALLQNLYQPTEG-----QVLLDGEPLP 570
Cdd:PRK14271 28 TLGFAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 571 KYEHRY-LHRQVAAVGQEPLLFGRSFKENIAYGLVQEPTMEEITAAAVesgAHGFISE--LSEGYDTEVGEAGSQLSGGQ 647
Cdd:PRK14271 92 NYRDVLeFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGV---AQARLTEvgLWDAVKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERgsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTH 726
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPT 246
|
....*.
gi 529002597 727 QQLMTN 732
Cdd:PRK14271 247 EQLFSS 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
503-729 |
1.59e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQVLLDGEPLPKYEHRYLHR 579
Cdd:PRK09473 15 VKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 ----QVAAVGQEPLlfgRSFKeniAYGLVQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQL-------SGGQR 648
Cdd:PRK09473 94 lraeQISMIFQDPM---TSLN---PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyphefSGGMR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQ 727
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNAR 247
|
..
gi 529002597 728 QL 729
Cdd:PRK09473 248 DV 249
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
191-454 |
2.13e-14 |
|
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: 74.50 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGEMAIPFFTGRLTDWIVQDE-TAAAFTQNVTLMSVLTIASAVLeFAADGIYNSTMG---------RVHSHL 260
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALL-NFLRIYLNHVAEqkvvadlrsDLYDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 261 QgevfqavlRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFL 340
Cdd:cd18778 84 Q--------RLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 341 LPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHE----MMVLNQKEALAYAVNVWTSS 416
Cdd:cd18778 156 GAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRyrkaQLRAMKLWAIFHPLMEFLTS 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 529002597 417 LsGMLLkvgILYFGGQLVTSGSVSSGRLVTFILYQIQF 454
Cdd:cd18778 236 L-GTVL---VLGFGGRLVLAGELTIGDLVAFLLYLGLF 269
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
497-733 |
2.43e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 497 LTLRGSVQFQDVSFAYPNRP--DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPK--- 571
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 572 --YEHRYLHRQVAAVGQEP--LLFGRSFKENIAYGLVQEPTMEEITAAAVESGAHgfISELSEGYdteVGEAGSQLSGGQ 647
Cdd:PRK13645 81 kiKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLK--LVQLPEDY---VKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQ----SLVERLlyeSPERGSRsVLFITQRLSSVEQ-ADHILFLEGGTIIE 722
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERL---NKEYKKR-IIMVTHNMDQVLRiADEVIVMHEGKVIS 231
|
250
....*....|.
gi 529002597 723 AGTHQQLMTNE 733
Cdd:PRK13645 232 IGSPFEIFSNQ 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-725 |
2.62e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 499 LRGSVQfqdvSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG-EPLPKyEHRYL 577
Cdd:COG4586 20 LKGALK----GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKR-RKEFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 hRQVAAV-GQE-------PLLfgRSFKENIA-YGLVQE---PTMEEITAaavesgahgfISELSEGYDTEVgeagSQLSG 645
Cdd:COG4586 95 -RRIGVVfGQRsqlwwdlPAI--DSFRLLKAiYRIPDAeykKRLDELVE----------LLDLGELLDTPV----RQLSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 646 GQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDG 237
|
.
gi 529002597 725 T 725
Cdd:COG4586 238 S 238
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
520-745 |
2.72e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTE-------GQVLLDGEPLPKYEHRYLHRQVAAVGQ--EPl 589
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 590 LFGRSFKENIAYGlvQEPTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSQLSGGQRQAVALARAL---------IRK 660
Cdd:PRK13547 95 AFAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 661 PRVLILDDATSALDANSQslvERLLyESPERGSRS----VLFITQRLS-SVEQADHILFLEGGTIIEAGTHQQLMTNE-- 733
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQ---HRLL-DTVRRLARDwnlgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLTPAhi 248
|
250
....*....|....*.
gi 529002597 734 ----GRYWAMVQAPGG 745
Cdd:PRK13547 249 arcyGFAVRLVDAGDG 264
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-725 |
3.37e-14 |
|
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: 75.99 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQVL----------------LDGEPLPKYEHRYLH 578
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQEPLLFgRSFKENIA------YGLVQEPT-MEEITAAAVESGAHGFIS-----ELSEGYDTE--VGEAGSQLS 644
Cdd:TIGR03269 92 EEVDFWNLSDKLR-RRIRKRIAimlqrtFALYGDDTvLDNVLEALEEIGYEGKEAvgravDLIEMVQLShrITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSvLFITQRLSSV--EQADHILFLEGGTIIE 722
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS-MVLTSHWPEVieDLSDKAIWLENGEIKE 249
|
...
gi 529002597 723 AGT 725
Cdd:TIGR03269 250 EGT 252
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
189-478 |
5.50e-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: 73.19 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFL--SCFGEMAIPFFTGRLTDWIVQDETAAafTQNVTLMSVLTIASAVLEFAADGIYN---STMG-RVHSHLQG 262
Cdd:cd18544 1 FILALLLLllATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTyllQKLGqRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 EVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRGLCLL----GLMLWASPSLTMITlvalplL 338
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVT----LIGDLLLLigilIAMFLLNWRLALIS------L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 339 FLLP----------EKMGKWYKvlaeQVQESLAK-SSQVAiEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALA 407
Cdd:cd18544 149 LVLPllllatylfrKKSRKAYR----EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 408 YAV--NVwTSSLSGMLLkVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGFSEKI 478
Cdd:cd18544 224 FALfrPL-VELLSSLAL-ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
517-724 |
1.09e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 71.52 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQVLLDGEPLPKYE--------------------- 573
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpderaraglflafqypeeipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 574 ---HRYLHRQVAAV----GQEPL---LFGRSFKENIAyglvqeptmeeiTAAAVESGAHGFiseLSEGYdtevgeagsql 643
Cdd:TIGR01978 92 vsnLEFLRSALNARrsarGEEPLdllDFEKLLKEKLA------------LLDMDEEFLNRS---VNEGF----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLL--YESPERGsrsVLFIT--QRLSSVEQADHILFLEGGT 719
Cdd:TIGR01978 146 SGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGInrLREPDRS---FLIIThyQRLLNYIKPDYVHVLLDGR 222
|
....*
gi 529002597 720 IIEAG 724
Cdd:TIGR01978 223 IVKSG 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
503-678 |
1.68e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVA 582
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AvgqePLLFGRSF-------KENIAyglvqePTMEEITAAAVesgahgfiselsegydteVGEAGSQLSGGQRQAVALAR 655
Cdd:PRK09544 82 L----PLTVNRFLrlrpgtkKEDIL------PALKRVQAGHL------------------IDAPMQKLSGGETQRVLLAR 133
|
170 180
....*....|....*....|...
gi 529002597 656 ALIRKPRVLILDDATSALDANSQ 678
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQ 156
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
520-722 |
2.52e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKY--EHRYLHR--QVAAVGQEPLLFGR-S 594
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLRakHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 FKENiayglVQEPTMeeiTAAAVESGAHGFISELSE--GYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK10584 105 ALEN-----VELPAL---LRGESSRQSRNGAKALLEqlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 529002597 673 LDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIE 722
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-740 |
2.58e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR--------YLHRQVAAVG-- 585
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaqlgigIIYQELSVIDel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 --QEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVesgahgFISELSEGYDTEVGEagsqLSGGQRQAVALARALIRKPR 662
Cdd:PRK09700 96 tvLENLYIGRhLTKKVCGVNIIDWREMRVRAAMML------LRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 663 VLILDDATSALdanSQSLVERL--LYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLmTNEGRYWAM 739
Cdd:PRK09700 166 VIIMDEPTSSL---TNKEVDYLflIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV-SNDDIVRLM 241
|
.
gi 529002597 740 V 740
Cdd:PRK09700 242 V 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
509-677 |
3.42e-13 |
|
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: 68.83 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 509 SFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL---YQPTEGQVLLDGEPLPKYEHRYlHRQVAAVG 585
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLlfgrsfkeNIAYGLVQEpTMEeitaAAVESGAHGFIselsegydtevgeagSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:cd03233 90 EEDV--------HFPTLTVRE-TLD----FALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVLC 141
|
170
....*....|..
gi 529002597 666 LDDATSALDANS 677
Cdd:cd03233 142 WDNSTRGLDSST 153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
530-722 |
3.63e-13 |
|
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: 67.40 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 530 PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVL-LDGEPLPKYEHRYLHrqvaavgqepllfgrsfkeniayglvqept 608
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 609 meeitaaavesgahgfiselsegyDTEVGEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLV-----ER 683
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLR 106
|
170 180 190
....*....|....*....|....*....|....*....
gi 529002597 684 LLYESPERGSRSVLFITQRLSSVeqADHILFLEGGTIIE 722
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEKDL--GPALLRRRFDRRIV 143
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
494-724 |
5.92e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.21 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 494 LASLTLRgsvqfqDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE---PLP 570
Cdd:PRK11000 1 MASVTLR------NVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 571 KYEhrylhRQVAAVGQEPLLFGR-SFKENIAYGLVQEPTMEEITAAAVESGAHgfISELSEGYDTEVGEagsqLSGGQRQ 649
Cdd:PRK11000 72 PAE-----RGVGMVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAE--VLQLAHLLDRKPKA----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 650 AVALARALIRKPRVLILDDATSALDA--NSQSLVE--RLlyesPERGSRSVLFITQ-RLSSVEQADHILFLEGGTIIEAG 724
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAalRVQMRIEisRL----HKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
503-724 |
6.49e-13 |
|
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: 71.76 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAY--PNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQ--VLLDGEPLPKYEHRYLH 578
Cdd:TIGR03269 280 IKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAA--VG---QEPLLFG-RSFKENIAYGLVQEPTMEEITAAAVesgahgfISELSEGYDTEVGEA-----GSQLSGGQ 647
Cdd:TIGR03269 360 RGRAKryIGilhQEYDLYPhRTVLDNLTEAIGLELPDELARMKAV-------ITLKMVGFDEEKAEEildkyPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAG 724
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIG 510
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
506-733 |
6.80e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGE-----PLpkyeHRYLHRQ 580
Cdd:PRK10895 7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 581 VAAVGQEPLLFGR-SFKENIAYGLV--QEPTMEEITAAAVESGAHGFISELSEGYdtevgeaGSQLSGGQRQAVALARAL 657
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 658 IRKPRVLILDDATSALDANSQSLVERLLYESPERG---------SRSVLFITQRLSSVEQadhilflegGTIIEAGTHQQ 728
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGlgvlitdhnVRETLAVCERAYIVSQ---------GHLIAHGTPTE 223
|
....*
gi 529002597 729 LMTNE 733
Cdd:PRK10895 224 ILQDE 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
501-718 |
1.74e-12 |
|
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: 66.88 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 501 GSVQFQDVSFAYP-NRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----EGQVLLDGEPLPKyeh 574
Cdd:cd03232 2 SVLTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 575 rYLHRQVAAVGQEPLLFGRSfkeniaygLVQEPTMeeitaaavesgahgfISELSEGydtevgeagsqLSGGQRQAVALA 654
Cdd:cd03232 76 -NFQRSTGYVEQQDVHSPNL--------TVREALR---------------FSALLRG-----------LSVEQRKRLTIG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 655 RALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVL-FITQRLSSV-EQADHILFLEGG 718
Cdd:cd03232 121 VELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSG-QAILcTIHQPSASIfEKFDRLLLLKRG 185
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
194-458 |
1.79e-12 |
|
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: 68.84 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 194 VFLSCFGEMAIPFFTGRLTDWIVQDETAAAFT-------QNVTLMSVLTIASAVLEFAADGIYNSTM----GRVHSHLQG 262
Cdd:cd18558 17 AFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAgpfekleEEMTLYAYYYLIIGAIVLITAYIQGSFWglaaGRQTKKIRY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 EVFQAVLRQETEFFQKNQTGEITSRVTDDTST-----------MSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMit 331
Cdd:cd18558 97 KFFHAIMRQEIGWFDVNDTGELNTRLADDVSKinegigdkigvIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGL-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 332 lvalpllfllpeKMGKWYKVLAEQV---QESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAY 408
Cdd:cd18558 175 ------------SAVVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 529002597 409 AVNVWTSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAV 458
Cdd:cd18558 243 NISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSA 292
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
517-711 |
1.95e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYlHRQVAAVGQE----PLLfg 592
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 rSFKENIAYGLVQEPTMEEITAAAVesgahgfISELSEGYDTEVGeagsQLSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PRK13540 90 -TLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 529002597 673 LDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQADH 711
Cdd:PRK13540 158 LDELSLLTIITKIQEHRAKGG-AVLLTSHQDLPLNKADY 195
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
527-732 |
2.24e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.78 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQP----TEGQVLLDGEPL----PKYEHRYLHRQVAAVGQEPL-------LF 591
Cdd:COG4170 29 TLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklsPRERRKIIGREIAMIFQEPSscldpsaKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 592 GRSFKENIAYGLVQEPTMEEITAAAVESGA---------HGFISElSEGYdtevgeagsQLSGGQRQAVALARALIRKPR 662
Cdd:COG4170 109 GDQLIEAIPSWTFKGKWWQRFKWRKKRAIEllhrvgikdHKDIMN-SYPH---------ELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 663 VLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTN 732
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
506-689 |
2.42e-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: 69.96 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPnrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLldgePLPKYEHRYLHrqvaavg 585
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR----PQPGIKVGYLP------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLL-FGRSFKENIAYGLVQEPTM----EEITAAAVE---------------------SGAHGFISELSEG-------- 631
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKDAldrfNEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLEIAmdalrcpp 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 529002597 632 YDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESP 689
Cdd:TIGR03719 155 WDADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
516-721 |
2.42e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL----PKyehrylHRQVAAVG---QEP 588
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngPK------SSQEAGIGiihQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 LLFGR-SFKENIAYGlvQEPT--MEEITAAAVESGAHGFISELSEGY--DTEVGEagsqLSGGQRQAVALARALIRKPRV 663
Cdd:PRK10762 89 NLIPQlTIAENIFLG--REFVnrFGRIDWKKMYAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 664 LILDDATSAL-DANSQSLVeRLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTII 721
Cdd:PRK10762 163 IIMDEPTDALtDTETESLF-RVIRELKSQG-RGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
516-721 |
5.91e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 516 PDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLP-KYEHRYLHRQVAAVGQE-PLLFGR 593
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAYG-------LVQEPTMEEITAAAVEsgahgfisELseGYDTEVGEAGSQLSGGQRQAVALARALIRKPRVLIL 666
Cdd:PRK10982 89 SVMDNMWLGryptkgmFVDQDKMYRDTKAIFD--------EL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 667 DDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQ-ADHILFLEGGTII 721
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGC-GIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
519-725 |
6.44e-12 |
|
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: 69.66 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--------------PKYEHRYLHRQVAav 584
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmcPQHNILFHHLTVA-- 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 gqEPLLFGRSFKeniayGLVQEPTMEEITAAAVESGAHgfiselsegydTEVGEAGSQLSGGQRQAVALARALIRKPRVL 664
Cdd:TIGR01257 1022 --EHILFYAQLK-----GRSWEEAQLEMEAMLEDTGLH-----------HKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 665 ILDDATSALDANSQSLVERLLYESpeRGSRSVLFITQRLSSVE-QADHILFLEGGTIIEAGT 725
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
189-450 |
7.24e-12 |
|
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: 66.70 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFaadgIYNS---TMG-RVHSHLQGEV 264
Cdd:cd18549 6 LDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNY----FVTYwghVMGaRIETDMRRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 265 FQAVLRQETEFFQKNQTGEITSRVTDDTSTMseslssdlslLLWY-------LIRGLCLLG---LMLWASPSLTMITLVA 334
Cdd:cd18549 82 FEHLQKLSFSFFDNNKTGQLMSRITNDLFDI----------SELAhhgpedlFISIITIIGsfiILLTINVPLTLIVFAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 335 ----LPLLFLLPEKMGKWYKvlaeQVQESLAK-SSQVAiEVLSAMPTVRSFANEEGEAQKFRQKlhemmvlNQ--KEALA 407
Cdd:cd18549 152 lplmIIFTIYFNKKMKKAFR----RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEG-------NDrfLESKK 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 529002597 408 YAVNVWTSSLSGM-----LLKVGILYFGGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18549 220 KAYKAMAYFFSGMnfftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
517-726 |
8.26e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQVLLDGEPLPKYE--------------------- 573
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedragegifmafqypveipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 574 ---HRYLHRQVAAV----GQEPL---LFGRSFKENIAygLVQEPtmEEITAAAVESGahgfiselsegydtevgeagsqL 643
Cdd:PRK09580 93 vsnQFFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIA--LLKMP--EDLLTRSVNVG----------------------F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 644 SGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLyESPERGSRSVLFIT--QRLSSVEQADHILFLEGGTII 721
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGV-NSLRDGKRSFIIVThyQRILDYIKPDYVHVLYQGRIV 225
|
....*
gi 529002597 722 EAGTH 726
Cdd:PRK09580 226 KSGDF 230
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
189-461 |
8.45e-12 |
|
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: 66.74 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVF--LSCFGEMAIPFFTGRLTDWIVQDETAAAftqnVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQ----G 262
Cdd:cd18543 1 LILALLAalLATLAGLAIPLLTRRAIDGPIAHGDRSA----LWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEhdlrT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 263 EVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLwYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLP 342
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 343 EKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAvnVWTSSLSG--M 420
Cdd:cd18543 156 RRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRA--RFWPLLEAlpE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 529002597 421 LLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVL 461
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
239-486 |
1.13e-11 |
|
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: 66.71 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 239 AVLEFAADGIYNSTMGRVHSHL----QGEVFQAVLRQETEFF--QKNQTGEITSRVTDDTStmseslssdlslllwyLIR 312
Cdd:cd18578 62 AIVAGIAYFLQGYLFGIAGERLtrrlRKLAFRAILRQDIAWFddPENSTGALTSRLSTDAS----------------DVR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 313 GLC--LLGLML-----------WA--------------SPSLTMITLVAlpllfllpekmGKWYKVLAEQVQESLAKSSQ 365
Cdd:cd18578 126 GLVgdRLGLILqaivtlvagliIAfvygwklalvglatVPLLLLAGYLR-----------MRLLSGFEEKNKKAYEESSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 366 VAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYFGGQLVTSGSVSSGR-L 444
Cdd:cd18578 195 IASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfF 274
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 529002597 445 VTFILyqIQFTI-AVEVLLSRYPRVQKAVGFSEKIFEYLDRVP 486
Cdd:cd18578 275 IVFMA--LIFGAqSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
485-685 |
1.38e-11 |
|
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: 67.65 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 485 VPNCPKSGSLAsltlrgsVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLL 564
Cdd:TIGR03719 312 IPPGPRLGDKV-------IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 565 dGEPLpkyehrylhrQVAAVGQ--EPLLFGRSFKENIAYGLvqeptmEEITAAAVESGAHGFISELS-EGYDTE--VGea 639
Cdd:TIGR03719 382 -GETV----------KLAYVDQsrDALDPNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQkkVG-- 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 529002597 640 gsQLSGGQRQAVALARALIRKPRVLILDDATSALDANS-QSLVERLL 685
Cdd:TIGR03719 443 --QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETlRALEEALL 487
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
503-733 |
1.39e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.56 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLH---R 579
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLLF-GRSFKENIAYGL-----VQEPTMEEITAAAVESgahgfiselsegydteVGEAG------SQLSGGQ 647
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLrehtqLPAPLLHSTVMMKLEA----------------VGLRGaaklmpSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTIIEAGTH 726
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSA 228
|
....*..
gi 529002597 727 QQLMTNE 733
Cdd:PRK11831 229 QALQANP 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
506-721 |
2.59e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSfaYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQ-VAAV 584
Cdd:COG3845 261 ENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEPLLFG----RSFKENIAYGLVQEPTMeeitaaavesGAHGFIS---------ELSEGYD---TEVGEAGSQLSGGQR 648
Cdd:COG3845 339 PEDRLGRGlvpdMSVAENLILGRYRRPPF----------SRGGFLDrkairafaeELIEEFDvrtPGPDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSV-EQADHILFLEGGTII 721
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGA-AVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
527-683 |
2.72e-11 |
|
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: 64.35 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL--------PKYEHR---YLHRQVAAVGQEPllfgrSF 595
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikADYEGTvrdLLSSITKDFYTHP-----YF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 596 KENIAYGLVQEPTMeeitaaavesgahgfiselsegyDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDA 675
Cdd:cd03237 96 KTEIAKPLQIEQIL-----------------------DREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
....*...
gi 529002597 676 NSQSLVER 683
Cdd:cd03237 149 EQRLMASK 156
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
520-730 |
2.87e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT--EGQVLLDGEPLPKYehryLHRQVAAVGQEPLLFGR-SFK 596
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQ----ILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIAY-GLVQEPtmEEITAAAVESGAHGFISEL--SEGYDTEVGEAGSQ-LSGGQRQAVALARALIRKPRVLILDDATSA 672
Cdd:PLN03211 159 ETLVFcSLLRLP--KSLTKQEKILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 673 LDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQA-DHILFLEGGTIIEAGTHQQLM 730
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
520-733 |
2.89e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV---LLDGEPLPKYEH---------------------R 575
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 576 YLHRQVAAVGQ--EPLLFGRSFKENIAYGlvqePTMEEITAAAVESGAHGFIS--ELSEGYdteVGEAGSQLSGGQRQAV 651
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY---LQRSPFELSGGQKRRV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTIIEAG-THQQL 729
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDIL 253
|
....
gi 529002597 730 MTNE 733
Cdd:PRK13651 254 SDNK 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
521-729 |
4.90e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLL---DGEPLPKY-----EHRYLHR-QVAAVGQEP--- 588
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYalseaERRRLLRtEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 589 LLFGRSFKENIAyglvqEPTMeeitaaAVESGAHGFISELSEGYDTEVGEAGSQL-------SGGQRQAVALARALIRKP 661
Cdd:PRK11701 102 LRMQVSAGGNIG-----ERLM------AVGARHYGDIRATAGDWLERVEIDAARIddlpttfSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 662 RVLILDDATSALDANSQS----LVERLLYESpergSRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG-THQQL 729
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQArlldLLRGLVREL----GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGlTDQVL 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
503-733 |
5.58e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNrpdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYE-HRYLHRQV 581
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 582 AAVGQEPLLFGR-SFKENIAYG-LVQEPTMEEITAAAVesgaHGFISELsegYDTEVGEAGSqLSGGQRQAVALARALIR 659
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGgFFAERDQFQERIKWV----YELFPRL---HERRIQRAGT-MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 660 KPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQLMTNE 733
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
189-454 |
6.80e-11 |
|
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: 64.03 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFaadgIYNSTMGRV------------ 256
Cdd:cd18545 4 LALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASR----LRIYLMAKVgqrilydlrqdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 257 HSHLQGEVFQavlrqeteFFQKNQTGEITSRVTDDTSTMSESlssdlslllwyLIRGL-----------CLLGLMLWASP 325
Cdd:cd18545 80 FSHLQKLSFS--------FFDSRPVGKILSRVINDVNSLSDL-----------LSNGLinlipdlltlvGIVIIMFSLNV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 326 SLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAK-SSQVAiEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKe 404
Cdd:cd18545 141 RLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 405 alAYAVN--VW-TSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQF 454
Cdd:cd18545 219 --AVRLNalFWpLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRF 269
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
233-450 |
6.95e-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: 64.07 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 233 VLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIR 312
Cdd:cd18564 62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 313 GLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQ 392
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 393 KLHEMMvlnqKEAL-AYAVNVWTSSLSGMLLKVG---ILYFGGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18564 222 ENRKSL----RAGLrAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
514-733 |
7.80e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 514 NRPDVPVLQ----------GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR-------- 575
Cdd:PRK15439 262 QAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 576 YL--HRQVAAVGQE-PLLFGRSFKENIAYGLVQEPTMEeitaAAVESGAHGFISELSEGYDTEVGeagsQLSGGQRQAVA 652
Cdd:PRK15439 342 YLpeDRQSSGLYLDaPLAWNVCALTHNRRGFWIKPARE----NAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 653 LARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMT 731
Cdd:PRK15439 414 IAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNV-AVLFISSDLEEIEQmADRVLVMHQGEISGALTGAAINV 492
|
..
gi 529002597 732 NE 733
Cdd:PRK15439 493 DT 494
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
521-733 |
1.13e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLhrqVAAVGQE-------PLL--- 590
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 ---FGRSFKeniaYGLVQEPTME--EITAAAVESgahgfiSELSEGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLI 665
Cdd:PRK15056 100 vvmMGRYGH----MGWLRRAKKRdrQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEgGTIIEAGTHQQLMTNE 733
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSVtEFCDYTVMVK-GTVLASGPTETTFTAE 232
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
190-447 |
3.61e-10 |
|
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: 61.75 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVFLSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18588 8 LLASLFLQLFA-LVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRV----------TDDTSTMSESlssdlslllwyLIRGLCLLGLMLWASPSLTMITLVALPLLF 339
Cdd:cd18588 87 RLPLSYFESRQVGDTVARVrelesirqflTGSALTLVLD-----------LVFSVVFLAVMFYYSPTLTLIVLASLPLYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 340 LLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALayaVNVWTSSLSG 419
Cdd:cd18588 156 LLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTAN---LSNLASQIVQ 232
|
250 260 270
....*....|....*....|....*....|.
gi 529002597 420 MLLK---VGILYFGGQLVTSGSVSSGRLVTF 447
Cdd:cd18588 233 LIQKlttLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
189-458 |
3.66e-10 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 61.65 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAAdGIYNST----MGRvhsHLQGEV 264
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILA-GYFAAKasqgFGR---DLRKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 265 FQAVLRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLllwyLIRG--LCLLG--LMLWASPSLTMITLVALpllfl 340
Cdd:cd18548 79 FEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRM----LVRApiMLIGAiiMAFRINPKLALILLVAI----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 341 lP----------EKMGKWYKvlaeQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKealayaV 410
Cdd:cd18548 150 -PilalvvflimKKAIPLFK----KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLK------A 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 529002597 411 NVWTSSLSGM------LLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAV 458
Cdd:cd18548 219 GRLMALLNPLmmlimnLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSL 272
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
519-702 |
3.88e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY--QPTEGQVLLDGEPLPkyehrylhRQVAAVgqEPLLFGRSFK 596
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLI--DAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIayglvqeptmeEITAAAVESGAHGFISELSEgydtevgeagsqLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:COG2401 114 DAV-----------ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 529002597 677 SQSLVERLLYESPERGSRSVLFITQR 702
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVATHH 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-720 |
4.14e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPkyehryLHRQVAAV-----------GQEPLLFGR 593
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIA---------YGLVQEPTMEEITAAAvesgahgFISELS---EGYDTEVGeagsQLSGGQRQAVALARALIRKP 661
Cdd:PRK11288 347 SVADNINisarrhhlrAGCLINNRWEAENADR-------FIRSLNiktPSREQLIM----NLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 662 RVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTI 720
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
521-729 |
4.80e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLyqptegQVLLDGEPLPKYEHRYLHRQVAAVGQepllFGRSFKENIA 600
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHL------SGLITGDKSAGSHIELLGRTVQREGR----LARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 601 --------YGLVQEPT-MEEITAAAVESGAH-----GFISELSEGYD----TEVGEAG------SQLSGGQRQAVALARA 656
Cdd:PRK09984 87 ntgyifqqFNLVNRLSvLENVLIGALGSTPFwrtcfSWFTREQKQRAlqalTRVGMVHfahqrvSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLLYE-SPERGSRSVLFITQRLSSVEQADHILFLEGGTIIEAGTHQQL 729
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
642-725 |
4.98e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 642 QLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSV-EQADHILFLEGGTI 720
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*
gi 529002597 721 IEAGT 725
Cdd:PRK11022 233 VETGK 237
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
189-485 |
5.69e-10 |
|
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: 60.94 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVfLSCFGeMAIPFFTgrltDWIVqDETAAafTQNVTLMSVLTIA-------SAVLEFAAD--GIYNSTmgRVHSH 259
Cdd:cd18567 8 LLLSLA-LELFA-LASPLYL----QLVI-DEVIV--SGDRDLLTVLAIGfglllllQALLSALRSwlVLYLST--SLNLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 260 LQGEVFQAVLRQETEFFQKNQTGEITSR----------VTDDTSTMseslssdlslllwyLIRGL---CLLGLMLWASPS 326
Cdd:cd18567 77 WTSNLFRHLLRLPLSYFEKRHLGDIVSRfgsldeiqqtLTTGFVEA--------------LLDGLmaiLTLVMMFLYSPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 327 LTMITLVALPLLFLLpeKMGkWYKVLAEQVQESL---AKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEmmVLNQK 403
Cdd:cd18567 143 LALIVLAAVALYALL--RLA-LYPPLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVD--AINAD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 404 EALAYaVNVWTSSLSGMLL---KVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTiavevllsryprvQKAVGFSEKIFE 480
Cdd:cd18567 218 IRLQR-LQILFSAANGLLFgleNILVIYLGALLVLDGEFTVGMLFAFLAYKDQFS-------------SRASSLIDKLFE 283
|
330
....*....|.
gi 529002597 481 Y------LDRV 485
Cdd:cd18567 284 LrmlrlhLERL 294
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
515-685 |
7.39e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 515 RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylhRQVAAVGQEPLLfgrs 594
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 595 fKENIAyglvqepTMEEITAAaveSGAHGFISELSEGYD-TEVGEAG------SQLSGGQRQAVALARALIRKPRVLILD 667
Cdd:PRK13543 94 -KADLS-------TLENLHFL---CGLHGRRAKQMPGSAlAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170
....*....|....*...
gi 529002597 668 DATSALDANSQSLVERLL 685
Cdd:PRK13543 163 EPYANLDLEGITLVNRMI 180
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
519-730 |
8.26e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 519 PVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL-PKYEHRYLHRQVAAVGQEP----LLFGR 593
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRkrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 SFKENIAyglvqeptmeeITAAAVESGAHGFISELSE----------------GYDTEVGEagsqLSGGQRQAVALARAL 657
Cdd:PRK10762 346 SVKENMS-----------LTALRYFSRAGGSLKHADEqqavsdfirlfniktpSMEQAIGL----LSGGNQQKVAIARGL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 658 IRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTI-----IEAGTHQQLM 730
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
529-704 |
1.27e-09 |
|
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: 59.69 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 529 RPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQvlLDGEP-------------LPKYEHRYLHRQVAAVgQEPL---LFG 592
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgseLQNYFTKLLEGDVKVI-VKPQyvdLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 RSFKENIayglvqeptmEEITAAAVESGAHGFIS---ELSEGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDA 669
Cdd:cd03236 101 KAVKGKV----------GELLKKKDERGKLDELVdqlELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*
gi 529002597 670 TSALDANSQSLVERLLYESPERGsRSVLFITQRLS 704
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDD-NYVLVVEHDLA 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
427-717 |
1.42e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 427 LYFGGQLVTSGSVSSGRLVTFILYQIQ---FTIAVEVLLSRYPRVQK------AVGFSEKIFEYLDRVPNCPKSGSLASL 497
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLMLAGRDMTRlagFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIVEYQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 498 TLRgsVQFQDVSFAYPNRpDVpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQVLLDGEPlpkyehryl 577
Cdd:TIGR00954 449 DNG--IKFENIPLVTPNG-DV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAK--------- 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 578 hRQVAAVGQEPLLFGRSFKENIAYGL---------VQEPTMEEItaaaVESGAHGFISELSEGYDTeVGEAGSQLSGGQR 648
Cdd:TIGR00954 515 -GKLFYVPQRPYMTLGTLRDQIIYPDssedmkrrgLSDKDLEQI----LDNVQLTHILEREGGWSA-VQDWMDVLSGGEK 588
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 649 QAVALARALIRKPRVLILDDATSALDANsqslVERLLYESPERGSRSVLFITQRLSSVEQADHILFLEG 717
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
506-689 |
1.51e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPnrPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLldgePLPKYEHRYLHrqvaavg 585
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR----PAPGIKVGYLP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEPLL-FGRSFKENIAYGlVQEPT-----MEEITAAAVE---------------------SGAHGFISELSEG------- 631
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEG-VAEVKaaldrFNEIYAAYAEpdadfdalaaeqgelqeiidaADAWDLDSQLEIAmdalrcp 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 632 -YDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESP 689
Cdd:PRK11819 156 pWDAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP 210
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
275-450 |
1.53e-09 |
|
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: 59.74 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 275 FFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWYKVLAE 354
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 355 QVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQK----EALAYA-VNVWTSslSGMLLKVGilyF 429
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKhtrwNAKTFSaVNTITD--LAPLLVIG---F 250
|
170 180
....*....|....*....|.
gi 529002597 430 GGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18554 251 AAYLVIEGNLTVGTLVAFVGY 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
520-724 |
1.73e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPTEGQVLLDGEPLpkyehrylhrqvaaVGQEPLlfGRSFKENI 599
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRL--------------VNGRPL--DSSFQRSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYGLVQEPTMEEIT-------AAAVESGAHGFISE-------------LSEGYDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:TIGR00956 839 GYVQQQDLHLPTSTvreslrfSAYLRQPKSVSKSEkmeyveeviklleMESYADAVVGVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 660 KPRVLI-LDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV--EQADHILFLE-GGTIIEAG 724
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHG-QAILCTIHQPSAIlfEEFDRLLLLQkGGQTVYFG 986
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-683 |
1.42e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVlldgeplpkyehrylhrqvaavgqepllfgrSFKENIAY----- 601
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------------------------DPELKISYkpqyi 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 602 GLVQEPTMEEITAAAVES-GAHGFISELSEG------YDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PRK13409 410 KPDYDGTVEDLLRSITDDlGSSYYKSEIIKPlqlerlLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
....*....
gi 529002597 675 ANSQSLVER 683
Cdd:PRK13409 486 VEQRLAVAK 494
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
506-730 |
1.49e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTEGQVLLDGEPL--------------- 569
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnpaqairagiam 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 570 -PKYEHRYLHRQVAAVGQepllfgrsfkeNIAYGLVQE-PTMEEITAAAVESGAHGFISELSEGYDTEVGEAGSqLSGGQ 647
Cdd:TIGR02633 341 vPEDRKRHGIVPILGVGK-----------NITLSVLKSfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 648 RQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSrSVLFITQRLSSV-EQADHILF-----LEGGTII 721
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGV-AIIVVSSELAEVlGLSDRVLVigegkLKGDFVN 487
|
....*....
gi 529002597 722 EAGTHQQLM 730
Cdd:TIGR02633 488 HALTQEQVL 496
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
190-447 |
1.57e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 56.83 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 190 ILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVL 269
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 270 RQETEFFQKNQTGEITSRVtDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLLPEKMGKWY 349
Cdd:cd18782 87 RLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 350 KVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGMLLKVGILYF 429
Cdd:cd18782 166 RRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWV 245
|
250
....*....|....*...
gi 529002597 430 GGQLVTSGSVSSGRLVTF 447
Cdd:cd18782 246 GAYLVLRGELTLGQLIAF 263
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
503-685 |
1.78e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPNRPdvPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLldgeplpkyehRYLHRQVA 582
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQE----------PLLF-GRSFkeniayglvqePTMEEITAAAvESGAHGFISELSEgydtevgEAGSQLSGGQRQAV 651
Cdd:PLN03073 576 VFSQHhvdgldlssnPLLYmMRCF-----------PGVPEQKLRA-HLGSFGVTGNLAL-------QPMYTLSGGQKSRV 636
|
170 180 190
....*....|....*....|....*....|....*
gi 529002597 652 ALARALIRKPRVLILDDATSALDANS-QSLVERLL 685
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV 671
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
521-724 |
2.72e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEplpkyehrylhrqVAAVGQEPLLFGR-SFKENI 599
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQlTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 600 AYGLV----QEPTMEEITAAAVEsgahgfISELSEGYDTEVgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDa 675
Cdd:PRK13546 107 EFKMLcmgfKRKEIKAMTPKIIE------FSELGEFIYQPV----KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 676 nsQSLVERLL---YESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:PRK13546 176 --QTFAQKCLdkiYEFKEQN-KTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYG 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
533-724 |
2.81e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 533 VTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHR-YL---HRQVAAVGQEPLLFGR-SFKENIAYGLVqeP 607
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGMA--K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 608 TMEEITAAAVESGAhgfISELSEGYDtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDA-NSQSLVERLly 686
Cdd:PRK11144 104 SMVAQFDKIVALLG---IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLpRKRELLPYL-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 529002597 687 espERGSRSV----LFITQRLSSVEQ-ADHILFLEGGTIIEAG 724
Cdd:PRK11144 172 ---ERLAREInipiLYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
517-674 |
3.67e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQnlyqpteGQVLLD------------------------------- 565
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdgriiyeqdlivarlqqdpprnvegtvydfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 566 -------GEPLPKYeHRYLHRqvaaVGQEPLlfgrsfKENIA-YGLVQEpTMEEITAAAVESGAHGFISELSEGYDTEVg 637
Cdd:PRK11147 88 aegieeqAEYLKRY-HDISHL----VETDPS------EKNLNeLAKLQE-QLDHHNLWQLENRINEVLAQLGLDPDAAL- 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 529002597 638 eagSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PRK11147 155 ---SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-685 |
3.73e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVllDGEPLPKYEHRYLhrqvaavgqepllfgrsfkENIAYGLVQE 606
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYI-------------------SPDYDGTVEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 607 pTMEEITAAAVESGAhgFISELSEG------YDTEVGEagsqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSL 680
Cdd:COG1245 421 -FLRSANTDDFGSSY--YKTEIIKPlgleklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 493
|
....*
gi 529002597 681 VERLL 685
Cdd:COG1245 494 VAKAI 498
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
461-731 |
4.99e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 461 LLSRYPRVQKAVGfsEKIFEyldrVPNcpksgslasltlrgsvqfqdVSFAYPNRPDVPVLQGLTFTLRPGEVTALVGPN 540
Cdd:PRK13549 244 LTALYPREPHTIG--EVILE----VRN--------------------LTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 541 GSGKSTVAALLQNLYQ-PTEGQVLLDGEPLP-KYEHRYLHRQVAAV-------GQEPLLfgrSFKENIAYG-LVQEPTME 610
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAIAQGIAMVpedrkrdGIVPVM---GVGKNITLAaLDRFTGGS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 611 EITAAAVESGAHGFISELSEGYDTEVGEAGSqLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPE 690
Cdd:PRK13549 375 RIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 529002597 691 RGSrSVLFITQRLSSV-EQADHILF-----LEGGTIIEAGTHQQLMT 731
Cdd:PRK13549 454 QGV-AIIVISSELPEVlGLSDRVLVmhegkLKGDLINHNLTQEQVME 499
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
517-567 |
5.03e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 5.03e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTEGQVLLDGE 567
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE 71
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
469-685 |
6.06e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 469 QKAVGFSEkIFeyldrVPNCPKSGSLAsltlrgsVQFQDVSFAYPNRpdvpVL-QGLTFTLRPGEVTALVGPNGSGKSTV 547
Cdd:PRK11819 304 QKRNETNE-IF-----IPPGPRLGDKV-------IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 548 AALLQNLYQPTEGQVLLdGEPLpkyehrylhrQVAAVGQ--EPLLFGRSFKENIAYGLvqeptmEEITAAAVES------ 619
Cdd:PRK11819 367 FKMITGQEQPDSGTIKI-GETV----------KLAYVDQsrDALDPNKTVWEEISGGL------DIIKVGNREIpsrayv 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 620 GAHGFiselsEGYDTE--VGeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANS-QSLVERLL 685
Cdd:PRK11819 430 GRFNF-----KGGDQQkkVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETlRALEEALL 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
526-730 |
7.90e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQ--------VLLDGEPLPKY-EHRYLHRQVAAVGQEPLLFGRSFK 596
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 597 ENIAYGlVQEPTMEEITAAAVesgahGFISELSEGYdtevgeagSQLSGGQRQAVALARALIRKPRVLILDDATSALDAN 676
Cdd:PRK10938 104 EIIQDE-VKDPARCEQLAQQF-----GITALLDRRF--------KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 529002597 677 SQSLVERLLYESPERGSRSVLfITQRLSSV-EQADHILFLEGGTIIEAGTHQQLM 730
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVL-VLNRFDEIpDFVQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
187-448 |
8.07e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.49 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 187 VQFILALVFLSCFGeMAIPFFTgrltdWIVQDETAAAftQNVTLMSVLTIASAVLefaadGIYNSTMGRVHSHLQ----- 261
Cdd:cd18568 5 AEILLASLLLQLLG-LALPLFT-----QIILDRVLVH--KNISLLNLILIGLLIV-----GIFQILLSAVRQYLLdyfan 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 262 -------GEVFQAVLRQETEFFQKNQTGEITSRV----------TDDTSTMSESlssdlslllwyLIRGLCLLGLMLWAS 324
Cdd:cd18568 72 ridlsllSDFYKHLLSLPLSFFASRKVGDIITRFqenqkirrflTRSALTTILD-----------LLMVFIYLGLMFYYN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 325 PSLTMITLVALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEegeaQKFRQKLHEMMVLN--- 401
Cdd:cd18568 141 LQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENKFAKAlnt 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 529002597 402 --QKEALAYAVNVwTSSLSGMLLKVGILYFGGQLVTSGSVSSGRLVTFI 448
Cdd:cd18568 217 rfRGQKLSIVLQL-ISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFN 264
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
517-734 |
1.64e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTvAALLQNLYQPTEGQvlldgEPLPKY----EHRYLHRQVAAvgQEPLLFG 592
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR-----RPWRF*twcaNRRALRRTIG*--HRPVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 593 R----SFKENI-AYGLVQEPTMEEITAAAvesgahgfiSELSEGYD-TEV-GEAGSQLSGGQRQAVALARALIRKPRVLI 665
Cdd:NF000106 97 RresfSGRENLyMIGR*LDLSRKDARARA---------DELLERFSlTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 666 LDDATSALDANSQSLVERLLyESPERGSRSVLFITQRLSSVEQADHIL-FLEGGTIIEAGTHQQLMTNEG 734
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVIDRGRVIADGKVDELKTKVG 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
520-725 |
1.77e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlyQPT----EGQVLLDGEP--------LPKY-EHRYLHRQVAAVgQ 586
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPkkqetfarISGYcEQNDIHSPQVTV-R 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 587 EPLLFGRSFKeniaygLVQEPTMEEiTAAAVESGAHgfISELSEGYDTEVGEAG-SQLSGGQRQAVALARALIRKPRVLI 665
Cdd:PLN03140 972 ESLIYSAFLR------LPKEVSKEE-KMMFVDEVME--LVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529002597 666 LDDATSALDANSQSLVERLLYESPERGSRSVLFITQ-RLSSVEQADHILFLE-GGTIIEAGT 725
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpSIDIFEAFDELLLMKrGGQVIYSGP 1104
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
189-485 |
2.19e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 53.28 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALvFLSCFGeMAIPFFTGRLTDWIVQdetaaafTQNVTLMSVLTIASAVLeFAADGIYNSTMGRV--------HSHL 260
Cdd:cd18555 8 LLLSL-LLQLLT-LLIPILTQYVIDNVIV-------PGNLNLLNVLGIGILIL-FLLYGLFSFLRGYIiiklqtklDKSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 261 QGEVFQAVLRQETEFFQKNQTGEITSRVTDDTstmseslssdlslllwyLIRGL-----------CLL-----GLMLWAS 324
Cdd:cd18555 78 MSDFFEHLLKLPYSFFENRSSGDLLFRANSNV-----------------YIRQIlsnqvisliidLLLlviylIYMLYYS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 325 PSLTMITLVALPLlfllpekMGKW----YKVLAEQVQESLAKSSQVA---IEVLSAMPTVRSFANEEGEAQKFRQKLHEM 397
Cdd:cd18555 141 PLLTLIVLLLGLL-------IVLLllltRKKIKKLNQEEIVAQTKVQsylTETLYGIETIKSLGSEKNIYKKWENLFKKQ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 398 MVLNQKEALAYA-VNVWTSSLSgMLLKVGILYFGGQLVTSGSVSSGRLVTFILYQIQFTIAVEVLLSRYPRVQKAVGfse 476
Cdd:cd18555 214 LKAFKKKERLSNiLNSISSSIQ-FIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKS--- 289
|
....*....
gi 529002597 477 kifeYLDRV 485
Cdd:cd18555 290 ----YLERL 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
508-731 |
2.28e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 508 VSFAYPNRPdVPVLQGLTFTLRPGEVTALVGPNGSGKSTVA----ALLQNLYQPTEGQVLLDGEPL----PKYEHRYLHR 579
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 580 QVAAVGQEPLL-------FGRSFKENIA-----------YGLVQEPTMEEITAAAVE---SGAHGFISELSEGydtevge 638
Cdd:PRK15093 90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKdhkDAMRSFPYELTEG------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 639 agsqlsggQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLFITQRLSSVEQ-ADHILFLEG 717
Cdd:PRK15093 163 --------ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYC 234
|
250
....*....|....
gi 529002597 718 GTIIEAGTHQQLMT 731
Cdd:PRK15093 235 GQTVETAPSKELVT 248
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
506-685 |
6.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDgeplPKYEHRYLHRQVAAVG 585
Cdd:PRK11147 323 ENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 586 QEpllfgRSFKENIAYGlvqeptMEEITAAAVESGAHGFISelsegyD---------TEVgeagSQLSGGQRQAVALARA 656
Cdd:PRK11147 396 PE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQ------DflfhpkramTPV----KALSGGERNRLLLARL 454
|
170 180
....*....|....*....|....*....
gi 529002597 657 LIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLELLEELL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
517-711 |
1.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 517 DVPVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQnlyqptegqvLLDGEplpkyehrylHRQvaAVGQEPLLFGR--- 593
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKST---LLS----------LITGD----------HPQ--GYSNDLTLFGRrrg 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 594 ------SFKENIAYgLVQEPTMEEITAAAVE----SGAH---GFISELSE-------------GYDTEVGEAGSQ-LSGG 646
Cdd:PRK10938 327 sgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFdsiGIYQAVSDrqqklaqqwldilGIDKRTADAPFHsLSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 647 QRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGSRSVLF-----------ITQRLSSVEQADH 711
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFvshhaedapacITHRLEFVPDGDI 481
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
205-455 |
2.44e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 50.26 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 205 PFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLRQETEFFQKNQTGEI 284
Cdd:cd18565 34 ASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 285 TSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFLlpekMGKWYKVLAE----QVQESL 360
Cdd:cd18565 114 MSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIA----GTYWFQRRIEpryrAVREAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 361 AK-SSQVAiEVLSAMPTVRSFANEEGEAQKFR---QKLHEMMVLNQKEALAYAVNVWTSSLSGMLLkvgILYFGGQLVTS 436
Cdd:cd18565 190 GDlNARLE-NNLSGIAVIKAFTAEDFERERVAdasEEYRDANWRAIRLRAAFFPVIRLVAGAGFVA---TFVVGGYWVLD 265
|
250 260
....*....|....*....|....*
gi 529002597 437 G------SVSSGRLVTFILYQIQFT 455
Cdd:cd18565 266 GpplftgTLTVGTLVTFLFYTQRLL 290
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
191-447 |
2.85e-06 |
|
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: 49.82 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 191 LALVFLSCFGeMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAVLR 270
Cdd:cd18783 9 IASLILHVLA-LAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 271 QETEFFQKNQTGEITSRVTD-----------------DTSTMseslssdlslllwylirgLCLLGLMLWASPSLTMITLV 333
Cdd:cd18783 88 LPIDFFERTPAGVLTKHMQQierirqfltgqlfgtllDATSL------------------LVFLPVLFFYSPTLALVVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 334 ALPLLFLLPEKMGKWYKVLAEQVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALayaVNVW 413
Cdd:cd18783 150 FSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNW 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 529002597 414 TSSLSG---MLLKVGILYFGGQLVTSGSVSSGRLVTF 447
Cdd:cd18783 227 PQTLTGpleKLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
521-736 |
2.89e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.66 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLHRQVAAVgqepllfgrsfkENIA 600
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 601 -----YGLVQEpTMEEITAAAVESGAHG-FISELSEGYdtevgeagsqlSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:PRK13545 108 lkglmMGLTKE-KIKEIIPEIIEFADIGkFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529002597 675 ansQSLVERLL---YESPERGsRSVLFITQRLSSVEQ-ADHILFLEGGTIIEAGTHQQLMTNEGRY 736
Cdd:PRK13545 176 ---QTFTKKCLdkmNEFKEQG-KTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
536-687 |
3.06e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 536 LVGPNGSGKSTVAALLQNLYQPTEGQVLLD-GEPLPK-------YE-HRYL------HRQVAAVGQEpllfgrsfKENIa 600
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKlrqdqfaFEeFTVLdtvimgHTELWEVKQE--------RDRI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 601 YGLvqePTMEE---ITAAAVEsgahgfiSELSE--GYDTEvGEAGSQLSG---------GQRQAVA--------LARALI 658
Cdd:PRK15064 103 YAL---PEMSEedgMKVADLE-------VKFAEmdGYTAE-ARAGELLLGvgipeeqhyGLMSEVApgwklrvlLAQALF 171
|
170 180
....*....|....*....|....*....
gi 529002597 659 RKPRVLILDDATSALDANSQSLVERLLYE 687
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLNE 200
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
189-450 |
3.19e-06 |
|
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: 49.41 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAV 268
Cdd:cd18546 3 LALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 269 LRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLlwyLIRGLCLLG---LMLWASPSLTMITLVALPLLFLlpekM 345
Cdd:cd18546 83 QRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQL---VVSLLTLVGiavVLLVLDPRLALVALAALPPLAL----A 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 346 GKWYKVLAE----QVQESLAKSSQVAIEVLSAMPTVRSFANEEGEAQKFRQKLHEMMVLNQKEALAYAVNVWTSSLSGML 421
Cdd:cd18546 156 TRWFRRRSSrayrRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNL 235
|
250 260
....*....|....*....|....*....
gi 529002597 422 LKVGILYFGGQLVTSGSVSSGRLVTFILY 450
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
506-742 |
3.83e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 506 QDVSFAYPN--RPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL-PKYEHRYLHRQVA 582
Cdd:PRK09700 262 HETVFEVRNvtSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQ---EPLLFGR-SFKENIA-------------YGLVQEpTMEEITAAAvesgAHGFISELSEGYDTEVGEagsqLSG 645
Cdd:PRK09700 342 YITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHE-VDEQRTAEN----QRELLALKCHSVNQNITE----LSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 646 GQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPERGsRSVLFITQRLSSV-EQADHILFLEGGTIIEAG 724
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIiTVCDRIAVFCEGRLTQIL 491
|
250
....*....|....*....
gi 529002597 725 THQQLMTNEG-RYWAMVQA 742
Cdd:PRK09700 492 TNRDDMSEEEiMAWALPQE 510
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
526-674 |
4.20e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPL-PK-YEHRylhRQVAAVGQEPLLFGR-SFKENIA-- 600
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGdIATR---RRVGYMSQAFSLYGElTVRQNLElh 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529002597 601 ---YGLvqePTmEEITAAavesgahgfISELSEGYD-TEVGEA-GSQLSGGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:NF033858 364 arlFHL---PA-AEIAAR---------VAEMLERFDlADVADAlPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
527-713 |
4.30e-06 |
|
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: 47.35 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAallqnlyqptegqvlldgeplpkyehrylhRQVAAVgqeplLFGRSFKENiAYGLVQE 606
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGAQSATR-RRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 607 PtmeeITAAAVESGAHGFISelsegydtevgeagsQLSGGQRQAVALARALI---RKPRVL-ILDDATSALDANSQSLVE 682
Cdd:cd03227 61 G----CIVAAVSAELIFTRL---------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|.
gi 529002597 683 RLLYESPERGSRsVLFITQRLSSVEQADHIL 713
Cdd:cd03227 122 EAILEHLVKGAQ-VIVITHLPELAELADKLI 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
513-674 |
5.32e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 513 PNRPDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLY-QPTEGQVLLDGEPLpkyehrylhrQVAAVGqepll 590
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYgRNISGTVFKDGKEV----------DVSTVS----- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 fgRSFKENIAY--------GLV-QEPTMEEITAAAVESGA-HGFISE-----LSEGY-----------DTEVGeagsQLS 644
Cdd:NF040905 333 --DAIDAGLAYvtedrkgyGLNlIDDIKRNITLANLGKVSrRGVIDEneeikVAEEYrkkmniktpsvFQKVG----NLS 406
|
170 180 190
....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALD 674
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
521-724 |
6.56e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.32 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 521 LQGLTFTLRPGEVTALVGPNGSGKSTVaaLLQNLYqpTEGQVLLDgEPLPKYEHrylhrqvaavgqEPLLFGRSFKENIA 600
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI-SFLPKFSR------------NKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 601 YGLvqeptmeeitaaavesgahgfiselseGYDTeVGEAGSQLSGGQRQAVALARALIR--KPRVLILDDATSALDansQ 678
Cdd:cd03238 74 VGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLH---Q 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 529002597 679 SLVERLLYESPERGSR--SVLFITQRLSSVEQADHILFL------EGGTIIEAG 724
Cdd:cd03238 123 QDINQLLEVIKGLIDLgnTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
527-674 |
1.20e-05 |
|
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: 48.63 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVllDGEP-----LPKYE----HRYLhRQVAA----VGQEPL---L 590
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYF-KKLANgeikVAHKPQyvdL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 591 FGRSFKeniayGlvqepTMEEITAAAVESGAHGFISE---LSEGYDTEVGEagsqLSGGQRQAVALARALIRKPRVLILD 667
Cdd:COG1245 172 IPKVFK-----G-----TVRELLEKVDERGKLDELAEklgLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 529002597 668 DATSALD 674
Cdd:COG1245 238 EPSSYLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
500-562 |
2.40e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 2.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529002597 500 RGSVQFQDVSFAYPNRPdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQV 562
Cdd:PRK15064 317 RNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
520-685 |
2.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDG---------------EPLPKY------EHRYLH 578
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYvidgdrEYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 579 RQVAAVGQE------PLLFGRsfkeniayglvqeptMEEITAAAVESGAHGFISELseGYDTE-VGEAGSQLSGGQRQAV 651
Cdd:PRK10636 96 AQLHDANERndghaiATIHGK---------------LDAIDAWTIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRL 158
|
170 180 190
....*....|....*....|....*....|....
gi 529002597 652 ALARALIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL 192
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
609-690 |
4.16e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 609 MEEITAAAVESGAHGFISELSEGYDTEVgEAGSQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYES 688
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW 390
|
..
gi 529002597 689 PE 690
Cdd:PLN03073 391 PK 392
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
527-684 |
6.32e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVllDGEP-----LPKYE----HRYLHRqvaavgqeplLFGRSFKe 597
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevLKRFRgtelQNYFKK----------LYNGEIK- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 598 niaygLVQEPTMEEITAAAVEsgahGFISELSEGYDtevgEAG-------------------SQLSGGQRQAVALARALI 658
Cdd:PRK13409 162 -----VVHKPQYVDLIPKVFK----GKVRELLKKVD----ERGkldevverlglenildrdiSELSGGELQRVAIAAALL 228
|
170 180
....*....|....*....|....*.
gi 529002597 659 RKPRVLILDDATSALDansqsLVERL 684
Cdd:PRK13409 229 RDADFYFFDEPTSYLD-----IRQRL 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
503-734 |
7.37e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 503 VQFQDVSFAYPnrpDVPVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRylhrqvA 582
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 583 AVGQE----PLLFGR------SFKENIA-----YGLVQ---EPTMEEITAAaveSGAHGFISELsegydtevgeAGsQLS 644
Cdd:NF033858 73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPFADRP----------AG-KLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 645 GGQRQAVALARALIRKPRVLILDDATSALD--ANSQ--SLVERLlyespeRGSR---SVLFITQRLSSVEQADHILFLEG 717
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwELIDRI------RAERpgmSVLVATAYMEEAERFDWLVAMDA 212
|
250
....*....|....*..
gi 529002597 718 GTIIEAGTHQQLMTNEG 734
Cdd:NF033858 213 GRVLATGTPAELLARTG 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
531-717 |
1.40e-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: 43.33 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 531 GEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGePLPKYEHRYLhrqvaavgqepllfgrsfkeniayglvqeptme 610
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI--------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 611 eitaaavesgahgfiselsegydtevgeagsQLSGGQRQAVALARALIRKPRVLILDDATSALDANSQSLVERLLYESPE 690
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*...
gi 529002597 691 RGSRSVLFITQRLSSVEQ-ADHILFLEG 717
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
637-729 |
2.54e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 637 GEAGSQLSGGQRQAVALARALIRK---PRVLILDDATSAL---DANS-----QSLVErllyesperGSRSVLFITQRLSS 705
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKllevlQRLVD---------KGNTVVVIEHNLDV 894
|
90 100 110
....*....|....*....|....*....|
gi 529002597 706 VEQADHILFL------EGGTIIEAGTHQQL 729
Cdd:TIGR00630 895 IKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
505-685 |
3.03e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 505 FQDVSFAYPNRpdvpVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQVLLDGEPLPKYEHRYLhrqvAAV 584
Cdd:PRK13541 4 LHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 585 GQEpllfgrsfkeniaYGLVQEPTMEE---------ITAAAVESGAHGFisELSEGYDTEVgeagSQLSGGQRQAVALAR 655
Cdd:PRK13541 76 GHN-------------LGLKLEMTVFEnlkfwseiyNSAETLYAAIHYF--KLHDLLDEKC----YSLSSGMQKIVAIAR 136
|
170 180 190
....*....|....*....|....*....|
gi 529002597 656 ALIRKPRVLILDDATSALDANSQSLVERLL 685
Cdd:PRK13541 137 LIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
522-551 |
1.35e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|....
gi 529002597 522 QGLTFTLRPGEVTALVGPNGSGKST----VAALL 551
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
189-413 |
1.41e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 41.34 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 189 FILALVFLSCFGEMAIPFFTGRLTDWIVQDETAAAFTQNVTLMSVLTIASAVLEFAADGIYNSTMGRVHSHLQGEVFQAV 268
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 269 LRQETEFFQKNQTGEITSRVTDDTSTMSESLSSDLSLLLWYLIRGLCLLGLMLWASPSLTMITLVALPLLFllpeKMGKW 348
Cdd:cd18580 83 LRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYY----LLQRY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529002597 349 YKVLAEQVQ--ESLAKS---SQVAiEVLSAMPTVRSFaneeGEAQKFRQKLHEMMVLNQK-EALAYAVNVW 413
Cdd:cd18580 159 YLRTSRQLRrlESESRSplySHFS-ETLSGLSTIRAF----GWQERFIEENLRLLDASQRaFYLLLAVQRW 224
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
526-547 |
5.71e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 5.71e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
631-736 |
6.47e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529002597 631 GYDTeVGEAGSQLSGGQRQAVALARALIRKP--RVL-ILDDATSAL---DansqslVERLLyespergsrSVLfitQRLs 704
Cdd:PRK00349 820 GYIK-LGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLhfeD------IRKLL---------EVL---HRL- 879
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 529002597 705 sVEQ----------------ADHILFL------EGGTIIEAGTHQQLMTNEGRY 736
Cdd:PRK00349 880 -VDKgntvvviehnldviktADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| |
